TR2022016538T3 - METHODS AND COMPOSITIONS FOR TREATMENT OF COMPLEMENT-RELATED DISORDERS - Google Patents

Abstract

The present disclosure relates, inter alia, to compositions comprising an inhibitor of human complement and to the use of the compositions in methods of treating or preventing complement-related disorders. In some embodiments, the inhibitor is administered to patients chronically. In some embodiments, the inhibitor is administered to a patient at a frequency and in an amount to maintain systemic complement inhibition and prevent progression. In some embodiments, the composition includes an antibody or antigen binding binding to a human complement component C5 protein or a fragment thereof, such as C5a or C5b.

Description

DESCRIPTION METHODS AND COMPOSITIONS FOR TREATMENT OF COMPLEMENT-RELATED DISORDERS Technical Field The field of the invention is medicine, immunology, molecular biology and protein chemistry. Background of the Invention The complement system acts in conjunction with other immunological systems of the body that defend against the intrusion of cellular and viral pathogens. There are at least 25 complement proteins that exist as a complex collection of plasma proteins and membrane cofactors. Plasma proteins constitute approximately 10% of the globulins in vertebrate serum. Complement components achieve their immune defense functions by interacting through a series of complex but sensitive enzymatic cleavage and membrane binding states. The resulting complement cascade leads to the production of products with opsonic, immunoregulatory and lytic functions. A brief summary of the biological activities associated with complement activation is provided, for example, in The Merck Manual, 16th Edition. The complement cascade can proceed through the classical pathway (CP), the lectin pathway, or the alternative pathway (AP). The lectin pathway is typically initiated by binding of mannose-binding lectin (MBL) to high-mannose substrates. AP can be antibody independent and initiated through specific molecules on pathogen surfaces. CP is typically initiated by antibody recognition of or binding to an antigenic site on a target cell. These pathways converge at CS convertase—where the complement component CS is cleaved by an active protease to provide C3a and C3b. AP CS convertase is initiated by the spontaneous hydrolysis of the complement component C3, which is abundant in blood plasma. This process, also known as an "autoactivation", occurs through spontaneous cleavage of a thioester at C3 to form C3i or C3(H2O). The autoactivation process is facilitated by the presence of surfaces (e.g., bacterial cell surfaces) that support the binding of activated C3 and/or have neutral or positive charge characteristics. This formation of C3(H20) allows the plasma protein Factor B to bind, thus allowing Factor D to split Factor B into Ba and Bb. The Bb fragment remains attached to O3 to form a complex containing CS(H2O)Bb - "liquid-phase" or "first" CS convertase. Although produced in only small amounts, liquid phase C3 convertase can cleave multiple CS proteins into C3a and CSb, resulting in the production and subsequent covalent attachment of C3b to a surface (e.g., a bacterial surface). Factor B bound to the surface-bound CSb is therefore cleaved by Factor D to form the surface-bound AP C3 convertase complex containing CSb,Bb. (See AP C5 convertase - (C3b)2,Bb - is the addition of a second C3b monomer to the AP CS convertase, which binds and exposes it for cleavage via Bb. (See, for example, Medicus et al. above. (1976) the trimeric protein is stabilized by the addition of properdin. However, properdin binding is not required to establish the functional alternative pathway CS or C5 convertase. (See, for example, Schreiber et al. ( Proc Natl Acad CP CS convertase is formed upon the interaction of an antibody bound to a target antigen (e.g., a microbial antigen) and the complement component C1, a complex of C1q, C1r, and C1s. Binding of the C1q portion of C1 to the antibody-antigen complex causes a conformational change in C1 that activates C1r. Active C1r then cleaves C1s associated with C1 to form an active serine protease. Active C1s cleaves the complement component C4 into C4b and C4a. The newly produced C4b fragment, like C3b, contains a highly reactive thiol that readily forms amide or ester bonds with appropriate molecules on a target surface (e.g., a microbial cell surface). C1s also cleaves the complement component C2 into C2b and C2a. The complex formed through C4b and C2a is the CP C3 convertase, which can process C3 into C3a and C3b. CP C5 convertase - C4b,C2a,C3b - is formed upon addition of a C3b monomer to CP C3 convertase. (See, for example, Müller-Eberhard (1988), supra and Cooper et al. (1970) J Exp Med 132:775-793. ) In addition to its role in C3 and C5 convertase, C3b also functions as an opsonin through interaction with complement receptors located on the surfaces of antigen-presenting cells such as macrophages and dendritic cells. The opsonic function of C3b is generally considered to be one of the most important anti-infective functions of the complement system. Patients with genetic lesions that block C3b function are more prone to infection from a wide variety of pathogenic organisms, whereas patients with lesions later in the complement cascade, i.e. patients with lesions that block C5 functions, are more prone to infection with Neisseria and only to some extent later. AP and CP C5 convertases, for which it is prone, cleave C5, the 190 kDa beta globulin found in normal human serum, at approximately 75 µg/ml. C5 has approximately one hundredth of the mass attributed to the carbohydrate. It is glycosylated with 5-3. Mature C5 is a heterodimer of a 999 amino acid 115 kDa alpha chain that is disulfide linked to a 655 amino acid 75 kDa beta chain. C5, a single-strand precursor protein product of a single-copy gene, predicts a secreted pro-C5 precursor whose sequence consists of 1658 amino acids with a leader sequence of 18 amino acids (see, e.g., U. S. Patent No. 6,355,245). The pro-C5 precursor consists of the beta chain as an amino terminal fragment (amino acid residues +1 to 655 of the above sequence) with four amino acids deleted between the two (amino acid residues 656 to 659 of the above sequence) and the carboxyl terminal fragment (amino acid residues of the above sequence 660 to 1658) is cleaved after amino acids 655 and 659 to provide the alpha chain. C5a is cleaved from the alpha chain of C5 by alternative or classical C5 convertase as an amino terminal fragment containing the first 74 amino acids of the alpha chain (i.e. amino acid residues 660-733 of the above sequence). Approximately 20 percent of the 11 kDa mass of C5a is attributed to carbohydrate. The cleavage site for the convertase action is at or immediately adjacent to amino acid residue 733 of the above sequence. A compound at or adjacent to this cleavage site has the potential to block access of C5 convertase enzymes to the cleavage site and thus act as a complement inhibitor. C5 can also be activated by means other than C5 convertase activity. Restricted can also cleave C5 and produce active C5b. Cleavage of C5 releases C5a, a potent anaphylatoxin and chemotactic factor, and leads to the formation of the lytic terminal complement complex, C5b-9. C5a and C5b-9 also have pleiotropic cell-activating properties by enhancing the release of downstream inflammatory factors such as hydrolytic enzymes, reactive oxygen species, arachidonic acid metabolites, and various cytokines. The first step in the formation of the terminal complement complex involves the combination of C6, C7, and C8 with C5b to form the C5b-8 complex on the target cell surface. Following the binding of the C5b-8 complex with a few C9 molecules, the membrane attack complex (MAC, C5b-9, terminal complement complex--TCC) is formed. When sufficient numbers of MACs enter target cell membranes, the openings forming MAC pores mediate rapid osmotic lysis of target cells. Lower nonlytic concentrations of MACs may produce other effects. In particular, membrane insertion of small numbers of C5b-9 complexes into endothelial cells and platelets may result in harmful cell activation. In some cases, activation may precede cell lysis. As mentioned above, C3a and C5a are anaphylatoxins. These activated complement components can trigger mast cell degranulation, which releases histamine from basophils and mast cells and other mediators of inflammation, resulting in smooth muscle contraction, increased grooming permeability, leukocyte activation, and other inflammatory phenomena including cellular proliferation resulting in hypercellularity. C5a also functions as a chemotactic peptide that functions to recruit pro-inflammatory granulocytes to the site of complement activation. C5a receptors are found on the surfaces of bronchial and alveolar epithelial cells and bronchial smooth muscle cells. C5a receptors have also been found on eosinophils, mast cells, monocytes, neutrophils and activated lymphocytes. While a properly functioning complement system provides a strong defense against infecting microbes, improper regulation or activation of complement, such as rheumatoid arthritis (RA); lupus nephritis; ischemia-reperfusion injury; atypical hemolytic uremic syndrome (aHUS); dense deposit disease (DDD); macular degeneration (e.g. age-related macular degeneration (AMD)); hemolysis, high liver enzymes and low platelets (HELLP) syndrome; thrombotic thrombocytopenic purpura (TTP); spontaneous fetal loss; Pauci-immune vasculitis; epidermolysis bullosa; recurrent fetal loss; multiple sclerosis (MS); traumatic brain injury; and in the pathogenesis of various disorders, including myocardial infarction, cardiopulmonary bypass, and damage from hemodialysis. Würzner and Zimmerhackl, 2006, in: Complement and Kidney Disease (pp. 149- Annu. Rev. Med. 59:293-309, all describe aHUS therapy strategies. Brief Description The present invention provides an antibody for use in treating atypical hemolytic uremic syndrome (aHUS) in a patient, wherein the antibody is eculizumab. The present invention is thus directed to the treatment of aHUS. Treatment of other complement-related disorders is not within the scope of the present invention. The present disclosure relates to compositions comprising an inhibitor of human complement (e.g., an inhibitor of complement component C5, such as an anti-C5 antibody) and methods for using the compositions to treat or prevent complement-related disorders. In some embodiments, the compositions include an antibody or antigen binding fragment thereof that binds to a human complement component C5 protein. In some embodiments, the compositions contain an antibody that binds to human C5 fragment C5a or C5b or an antigen binding fragment thereof. In some embodiments, the CS inhibitor is a small molecule or a nucleic acid, such as an siRNA or an anti-sense RNA, that binds to and promotes inactivation of CS mRNA in a mammal. Complement-related disorders include any medical disorder in a human being treated that may benefit directly or indirectly from inhibition of the complement system. Disorders are generally characterized by inappropriate regulation of the complement system, such as: (i) activation of the complement system or (ii) duration of an activated complement system in a subject. Complement-related disorders include, but are not limited to, inflammatory and autoimmune disorders. A complement-related disorder such as RA; antiphospholipid antibody syndrome (APS); lupus nephritis; ischemia-reperfusion injury; aHUS; typical (also diarrheal or infectious) hemolytic uremic syndrome (tHUS); DDD; neuromyelitis optica (NMO); multifocal motor neuropathy (MMN); MS; macular degeneration (eg, AMD); HELLP syndrome; TTP; spontaneous fetal loss; Pauci-immune vasculitis; epidermolysis bullosa; recurrent fetal loss; and traumatic brain injury may occur. Complement-related disorders, a cardiovascular disorder, myocarditis, a cerebrovascular disorder, a peripheral (e.g. musculoskeletal) vascular disorder, a renovascular disorder, a mesenteric/enteric vascular disorder, vasculitis, Henoch-Schönlein purpura nephritis, vasculitis associated with systemic lupus erythematosus, vasculitis associated with rheumatoid arthritis, immune complex vasculitis, Takayasu disease, dilated cardiomyopathy, diabetic angiopathy, Kawasaki disease (arthritis), venous gas embolus (VGE), and a complement such as restenosis following stent placement, rotational atherectomy, and percutaneous transluminal coronary angioplasty (PTCA). Includes vascular disorders associated with Additional complement-related disorders include, without limitation, myasthenia gravis (MG), cold agglutinin disease (CAD), dermatomyositis, paroxysmal cold hemoglobinuria (PCH), Graves' disease, atherosclerosis, Alzheimer's disease, systemic inflammatory response sepsis, septic shock, spinal cord injury, They include glomerulonephritis, Hashimoto's thyroiditis, type I diabetes, psoriasis, pemphigus, autoimmune hemolytic anemia (AIHA), idiopathic thrombocytopenic purpura (ITP), Goodpasture syndrome, Degos disease, and catastrophic APS (CAPS). The disclosure highlights a method of treating or preventing a complement-related disorder in a human. The method includes administering to a human in need thereof a therapeutically effective amount of a composition comprising an inhibitor of human complement (e.g., an inhibitor of the human complement component CS). The disclosure discloses a method of treating or preventing a complement-related disorder in a human, comprising administering to a human in need thereof a composition comprising a therapeutically effective amount of an inhibitor of human complement (e.g., an inhibitor of the human complement component CS). inhibitor). In some embodiments of any of the methods disclosed herein that are not within the scope of the foregoing, the inhibitor may inhibit the expression of a human complement component CS protein. The inhibitor may inhibit protein expression of a human complement component CS protein or may inhibit expression of an mRNA encoding the protein. In some embodiments of any of the methods disclosed herein, the inhibitor may inhibit the cleavage of the human complement component CS into CSa and CSb fragments. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments of any of the methods disclosed herein, the inhibitor binds to and inhibits one or both CSa and CSb. The inhibitor may, for example, be an antibody that binds to CSa or CSb. In some embodiments, the inhibitor is an antibody that binds to CSa, but not full-length 05. In some embodiments, the inhibitor is an antibody that binds to CSb but not full-length 05. In some embodiments, the inhibitor is an antibody that binds to a CSa protein or a fragment thereof having an amino acid sequence comprising or consisting of at least four (e.g., excess) consecutive amino acids as described in any of the following SEQ ID NOs: 12-25. In some embodiments, the inhibitor is an antibody that binds to human CSa protein having the amino acid sequence shown in SEQ ID NO:12. In some embodiments, the inhibitor is based on a human CSb protein or fragment thereof having an amino acid sequence comprising or consisting of at least four (e.g., at least four, five, six, acids) specified in any of SEQ ID NOs: 4 or 26. It is an antibody that binds. In some embodiments, the inhibitor is an antibody that binds to the human CSb protein having the amino acid sequence specified in SEQ ID NO:4 or 26. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments of any of the methods disclosed herein, the inhibitor may be selected from the group consisting of a polypeptide, a polypeptide analog, a nucleic acid, a nucleic acid analog, and a small molecule. The polypeptide may be or consists of an antibody or antigen binding fragment thereof that binds to a human complement component CS protein, such as any of those described herein. In some embodiments, the antibody may bind to the alpha chain of the complement component CS protein. In some embodiments, the antibody may bind to the beta chain of the complement component CS protein. In some embodiments, the antibody may bind to the alpha chain of the human complement component CS, and the antibody may (i) inhibit complement activation in a human body fluid, (ii) inhibit the binding of the purified human complement component CS to human complement component C3b or human complement component C4b. and/or (iii) the human activation product may not bind to free CSa (or a combination of any of the above features). The antibody can bind to the human complement component CS protein having or consisting of the amino acid sequence specified in any of SEQ ID NOs: 1-11. The antibody may bind to an isolated oligopeptide comprising an amino acid sequence corresponding to amino acid position 8 to amino acid position 12 of SEQ ID NO: 5. In some embodiments, the antibody includes a monoclonal antibody, a single chain antibody, a humanized antibody, a fully human antibody, a polyclonal antibody, a recombinant antibody, a binary antibody, a chimerized or chimeric antibody, a deimmunized human antibody, a fully human The antibody may be a single chain antibody, an Fv fragment, an Fd fragment, a Fab fragment, a Fab' fragment or an F(ab')2 fragment. In some embodiments, the antibody may be eculizumab or pexelizumab. In the present invention, the antibody is eculizumab. In some embodiments of any of the methods disclosed herein, the composition may be administered intravenously to the human. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments of any of the methods disclosed herein, the complement-associated disorder is an alternative complement pathway-associated disorder. In some embodiments of any of the methods disclosed herein, the complement-associated disorder is a classical complement pathway-associated disorder. In some embodiments, complement-related disorder, rheumatoid arthritis, ischemia-reperfusion injury, atypical hemolytic uremic syndrome, thrombotic thrombocytopenic purpura, dense deposit disease, age-related macular degeneration, spontaneous fetal loss, Pauci-immune vasculitis, epidermolysis bullosa, recurrent fetal loss, multiple sclerosis, HELLP, preeclampsia, traumatic brain injury, Alzheimer's disease, myasthenia gravis, cold agglutinin disease, dermatomyositis, Graves' disease, Hashimoto's thyroiditis, type I diabetes, psoriasis, pemphigus, autoimmune hemolytic anemia, idiopathic thrombocytopenic purpura, Goodpasture syndrome, antiphospholipid syndrome , catastrophic antiphospholipid syndrome, neuromyelitis optica (NMO), multifocal motor neuropathy (MMN), Degos disease, and any other complement-related disorder described herein. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, any of the methods disclosed herein may further include the step of identifying a human as having, suspected of having, or at risk of developing a complement-related disorder. In some embodiments, any of the methods disclosed herein may also include monitoring the human for an improvement in one or more symptoms of the complement-related disorder after administration. In the present invention, the complement-related disorder is atypical uremic syndrome (aHUS). aHUS can be in genetic, acquired or idiopathic form. In some embodiments, aHUS is defined as aHUS associated with complement factor H (CFH) (e.g., due to the presence of antibodies in the subject bound to CFH or mutations in CFH), aHUS associated with membrane cofactor protein (MCP), aHUS associated with complement factor H (CFI). aHUS associated with C4b-binding protein (C4BP), a von Willibrand Factor (vWF)-associated disorder, aHUS associated with complement factor B-(CFB), or resulting in low C3 levels as a result of increased CS consumption There may be a defect in the alternative pathway. In some embodiments not in accordance with the present invention, any of the methods disclosed herein may further include identifying the subject as having, suspected of having, or at risk of developing aHUS. Any of the methods disclosed herein not in accordance with the present invention may include monitoring the subject for an improvement in one or more symptoms of aHUS after administration. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments of any of the methods disclosed herein, the composition may be administered to the subject before, during, or following a plasma therapy (e.g., plasma exchange or plasma infusion). In some embodiments, administration of the subject C5 inhibitor may alleviate the need for plasma therapy by a patient. For example, in some embodiments, administration of the C5 inhibitor to the subject (e.g., chronic administration) may alleviate or substantially reduce the need for plasma therapy by a patient for at least 2 months (e.g., 3 months, 4 months, 5 months). In some embodiments, any of the methods disclosed herein may include administering to the subject one or more additional active agents useful for treating typical HUS or aHUS. One or more additional active agents may be selected from the group consisting of, for example, anti-hypertensives, anti-platelet agents, prostacyclin, fibrinolytic agents and anti-oxidants. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, a human is a baby. Baby, for example 0. 5 (e.g., 1, 1. 5, 2, 2. 5, 3, The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In embodiments of any of the methods described herein where the complement-associated disorder is typical HUS, typical HUS is an E. coli infection. TO. coli infection may occur. In some embodiments of any of the methods disclosed herein, the typical hemolytic uremic syndrome may be associated with a Shigella dysenteriae infection in or on the human. Shigella dysenteriae infection may be a Shigella dysenteriae type 1 infection. Any of the methods described herein may also involve identifying a person as having, suspected of having, or at risk of developing typical hemolytic uremic syndrome. Any of the methods described herein may include monitoring the human for an improvement in one or more symptoms of the typical hemolytic uremic syndrome after its administration. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In embodiments of any of the methods disclosed herein where the complement-associated disorder is CAPS, CAPS may be associated with a precipitation state. Precipitating conditions may be, for example, a cancer, transplantation, an infection, surgery, primary antiphospholipid syndrome, or an autoimmune disorder such as rheumatoid arthritis or systemic Iupus erythematosus. Accordingly, in some embodiments, CAPS may be associated with a cancer, such as stomach cancer, ovarian cancer, or any other cancer known in the art to be associated or precipitated. In some embodiments, CAPS may be idiopathic. Any of the methods described herein may also involve identifying a person as having, suspected of having, or at risk of developing CAPS. This may include monitoring the human for an improvement in one or more symptoms of CAPS after applying any of the methods described herein. The composition may be administered to the human before, during, or following a plasma exchange, plasmapheresis, IVIG, or any other adjunctive therapy for the treatment of CAPS. Any of the methods disclosed herein may also include human administration of one or more additional active agents useful for treating CAPS. One or more additional active agents may be selected from the group consisting of anti-hypertensives, anti-cytokine agents, steroids, anti-coagulants or fibrinolytic agents. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. The complement-related disorder is TTP, and TTP can be inherited in any of the embodiments of any of the methods described here. For example, a person may carry one or more (e.g., two, three, four, or five or more) mutations in the ADAMTS 13 gene. In embodiments of any of the methods described herein, TTP may be an acquired form. For example, in some embodiments, the human can produce antibodies that can bind to and inhibit ADAMTS 13 metalloproteinase. In some embodiments of any of the methods described herein, TTP may occur in a relapsing form. For example, the person might be someone with TTP. In some embodiments of any of the methods disclosed herein, TTP (or recurrent TTP) is associated with, but is not limited to, a precipitating condition such as a cancer, pregnancy, bacterial or viral infection, surgery, or any other TTP-related condition disclosed herein or known in the art. In some embodiments of any of the methods disclosed herein, TTP (or recurrent TTP) is associated with the use of a therapeutic agent that is associated with TTP. For example, TTP may be associated with the use of a platelet aggregation inhibitor, such as ticlopidine or clopidogrel, or an immunosuppressant (eg, cyclosporine, mitomycin C, FK506, or interferon-alpha). Any of the methods described herein may involve identifying people who have, are suspected of having, or are at risk of developing the disease. Any of the methods described herein may include monitoring the human for an improvement in one or more symptoms of TTP after administration. In any of the methods disclosed herein, the composition may be administered to a human before, during, or following a plasma exchange, plasma infusion, plasmapheresis, or a splenectomy. Any of the methods disclosed herein may include administering to humans one or more additional active agents useful for treating or preventing TTP. One or more additional active agents may be selected from the group consisting of anti-hypertensives, steroids, anti-coagulants or fibrinolytic agents. In any of the ways in which the complement-related disorder has been described as DDD, DDD may be an inherited form of the disorder. For example, a person may have a DDD-associated mutation in the complement factor H gene, the complement factor H-related 5 gene, or the complement component CS gene. Any of the methods described here may involve identifying people who have, are suspected of having, or are at risk of developing DDD. Any of the methods described herein may involve monitoring the human for an improvement in one or more symptoms of DDD after application. In any of the methods disclosed herein, the composition may be administered to the human before, during, or following a plasma exchange, plasma exchange, plasmapheresis, or intravenous gamma globulin therapy. Any of the methods disclosed herein may include administering to humans one or more additional active agents for treating DDD. One or more additional active agents may be selected from the group consisting of anti-hypertensives, corticosteroids, anti-coagulants or fibrinolytic agents. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In embodiments of any of the methods disclosed herein where the complement-associated disorder is MG, the human detects an MG-associated autoantibody such as, but not limited to, an MG-associated anti-AChR antibody, an MG-associated anti-MuSK antibody, or an MG-associated antistrial protein antibody. It may be expressive. MG may be ocular MG and/or a drug-induced form of MG, such as D-penicillinamine-induced MG. In some embodiments, the human may be in or at risk of developing myasthenic crisis. In some embodiments, the human may be a neonate with neonatal MG, where a mother with MG transmits MG-associated antibodies across the placenta to the child. Any of the methods described herein may also involve identifying people who have, are suspected of having, or are at risk of developing MG. Any of the methods described herein may further include monitoring the human for an improvement in one or more symptoms of MG after administration. The composition may be administered before, during, or following a plasma exchange, plasmapheresis, IVIG, or immunoadsorption therapy. The following embodiments on this page are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, any of the methods disclosed herein may include administering to humans one or more additional active agents useful for treating or preventing MG. One or more additional active agents may be, for example, acetylcholinesterase inhibitors, immunosuppressive agents, or any other additional active agent known in the art or disclosed herein that is useful for treating MG. In embodiments of any of the methods described herein where the complement-related disorder is paroxysmal cold hemoglobinuria (PCH), PCH may be associated with an infection (e.g., a viral or bacterial infection) or a neoplasm. For example, PCH, a Treponema pa/Iadium infection, an influenza virus infection, a varicella-zoster virus infection, a cytomegalovirus (CMV) infection, an Epstein-Barr virus (EBV) infection, an adenovirus infection, a parvovirus B19 infection, a Coxsackie A9 infection may be associated with a Haemophi/us influenza infection, a Mycop/asma pneumoniae infection, or a KIebsie/Ia pneumoniae infection. In some embodiments, PCH may be associated with non-Hodgkin lymphoma. In some embodiments, PCH may be associated with an immunization (e.g., a measles immunization). In some embodiments of any of the methods disclosed herein, PCH may be acute or relapsing. In some embodiments, any of the methods described herein may include identifying a human as having, suspected of having, or at risk of developing PCH disease. In some embodiments, any of the methods disclosed herein may include monitoring the human for an improvement in one or more symptoms of PCH after administration. In some embodiments of any of the methods disclosed herein, the composition may be administered to the human before, during, or following a plasma exchange, plasma infusion, IVIG therapy, red blood cell transfusion, or plasmapheresis. In some embodiments, any of the methods disclosed herein may include administering to humans one or more additional active agents useful for treating or preventing PCH. One or more additional active agents may be selected from the group consisting of anti-hypertensives, steroids, immunosuppressants (e.g., rituximab), antibiotics, anti-viral agents, and chemotherapeutic agents. In embodiments of any of the methods disclosed herein where the complement-associated disorder is CAD, the CAD may be associated with an infection (e.g., a viral or bacterial infection) or a neoplasm. For example, CAD may be associated with an HIV infection, a cytomegalovirus (CMV) infection, an Epstein-Barr virus (EBV) infection, or a Mycop/vine pneumoniae infection. CAD may be associated with non-Hodgkin's lymphoma. CAD in any of the methods described here can be primary or secondary. The following embodiments on this page are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, any of the methods described herein may include identifying a human as having, suspected of having, or at risk of developing CAD. In some embodiments, any of the methods disclosed herein may include monitoring the human for an improvement in one or more symptoms of CAD after administration. In some embodiments of any of the methods disclosed herein, the composition may be administered to the human prior to, during, or following a plasma exchange, plasma exchange, IVIG therapy, or plasmapheresis. In some embodiments, any of the methods disclosed herein may include administering to a human one or more additional active agents useful for treating or preventing CAD. One or more additional active agents may be selected from the group consisting of anti-hypertensives, steroids, immunosuppressants (e.g., rituximab), antibiotics, anti-viral agents, and chemotherapeutic agents. In the embodiments of any of the methods described herein, where the complement-related disorder is HELLP syndrome, the affected woman may be pregnant or a newly pregnant woman. For example, the woman may be someone who gave birth less than 14 days (e.g., 13 days, 12 days, 11 days, 10 days, nine days, eight days, seven days, six days, less than five hours) before the application. In some embodiments, the woman has been pregnant more than once. In some embodiments, the woman may have developed preeclampsia or HELLP syndrome during at least one previous pregnancy. In embodiments where the complement-related disorder is HELLP syndrome, the methods described herein may further include the step of identifying the woman who has, is suspected to have, or is at risk of developing HELLP syndrome. In some embodiments, any of the methods disclosed herein may further include the step of monitoring the woman for an improvement in one or more symptoms of HELLP syndrome. The following embodiments on this page are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments of any of the methods disclosed herein, the composition may be administered to the woman before, during, or following a plasma exchange, plasmapheresis, platelet transfusion, or red blood cell transfusion. In some embodiments, any of the methods disclosed herein may include the step of administering to a woman at least one or more additional active agents useful for treating or preventing HELLP syndrome in a woman. The one or more additional active agents may be selected from the group consisting of an antihypertensive, a steroid, an anti-seizure agent, and an anti-thrombotic agent. The disclosure characterizes a composition comprising an agent of manufacture comprising (consisting of) a container with a label and an inhibitor of human complement (e.g., an inhibitor of the human complement component CS). The labeling indicates that the composition is to be administered to a human who has, is suspected of having, or is at risk of developing a complement-related disorder, such as any of the complement-related disorders described herein. The inhibitor may, for example, be an antibody that binds to a complement component CS or a fragment thereof, such as CSa or CSb, or an antigen-binding fragment thereof. In some embodiments, the article of manufacture includes one or more additional active agents useful for treating or preventing a complement-related disorder (e.g., improving one or more symptoms of the disorder). The explanation also depends in part on the inventors' discovery that, following treatment with the CS inhibitor eculizumab, a patient with the renal complement-related disorder aHUS and thrombotic microangiopathy (TMA) experienced complete dissolution of TMA in the kidney without further development of TMA. Accordingly, the disclosure characterizes a method of treating thrombotic microangiopathy (TMA) or reducing the frequency or severity of TMA in a patient who has, is suspected of having, or is at risk of developing TMA. The method thus includes administering to the patient (in need) an inhibitor of complement, such as an inhibitor of the complement component C5, to treat TMA in the patient. The inhibitor can be any of the C5 inhibitors described herein, such as eculizumab. Administration of a C5 inhibitor may reduce the frequency or severity of TMA in the patient's brain and/or kidney. In some embodiments, administration of the C5 inhibitor treats or promotes the dissolution of pre-existing TMA in the patient, such as pre-existing TMA in the patient's brain or kidney. The inventors have also discovered that administration of eculizumab to patients with, for example, aHUS or CAPS, results in an unexpectedly rapid improvement of one or more symptoms of the diseases. For example, the inventors discovered that hypertension, reduced urine output, and low platelet levels improved in aHUS patients treated with eculizumab in less than one month (i.e., less than two weeks) after initiating chronic treatment with eculizumab. In another example, the inventors discovered that proteinuria in a patient with membranoproliferative glomerulonephritis improved within one month following the initiation of chronic treatment with eculizumab. Accordingly, the disclosure characterizes a method of ameliorating one or more symptoms associated with a complement-related disorder, such as any of the complement-related disorders described herein, except paroxysmal nocturnal hemoglobinuria. The method includes administering to a patient in need of an effective amount of an inhibitor of complement (e.g., an inhibitor of the complement component C5) to ameliorate one or more symptoms associated with a complement-related disorder, wherein the symptoms persist for more than two months after administration of the inhibitor. It is cured in a short time (e.g., less than an hour). The symptoms of complement-related disorders are well known in the medical art and are described herein. The complement inhibitor can be any of the C5 inhibitors described herein, such as eculizumab. Exemplary symptoms that may be improved with a C5 inhibitor in less than 2 months include, for example, proteinuria, hypertension, reduced platelet counts, and reduced urine output from the kidney. In some embodiments, at least one of the symptoms is at least 40% of the normal level or value (e.g., in embodiments, administration of the C5 inhibitor eculizumab to a hypertensive patient with aHUS may reduce the patient's hypertension to up to 40% of the normal blood pressure (diastolic and/or systolic). can heal. In some embodiments, administration of the C5 inhibitor may completely ameliorate one or more symptoms of the complement-related disorder in the subject. In some embodiments, the patient has received a kidney transplant, such as an aHUS patient who has recently undergone a kidney transplant. The complement-related disorder may be any of those described herein, such as membranoproliferative glomerulonephritis, Degos disease, atypical hemolytic uremic syndrome, antibody-mediated rejection, HELLP syndrome, and catastrophic antiphospholipid syndrome. Many of the complement-related disorders described here are characterized by episodic or sporadic symptomatic presentation and have historically been treated only if symptoms occur. However, the inventors discovered that an underlying complement-related disorder was present even when patients were asymptomatic. Inventors have also discovered that relapses or remissions of disorders can be prevented or at least minimized by chronic treatment using a complement-mediated inhibitor. Such chronic administration of the inhibitor is useful to prevent or minimize the often irreversible damage (e.g., loss of an organ such as a kidney) inflicted on patients with severe complement-related disorders (e.g., aHUS or CAPS) should regressions occur. Accordingly, it is critical to administer a complement inhibitor to the patient at a frequency and in an amount sufficient to consistently maintain a concentration of the inhibitor high enough to prevent or substantially inhibit systemic complement activity in the patient. Thus, the disclosure not covered by the phrasing of the claims characterizes a method of treating a complement-related disorder, chronically, at a frequency and in an amount effective to maintain systemic complement inhibition in patients provided that the complement-related disorder is not paroxysmal nocturnal hemoglobinuria. It involves administering a complement inhibitor (e.g., a C5 inhibitor such as an anti-C5 antibody) to a patient in need thereof. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. As used herein, "chronically administered," "chronically treated," "chronically treating," or similar grammatical variations thereof, refers to the use of a therapeutic agent in a patient's blood at a specific level to completely or substantially suppress systemic complement activity in the patient for an extended period of time. Refers to a treatment regimen used to maintain threshold concentration. Accordingly, a patient treated chronically with a complement inhibitor may be treated with the inhibitor for more than 2 weeks (e.g., the remaining 12 years of the patient's life) or for more than 2 weeks with the inhibitor sufficient to maintain a concentration in the patient's blood that inhibits or substantially inhibits systemic complement activity in the patient. can be treated for an equal period of time. In some embodiments, the complement inhibitor is administered to a patient who requires it at a frequency and at an amount effective to maintain serum less than or equal to 20% of serum lactate dehydrogenase. It can be administered to a patient on a cyclic basis and in an amount effective to maintain LDH levels. See Hill et al. (2005) supra. The base is administered to the patient at a frequency and in an amount effective to maintain a serum LDH level of less than 290, 280, or less than 270. To maintain systemic complement inhibition in a patient, the complement inhibitor may be administered to the patient chronically, for example, once a week, once every two weeks, twice a week, once a day, once a month, or once every three weeks. In some embodiments of any of the methods disclosed herein, a C5 inhibitor (e.g., an anti-C5 antibody) contains at least 0 per C5 molecule in the patient's blood. 7 (e.g., at least 0. 8, 0. 9, one, two, three, four, five, six, seven, eight, nine, or 10 or more) that are effective to maintain a concentration of divalent C5 inhibitor molecule(s) (e.g., a fully anti-C5 antibody such as eculizumab). It can be administered to a patient in some amount and with a frequency of administration. "Divalent" or "bivalent" with respect to a C5 inhibitor refers to a C5 inhibitor that contains at least two binding sites for a C5 molecule. If the C5 inhibitor is monovalent (e.g., a single chain anti-C5 antibody or a Fab that binds to C5), the inhibitor is at least 1 molecule per C5 molecule in the blood. 5 (e.g., may be administered to the patient at a frequency and in an amount effective to maintain concentration. In some embodiments, the monovalent C5 inhibitor may be administered to the patient at a frequency and in an amount effective to maintain a ratio of at least 2:1 (e.g., inhibitor to inhibitor). In some embodiments of any of the methods disclosed herein, a bivalent anti-C5 antibody is administered to the patient at a frequency and in an amount effective to maintain a concentration of at least 40 µg of the antibody per milliliter of the patient's blood. In preferred embodiments, a complete anti-C5 antibody (e.g., eculizumab) is administered at a frequency and in an amount to maintain a concentration of at least 50 µg of antibody per milliliter of the patient's blood. In preferred embodiments, a complete anti-C5 antibody (e.g., eculizumab) is administered at a frequency and in an amount to maintain a concentration of at least 100 µg of antibody per milliliter of the patient's blood. In some embodiments of any of the methods disclosed herein, a monovalent anti-C5 antibody (e.g., a single chain antibody or a Fab fragment) is administered at a frequency effective to maintain the concentration of at least 80 µg of the antibody per milliliter of the patient's blood (e.g., at a frequency effective to maintain its concentration and a It can be administered to a large number of patients. Exemplary chronic dosing strategies are described here. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. The disclosure characterizes a method of treating a complement-related disorder, comprising chronically administering to a patient in need an anti-C5 antibody at a frequency and in an amount effective to maintain systemic complement inhibition in the patients. In some embodiments, the anti-C5 antibody may be administered chronically to a patient who requires it at a frequency and in an amount effective to maintain serum hemolytic activity of less than or equal to 20%. It may be administered to a patient at a frequency and in an amount effective to maintain serum lactate dehydrogenase (LDH) levels within the following: less than or equal to the normal range of LDH (less than or equal to 270) IU/L. See, for example, Hill et al. (2005) supra. In some embodiments, the anti-C5 antibody is administered to the patient at a frequency and in an amount to maintain a concentration of each C5 (bivalent) anti-C5 antibody molecule(s) in the patient's blood. In some embodiments, anti-C5 may be administered to the patient at a frequency and in an amount effective to maintain the rate of anti-C5 antibody. If the anti-C5 antibody is monovalent, the anti-C5 antibody can be administered to the patient at a frequency and in an amount effective to maintain a concentration of at least 2 of the monovalent anti-C5 antibodies per C5 molecule in the blood. In some embodiments, the monovalent anti-C5 antibody may be administered to the patient at a frequency and in an amount effective to maintain a ratio of at least 2:1 (e.g., the antibody). Anti-C5 antibody, for example eculizumab. The patient may have, be suspected of having, or be at risk of developing a complement-related disorder, provided the disorder is not paroxysmal nocturnal hemoglobinuria. For example, complement-related disorder may be selected from the group consisting of membranoproliferative glomerulonephritis, Degos disease, atypical hemolytic uremic syndrome, antibody-mediated rejection, HELLP syndrome, and catastrophic antiphospholipid syndrome. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments of any of the methods disclosed herein, an anti-C5 antibody may be administered chronically to a patient, depending on the weight of the individual. In some embodiments of any of the methods described herein, an anti-C5 antibody (e.g., eculizumab) may be administered chronically to a patient under the dosing schedule set forth in Table 1 and depending on the individual's weight. Table 1. Exemplary Chronic Dosing Schedules for a Complete Anti-C5 Antibody (e.g., eculizumab) by Patient Weight Maintenance Dosing Patient Induction Loading (A) (E) Weight Dosing Any Five weeks per week for Four weeks Dosing at least one dose (A) once at weight less than 800 (e.g. 800 (e.g., at most, followed by more) rng 990, 1000, 1050, 1100, 1150, 1200, 1250, 1300, 1350 or 1400 or more) mg 40 kg per week for two weeks Three weeks at most less (A) dose once at least 500 (e.g. 800 (e.g. at least 800) , 680, 690, 770, 780, 790, 800 or 850 or at least 500 during the next week (e.g. 520, 530, 540, 570, 580, 590, 620, 630, 640, 670, 680, 690, 770, 7 80 , 790, 800 or 850 or more Maintenance Dosage 870, 880, 890, 940, 950, 960, 970, 980, 990, 1300, 1350 or 1400 or more At least 500 in three months (e.g. at least 510, 520, 530, 540, 550, 560, 570, 580, 590, 600, 610, 620, 630, 640, 650, 660, 670, 680, 690,700, 710, 720, 730, 740, 750, 760, 770, 780 , 790, 800 more AFAUA) mg (eg at least, 810, 820, 830, 840, 850, 860, 870, 880, 890, 900, 910, 920, 930, 940, 950, 960, 980, 990, 1000, 1050, 1050 , 1100, 1150, 1200, 1250, 1300, 1350 or 1400 mg (A) dose in excess, after this* twice (e.g. at least 510, 520, 530, 540, 550, 560, 570, 580, 590, 600, 610, 620, 630, 640, 650, 660, 670, 680, 690, 700, 710, 720, 730, 740, 750, 760, 770, 780, 790, 800 which is less than or equal to kg equal body less than or equal to kg body Induction Loading Dosing At least 500 (e.g. 520, 530, 540, 570, 580, 590, 620, 630, 640, 670, 680) once a week for one week , 690, 720, 730, 740, 770, 780, 790, 800, or 850 or more) mg at least 200 mg once a week for one week (e.g., 220, 230, 240, 270, 280, 290, 320, 330, 340, 370, 380, 390, 420, 430, 440, 470, 480, 490, 500, or 550 or more) mg Maintenance Dosing At least 200 every two weeks (e.g., at least 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 480, 490, 500 more) mg At least 200 in two weeks (e.g. at least 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, more) mg ( A) following the dose, then* every two weeks (e.g. at least 210, 220, 230, 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 480, 490, 500 more) following dose (A), every three weeks thereafter* (e.g. at least 210, 220, 230, 240, 250, 260, 270, 280, 290, 300,310, 320, Maintenance Dosing Patient InductionLoading (A) (E) Weight Dosing more) mg 420, 430, 440, 450, 460, 470, 480, 490, 500 more) mg ; for at least one (e.g., at least two, three, four, five, six, seven, eight, nine, 10, 11, 12, 13, 14, or 15 or more) years; or restoring the patient's life. An anti-C5 antibody (e.g., eculizumab) may be administered to a patient depending on the individual's weight under the dosing schedules suggested in Table 2. Table 2. Exemplary Chronic Dosing Schedules for a Complete Anti-C5 Antibody (e.g., eculizumab) by Patient Weight Maintenance Dosing Patient Induction Loading (A) (E) Weight Dosing Any Dose per week for Four weeks (A) at least once per week Five weeks 900 (e.g., at least 1200 followed by more or more) mg or 1400 (e.g. any patient with body weight at least equal to less than equal body weight less than equal to body weight Induction Loading Dosing For two weeks at least 600 (e.g., at least 850 or more) mg once a week At least 600 (e.g., at least 850 or more) mg once a week for two weeks Maintenance Dosing or more) mg at least (e.g., at least 910,920, 93Q 940,950,96Q 970,980,990, 1000, 1050, 1100, 1150 mg at least in three weeks (e.g. at least 610, 620, 630, 640, 650, 660, 670, 680, 690, 700, 710, 720 , 730, 740 , 750, 760, 770, 780, 790, 800 or 850 or more) mg following the (A) dose of 1225, 1250, 1300, 1350 or 1400 or more) mg, thereafter* every two weeks (e.g. at least 910, 920, 930, 940, 950, 960, 970, 980, 990, 1000, 1050, 1100, 1150, or 1200 or more) mg, then every two weeks thereafter (e.g., at least 610, 620, body weight greater than or equal to 630, 640, 650, 660, 670, 680, 690, 700, 710, 720, 730, 740, 750, 760, 770, 780, 790, 800 or less than kg less than equal body weight InductionLoading Dosing At least 600 (e.g., at least 850 or more) mg once a week for one week At least 300 (e.g., at least 550 or more) mg once a week for one week Maintenance Dosing at least every other week (e.g. at least 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 480, 490, 500 or 550 or more) mg Every two weeks at least (e.g. at least 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 480, 490, 500 or 550 or more) mg 850 or more) following the mg (A) dose, thereafter* every two weeks (e.g. at least 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, Following a mg (A) dose of 410, 420, 430, 440, 450, 460, 470, 480, 490, 500 or 550 or more), additional , 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 480, 490, 500 or Maintenance Dosing Patient InductionLoading (A) (E) Weight Dosing 550 or more) mg *According to current statement ( B) maintenance dosing schedule, treatment regimen duration, eg, at least one (e.g., at least two, three, four, five, six, seven, eight, nine, 10, (months); for at least one (e.g., at least two, three, four, five, six, seven, eight, nine, 10, 11, 12, 13, 14, or 15 or more) years; or for the remainder of the patient's life, exemplary dosing schedules in Tables 1 or 2 may be adjusted (frequency, duration and/or total amount of antibody administered) by a medical practitioner as necessary to maintain complete or substantially complete inhibition of systemic complement activity in the patient for the duration of the dosing regimen. as) should be understood. The disclosure, not covered by the phrasing of the claims, characterizes a method of treating a complement-related disorder, the method using an anti-inflammatory agent at a frequency and in an amount effective to maintain a concentration of 100, 110, or 120 or more µg per milliliter of the patient's blood. It involves chronic administration of the C5 antibody to a patient in need thereof, wherein the patient has, is suspected to have, or is at risk of developing a complement-associated disorder, provided that the disorder is not paroxysmal nocturnal hemoglobinuria. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, the anti-C5 antibody is administered to the patient at least once every two weeks. In some embodiments, the anti-C5 antibody is administered to the patient once a week. In some embodiments, the anti-C5 antibody is administered to the patient for at least 9 weeks (e.g., 12 years or for the remainder of the patient's life) under the following dosing schedule: at least 800 (e.g., at least 810, 1000 mg) of the anti-C5 antibody once per week for four consecutive weeks. mg; and anti-C5 mg twice weekly thereafter for the remainder of the dosing schedule. In preferred embodiments, at least 900 mg of the anti-C5 antibody is administered to the patient once weekly for four weeks; at least 1200 mg is administered to the patient during the fifth week; and at least 1200 mg of the anti-C5 antibody is administered to the patient during the fifth week of the chronic dosing schedule. For the rest, it is applied to the patient twice a week. The description, which is not covered by the sentence structure of the claims, characterizes a method for implanting an organ or tissue. The method involves implanting an organ or tissue into a patient in need thereof, wherein prior to the implantation and chronically following an inhibitor of human complement is administered to the patient at a frequency and in an amount effective to substantially inhibit systemic complement activity in the patient. The complement inhibitor may, for example, be a C5 inhibitor such as an anti-C5 antibody (e.g., eculizumab). As used herein, the C5 inhibitor (eg, anti-C5 antibody) contains at least 0 per C5 molecule in the patient's blood. (or at least 1 of 7 bivalent C5 inhibitor molecule(s) It can be administered cyclically and in an amount to maintain a concentration of 5 monovalent C5 inhibitor molecule(s). The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, the C5 inhibitor (e.g., anti-C5 antibody) may be administered to the patient at a frequency and in an amount to maintain a concentration of at least 120 or more µg of the inhibitor (e.g., anti-C5 antibody) in the patient's blood. In some embodiments, mg (e.g., 1200 or more) of anti-C5 antibody is administered to the patient 24 (e.g., less than 2) hours prior to implantation of the organ or tissue into the patient. In some embodiments, the methods also include contacting (e.g., liquid immersion) the organ or tissue with a C5 inhibitor (e.g., an anti-C5 antibody such as eculizumab) for a period of time and under conditions that inhibit complement activation in the organ or tissue following transplantation prior to implantation. may contain. The organ may be, for example, a skin, kidney, heart, lung, limb (e.g., finger or toe), eye, stem cell population, bone marrow, vascular tissue, muscle, nerve tissue, or liver. The patient may have, be at risk of developing, or be suspected of having aHUS. It is applied to patients for less than (some) hours. In some embodiments, the anti-C5 antibody is administered chronically to the patient following implantation. For example, an anti-C5 antibody may be administered to the patient chronically for years or the remainder of the patient's life: at least 700, 1100 or 1200 or more of the anti-C5 antibody once a week for four weeks after the dose for less than 24 hours after organ or tissue implantation. may be administered to a patient undergoing a transplant surgery during the remainder of the dosing schedule: at least 1200 mg of the anti-C5 antibody is administered to the patient less than 24 hours before insertion; at least 900 mg of anti-C5 antibody is administered to the patient within 24 hours of implantation; at least 1200 mg of anti-C5 antibody administered to the patient once a week for four weeks following the first postoperative administration of anti-C5 antibody; 1200 mg administered to the patient in the fifth week following the first postoperative administration of anti-C5 antibody; and at least 1200 doses of anti-C5 antibody administered to the patient twice weekly thereafter for the remainder of the chronic treatment regimen. Methods may also include one or more immunosuppressive agents such as, but not limited to, rapamycin, cyclosporin A, an anti-IL-2 agent, OKT3, and tacrolimus. may involve administering agents to the patient. One or more immunosuppressive agents may be administered before, during, or following insertion. One or more immunosuppressive agents may also be administered before, simultaneously with, or following administration of the C5 inhibitor. The disclosure, which is not covered by the sentence structure of the claim, also characterizes a method of reducing complement-mediated damage to an organ or a tissue when implanted in a patient. The method involves contacting the organ or tissue with a pharmaceutical solution containing an inhibitor of C5 for a period of time prior to implantation of an organ or tissue into a patient in need and under conditions that reduce complement-mediated damage to the organ or tissue upon implantation in the patient. The C5 inhibitor may also be administered to the patient before, during and/or after organ or tissue implantation. The solution may also contain one or more immunosuppressive agents, such as, but not limited to, rapamycin, cyclosporin A, an anti-IL-2 agent, OKT3, and tacrolimus. The inventors also found that in patients with severe complement-related disorders, such as CAPS and APS and attended remission, a low level of complement activity is still present in patients, predisposing them to remission or relapse. As mentioned above, recurrence of symptoms in patients with these severe disorders may indicate sudden and sometimes irreversible damage to major organs such as the kidney. Thus, while the explanation is in no way limited by any particular theory or mechanism of action, the inventors suggest that a patient with a complement-related disorder (e.g., aHUS and CAPS) should be treated to prevent sudden remission or relapse, even after improvement of one or more symptoms of the disorder and/or suggests that it should be treated chronically with a C5 inhibitor even after achieving a clinical remission. Thus, the disclosure characterizes a method of treating a complement-related disorder provided that the disorder is paroxysmal nocturnal hemoglobinuria, which is outside the subject of the claim. The method includes administering to a patient suffering from a complement-related disorder a C5 inhibitor (e.g., an anti-C5 antibody such as eculizumab) in an amount effective to treat the complement-related disorder. The C5 inhibitor is administered to the patient even after improvement of one or more (e.g., two, three, four, five, or six or more) symptoms of the disorder. The C5 inhibitor can be administered to the patient even after complete resolution of one or more symptoms. The C5 inhibitor can be administered to the patient even after the patient has entered clinical remission. The C5 inhibitor may be administered chronically to the patient, for example, after one or more symptoms have improved in the patient and/or for 12 years or the remainder of the patient's life. The complement-related disorder may be any of those described herein, such as membranoproliferative glomerulonephritis, Degos disease, atypical hemolytic uremic syndrome, antibody-mediated rejection, HELLP syndrome, and catastrophic antiphospholipid syndrome. While the explanation is in no way restricted to a particular theory or mechanism of action, for example, based on observations of the effect of eculizumab in patients with aHUS, the inventors concluded that the biological activity of the complement component C5a may contribute substantially to the vasoconstriction and hypertension associated with aHUS. Accordingly, inhibition of C5a using a C5a inhibitor is useful for treating aHUS and/or ameliorating vasoconstriction and hypertension associated with aHUS. The method includes administering to a patient in need of an inhibitor of the complement component C5a in an amount effective to treat aHUS in the patient. Hypertension associated with vasoconstriction and aHUS can be improved in less time (less than 5 hours or even less than 5 hours) by the use of a C5a inhibitor. A C5a inhibitor is an antibody (or an antibody) that binds to a human C5a protein or a fragment thereof that contains or has an amino acid sequence consisting of at least more of the consecutive amino acids shown in any of the following SEQ ID NOs: 12-25. antigen binding fragment). Disclosed herein is an antibody that binds to human C5a protein having the amino acid sequence disclosed in SEQ ID NO:12. The C5a inhibitor does not inhibit the cleavage of C5 into fragments C5a and C5b. The C5a inhibitor also does not inhibit the formation of C5b or the membrane attack complex. As described herein, the C5a inhibitor (e.g., an anti-C5a antibody) can inhibit the interaction between C5a and a C5a receptor (e.g., C5aR or C5L2). The antibody, a monoclonal antibody, a single chain antibody, a humanized antibody, a fully human antibody, a polyclonal antibody, a recombinant antibody, a binary antibody, a chimerized or chimeric antibody, a deimmunized human antibody, a fully human antibody, a single chain antibody may be a Fv fragment, a Fd fragment, a Fab fragment, a Fab" fragment or an F(ab')2 fragment. In the present invention, the complement-related disorder is atypical uremic syndrome (aHUS). aHUS can be in genetic, acquired or idiopathic form. In some embodiments, aHUS, aHUS associated with complement factor H (CFH) (e.g., aHUS associated with mutations in factor H or autoantibodies that bind to and inactivate factor H), aHUS associated with membrane cofactor protein (MCP), complement factor I aHUS associated with (CFI), aHUS associated with C4b-binding protein (C4BP), aHUS associated with complement factor B-(CFB), aHUS associated with complement factor B-(CFB) causing low levels of CS as a result of a vWF defect or increased consumption of CS aHUS may be associated with any other mutation in the alternative pathway of activation. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, any of the methods described herein may further include identifying a patient who has, is suspected to have, or is at risk of developing aHUS. In some embodiments, any of the methods described herein may include monitoring the patient for an improvement in one or more symptoms of aHUS after its administration. In some embodiments of any of the methods disclosed herein, the C5a inhibitor may be administered to the patient before, during, or following a plasma therapy (e.g., plasma exchange or plasma infusion). In some embodiments, administering the C5a inhibitor to the patient may ameliorate the need for plasma therapy with a patient. For example, in some embodiments, administration of a C5a inhibitor to the patient (e.g., chronically for 12 months or for 1, 2, 3, 4, 5, or 6 years or more) may improve or substantially reduce the need for plasma therapy by a patient. In some embodiments, any of the methods disclosed herein may include administering to the patient one or more additional active agents useful for treating typical HUS or aHUS. One or more additional active agents may be selected from the group consisting of, for example, anti-hypertensives, anti-platelet agents, prostacyclin, fibrinolytic agents and anti-oxidants. it could be. means any peptide-linked chain of amino acids, regardless of post modification. The complement component C5 proteins described herein may include or be native strain proteins or may be variants having no more than 50 (e.g., one, two, three, four, five, six, seven) amino acid substitutions. Conservative substitutions typically include substitutions within the following groups: glycine and alanine; valine, isoleucine and leucine; aspartic acid and glutamic acid; asparagine, glutamine, serine and threonine; lysine, histidine and arginine and phenylalanine and tyrosine. The human complement component C5 proteins described herein are also shorter than the proteins of the proteins but retain at least 10% (e.g., at least 10%, at least 15%, at least 995%, or 100% more (see "Methods for Producing an Antibody" below). Antigenic peptide fragments of a C5 protein contain terminal as well as internal deletion variants of the protein. Deletion variants may be missing one, two, three, four, five, six, (of two or more amino acids), or a single non-contiguous amino acid. 600 or more) amino acid residues (e.g., SEQ ID NO. 's: any of 1-11 adjacent amino acid residues of at least 6). In some embodiments, it has a human C5 amino acid (e.g., less than 500 contiguous amino acid residues in any of SEQ ID NOs: 1-11). In some embodiments, an antigenic protein fragment of a full-length, immature C5 protein (prepro-C5 protein) has at least 6 but less than 500 amino acid residues in length. In some embodiments, the human complement component C5 protein may have an amino acid sequence that is more identical than that set forth in SEQ ID NO:1 (see below). Percent (%) amino acid sequence identity is defined as the percentage of amino acids in a candidate sequence that are identical to amino acids in a reference sequence, after aligning the sequences and introducing gaps as necessary to obtain the maximum percentage sequence identity. Alignment for purposes of determining percent sequence identity can be accomplished in a variety of ways within the skill of the art, such as using publicly available computer software, such as BLAST, BLAST-2, ALIGN, ALIGN-2 or Megalign (DNASTAR) software. Suitable parameters for measuring alignment, including any algorithms required to obtain maximal alignment over the full length of the compared sequences, can be determined by known methods. Its antigenic peptide fragments as well as amino acid sequences for exemplary human C5 proteins are known in the art and are set forth below. As used throughout the present disclosure, the term "antibody" refers to a whole or intact antibody (e.g., IgM, IgG, IgA, IgD, or IgE) molecule produced by any of the various methods known in the art and described herein. The term "antibody" includes a polyclonal antibody, a monoclonal antibody, a chimerized or chimeric antibody, a humanized antibody, a deimmunized human antibody, and a fully human antibody. The antibody is obtained from any of various species, e.g., mammals, e.g., humans, non-human primates (e.g., monkeys, baboons, or chimpanzees), horses, cattle, pigs, sheep, goats, dogs, cats, rabbits, guinea pigs, meerkats, hamsters, It can be made or derived from rats and mice. The antibody may be purified or recombinant antibody. As used herein, the term "antibody fragment", "antigen binding fragment" or similar terms refer to an antigen (e.g., a complement component C5 protein), e.g., a single chain antibody, a single chain Fv fragment (scFv), an Fd fragment, refers to the fragment of an antibody that retains the ability to bind to a Fab fragment, a Fab' fragment, or an F(ab')2 fragment. A scFv fragment is a single polypeptide chain containing the heavy and light chain variable regions of the antibody from which scFv is derived. incorporated herein by reference) and intrabodies (Huston et al. (2001) Hum. Drug Discov. Today 9(22): 960-966, descriptions of each of which are incorporated herein by reference in their entirety) can be incorporated into compositions by binding to a complement component C5 protein and used in the methods disclosed herein. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as generally understood by one of ordinary skill in the art to which this description pertains. In case of dispute, the existing document containing the definitions will be checked. Although methods and materials similar or equivalent to those described herein have been used in practice and testing the methods and compositions currently disclosed, preferred methods and compositions are described below. Other features and advantages of the present disclosure, such as methods for treating or preventing a complement-related disorder, will become apparent from the following description, examples and claims. Detailed Description The present disclosure describes compositions comprising an inhibitor of the human complement component CS (e.g., a human complement component CS or an antibody that binds to a biologically active fragment such as CSa and CSb) for treating or preventing a complement-mediated disorder in a human. Provides methods for using the compositions. Without intending to be limiting in any way, exemplary compositions (e.g., pharmaceutical compositions and formulations) and methods for using the compositions are detailed below. Compositions The compositions disclosed herein include an inhibitor of human complement. Any compound that binds to human complement components or otherwise blocks the production and/or activity of any of the human complement components can be utilized in accordance with the present disclosure. For example, a complement inhibitor may be, for example, a small molecule, a nucleic acid or nucleic acid analog, a peptidomimetic, or a macromolecule that is not a nucleic acid or a protein. These agents include, but are not limited to, small organic molecules, RNA aptamers, L-RNA aptamers, Spiegelmers, antisense compounds, double-stranded RNA, small interfering RNA, locked nucleic acid inhibitors, and peptide nucleic acid inhibitors. In some embodiments, a complement inhibitor may be a protein or protein fragment. The compositions contain antibodies specific for a human complement component. Some compounds, C1, C2, C3, C4, C5 (or a fragment thereof; see below), C6, C7, C8, C9, complement compounds, Factor D, Factor B, Factor P, MBL' It contains antibodies directed against MASP-1 or MASP-2, thereby preventing the production of C5a-associated anaphylatoxic activity and/or preventing the assembly of the C5b-associated membrane attack complex. The compositions may also contain naturally occurring or soluble forms of complement inhibitor compounds, such as CR1, LEX-CR1, MCP, DAF, CD59, Factor H, cobra venom factor, FUT-175, complestatin and K76 COOH. Other compounds that may be used to bind human complement components or otherwise block the production and/or activity of any of the human complement components include, but are not limited to, proteins, protein fragments, peptides, small molecules, (commercially available from Archemix Corporation, Cambridge, MA). commercially available), double-stranded RNA including ARC187, L-RNA aptamers, spielgelmers, antisense compounds, serine protease inhibitors, molecules that can be used in RNA interference (RNAi), such as small interfering RNA (siRNA). , containing RNA aptamers, locked nucleic acid (LNA) inhibitors, peptide nucleic acid (PNA) inhibitors, and the like. In some embodiments, the inhibitor inhibits complement activation. For example, the complement inhibitor may inhibit and bind to the complement activation activity of C1 (e.g., C1q, C1r, or C1s), or the complement inhibitor may inhibit (e.g., inhibit their division) or bind to C2, C3, or C4. In some embodiments, it may inhibit the formation or assembly of C3 convertase and/or C5 convertase of the alternative and/or classical pathways of complement. In some embodiments, the inhibitor inhibits terminal complement formation, such as formation of the C5b-9 membrane attack complex. For example, an antibody complement inhibitor may include an anti-C5 antibody. Such anti-C5 antibodies may directly interact with C5 and/or C5b to inhibit the formation and/or physiological function of C5b. The compositions disclosed herein may include a human complement component C5 inhibitor (e.g., an antibody or antigen binding fragment thereof that binds to a human complement component C5 protein or a biologically active fragment thereof, such as C5a or C5b). As used herein, a "complement component C5 inhibitor" is any agent that inhibits: (i) the expression or appropriate intracellular traffic of a complement component C5 protein or its secretion by a cell; (ii) the activity of C5 cleavage fragments C5a or C5b (e.g., binding of C5a to cognate cellular receptors or binding of C5b to C6 and/or other components of the terminal complement complex; see above); (iii) a human Cleavage of the C5 protein to form C5a and C5b; or (iv) appropriate intracellular trafficking of a complement component C5 protein or secretion by a cell. Inhibition of complement component C5 protein expression includes: inhibition of transcription of a gene encoding a human C5 protein; increased degradation of an mRNA encoding a human C5 protein; inhibition of translation of an mRNA encoding a human C5 protein; increased degradation of a human C5 protein; inhibition of proper processing of a human pre-pro C5 protein; or inhibition of proper traffic of a human C5 protein; or Inhibition of secretion by the cell. Methods for determining whether a candidate agent is an inhibitor of human complement component C5 are known in the art and are described herein. A human complement component C5 inhibitor may, for example, be a small molecule, a polypeptide, a polypeptide analog, a nucleic acid, or a nucleic acid analog. As used herein, "small molecule" means less than about 6 kDa and most preferably less than about 2 kDa. It refers to an agent with a molecular weight of less than 5 kDa. Most pharmaceutical companies have extensive libraries of chemical and/or biological mixtures containing sequences of small molecules, often fungal, bacterial or algal extracts, that can be screened with any of the sequences of application. This application envisions using, among other things, small chemical libraries, peptide libraries or collections of natural products. Tan et al. described a library with over two million synthetic compounds compatible with miniaturized cell-based arrays that can be used to screen for inhibitors of component C5. There are many commercially available compound libraries, such as Chembridge DIVERSet. Libraries are also accessible for academic research, such as the NCI developmental therapeutics program's Diversity set library. Rational drug design can also be used. For example, smart drug design can exploit crystal or solution structural information on the human complement component C5 protein. See, for example, the structures described in Hagemann 28(1):172-85. Rational drug design can also be achieved based on known compounds, for example, a known inhibitor of C5 (for example, an antibody that binds to a human complement component C5 or its antigen-binding fragment). Peptidomimetics can be compounds in which at least a portion of the polypeptide of interest has been modified, and the three-dimensional structure of the peptidomimetics remains substantially the same as the three-dimensional structure of the polypeptide of interest. Peptidomimetics may themselves be analogs of a subject polypeptide of the disclosure. Alternatively, at least a portion of the polypeptide sequence of interest may be replaced by a non-peptide structure, thereby substantially preserving the three-dimensional structure of the polypeptide of interest. In other words, one, two or three amino acid residues within the polypeptide sequence of interest may be replaced with a non-peptide structure. In addition, other peptide portions of the polypeptide may, but are not necessarily, replaced by a non-peptide structure. Peptidomimetics (both peptide and non-peptidyl analogues) may have improved properties (e.g., lower proteolysis, higher retention, or higher bioavailability). Peptidomimetics generally have improved oral availability, making them particularly suitable for the treatment of disorders in a human or animal. It should be noted that peptidomimetics may or may not have similar two-dimensional chemical structures but will share common three-dimensional structural features and geometry. Each peptidomimetic may also have one or more unique additional binding elements. Nucleic acid inhibitors can be used to reduce the expression of an endogenous gene encoding human complement component C5. The nucleic acid antagonist may, for example, be an siRNA, dsRNA, a ribozyme, a triplex-helix former, an aptamer, or an antisense nucleic acid. siRNAs are small double-stranded RNAs (dsRNAs) that optionally contain overhangs. For example, the duplex region of an siRNA, approximately 18 to 25 siRNA sequences in length, may be completely complementary to the target mRNA. In particular, dsRNAs and siRNAs can be used to silence gene expression in mammalian cells (e.g., human cells). See, for example, Clemens et al. (2000) Proc. Natl. Acad. Sci. USA may contain nucleobases (i.e., between about 8 and about 80 nucleotides), for example, between about 8 and about 50 nucleobases, or between about 12 and about 30 nucleobases. Antisense compounds include riboenzymes, external guide sequence (EGS) oligonucleotides (oligoenzymes), and other short catalytic RNAs or catalytic oligonucleotides that hybridize to the target nucleic acid and modulate its expression. Antisense compounds may contain a contiguous stretch of at least eight nucleobases that is complementary to a sequence in the target gene. An oligonucleotide does not need to be 100% complementary to the target nucleic acid sequence to be specifically hybridized. When an oligonucleotide interferes with the normal function of the target molecule so that binding of the oligonucleotide to the target results in a loss of efficacy, and the oligonucleotide binds to the target under conditions where specific binding is desired, i.e. in the case of in vivo assays or under physiological conditions in the case of therapeutic treatment, or in vitro assays under the conditions under which the assays are carried out, the target It can be specifically hybridized when there is a sufficient level of complementarity to avoid nonspecific binding to female sequences. Hybridization of antisense oligonucleotides with mRNA (e.g., an mRNA encoding a human C5 protein) may interfere with one or more of the mRNA's normal functions. The functions of mRNA to be addressed include all key functions, such as translocation of RNA to the site of protein translation, translation of protein from RNA, splicing of RNA to yield one or more mRNA species, and catalytic activity that can be combined with RNA. Binding of specific protein(s) to RNA can also be interfered with by antisense oligonucleotide hybridization to RNA. Exemplary antisense compounds include DNA or RNA sequences that specifically hybridize to the target nucleic acid, e.g., mRNA encoding a human complement component C5 protein. The complementary region may extend from approximately 8 to approximately 80 nucleobases. Compounds may contain one or more modified nucleobases. Modified nucleobases may, for example, include 5-substituted pyrimidines, such as 5-iodouracil, -iodocytosine, and C5-propynyl pyrimidines, such as C5-propynylcytosine and C5-propynyluracil. Other suitable modified nucleobases include, for example, 7-substituted-8-aza-7-deazapurines and 7-substituted-7-deazapurines, such as 7-iodo-7-deazapurines, 7-cyano-7-deazapurines, 7-aminocarbonyl- Contains 7-deazapurines. Examples of these are 6-amino-7-iodo-7-deazapurines, 6-amino-7-cyano-7-deazapurines, 6-amino-7-aminocarbonyl-7-deazapurines, 2-amino-6-hydroxy-7-iodo - 7-deazapurines, 2-amino-6-hydroxy-7-cyano-7-deazapurines and 2-amino-6-hydroxy- U.S. No. 093,246. S. Patent Number; "Antisense RNA and DNA," D. A. Melton, Ed. , Cold Spring Harbor Laboratory, Cold Spring Harbor, N. Y. (1988); Haselhoff and Gerlach (1988) Aptamers are short oligonucleotide sequences that can be used to recognize and specifically bind to virtually any molecule, including cell surface proteins. Systemic evolution of ligands by exponential enrichment (SELEX) is robust and can be easily used to identify such aptamers. Aptamers can be made for a wide range of proteins important for therapy and diagnosis, such as growth factors and cell surface antigens. These oligonucleotides have similar affinities and specificities as antibodies 326 ). In some embodiments, the inhibitor of human C5 is an antibody or antigen binding fragment thereof that binds to a human complement component C5 protein. (From here on, the antibody may sometimes be referred to as an "anti-C5 antibody"). In some embodiments, the anti-C5 antibody may bind to an epitope in the human pro-C5 precursor protein. For example, anti-C5 antibody may bind to an epitope of human complement component C5 that contains or consists of the amino acid sequence shown in SEQ ID NO:1 (NCBI Accession No. AAA51925 and Haviland et al. , supra). An "epitope" refers to the region on a protein (eg, a human complement component C5 protein) that is bound by an antibody. "Crossing epitopes" include at least one (e.g., two, three, four, five, or six) amino acid residue(s) in common. The following embodiments generally relating to anti-C5 antibodies are not covered by the sentence structure of the claims but are considered useful for understanding the invention. Only eculizumab is covered by the sentence structure of the present claim. In some embodiments, the anti-C5 antibody binds to an epitope in the human pro-C5 precursor protein that lacks the leader sequence. For example, the anti-C5 antibody may bind to an epitope in the human complement component CS protein comprising or consisting of the amino acid sequence set forth in SEQ ID NO: 2, which is a human CS protein lacking the amino-terminal leader sequence. In some embodiments, the anti-CS antibody may bind to an epitope in the alpha chain of the human complement component CS protein. For example, the anti-CS antibody may bind to an epitope in or intersecting with a protein having the amino acid sequence shown in SEQ ID NO: 3, which is the human complement component CS alpha chain protein. Binding to the alpha chain of CS. In some embodiments, the anti-CS antibody may bind to an epitope on the beta chain of the human complement component CS protein. For example, the anti-CS antibody may bind to an epitope in or intersecting with a protein having the amino acid sequence shown in SEQ ID NO: 4, which is the human complement component CS beta chain protein. In some embodiments, the anti-CS antibody may bind to an epitope that intersects with or is contained within an antigenic peptide fragment of a human complement component CS protein. For example, the anti-CS antibody may bind to an epitope within or intersecting with an antigen peptide fragment of a human complement component CS protein, the fragment comprising or consisting of the following amino acid sequence: VIDHQGTKSSKCVRQKVEGSS (SEQ ID NO: 5) and KSSKC (SEQ ID NO: 5). 6). In some embodiments, the anti-CS antibody may bind to an epitope on or intersecting with an antigen peptide fragment containing or consisting of any of the following amino acid sequence of a human complement component CS protein (exemplary antigenic fragments of SEQ ID NO: 1 which is): NFSLE 1 W FGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIP LDLVPKTEIKRILSVKGLLVGEILSAVLS QEGINILTHLPKGSAEAELMSVVPVF YVFHYLETGNHWNIFHSD (SEQ 1D NO:7); SESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFS LETWFGKEI LVKTLRVVPEGVKRESYS GVTLDPRGIYGTIS RRKEFPYRIPLDLVPKTEIKRIL SVKGLLVGEILS AVLS QEGJNILTHLPKGS AEAELMSVVPVFYVFHYLET GNH WNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYS ( SEQ 1D NO:8); SHKDMQLGRLHMKTLLPVSKPEIRSYFPES (SEQ ID NO:9); SHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSL TTWEIQGIGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYN YRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTV LPLEIGLHNINFS LETWFGKEILVKTLRVVPEGVKRESY S GVTLDPRGIYGTISR RKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAE LMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNAD YSYS (SEQ 1D NO:10); and DHQGTKSSKCVRQKVEG (SEQ ID NO:11). Additional exemplary antigenic fragments of the human complement component CS, such as U. S. Patent No. It is disclosed in No. 6,355,245. In some embodiments, the anti-CS antibody specifically binds to a human complement component CS protein (e.g., the human CS protein having the amino acid sequence shown in SEQ ID NO: 1). The terms "specific binding" or "specifically binding" refer to two molecules forming a complex (e.g., a complex between an antibody and a complement component CS protein) that is relatively stable under physiological conditions. Typically, binding is considered specific when the association coefficient (Ka) is greater than 106 M1. Thus, an antibody can specifically bind to a CS protein having a Kα" of at least 106 M'1 or greater than or greater than 106 M'1. Examples of antibodies that specifically bind to a human complement component CS protein, e.g., U. S. Patent No. It is disclosed in No. 6,355,245. Methods for determining whether an antibody will bind to a protein antigen and/or the affinity of an antibody to a protein antigen are known in the art. For example, binding of an antibody to a protein antigen can be achieved using a variety of techniques, including, but not limited to, Western blotting, plasmon surface resonance method (e.g., BIAcore system; Pharmacia Biosensor AB, Uppsala, Sweden, and Piscataway, N. J. ) or enzyme-linked immunosorbent assays (ELISA). See, e.g., Harlow and Lane (1988) “Antibodies: A Laboratory Manual,” Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N. Y. ; Benny K. C. Lo (2004) "Antibody (1992) "Antibody Engineering, A Practical Guide," W. H. Freeman and Co. ,NY; Borrebaek (1995) "Antibody Engineering," 2nd Edition, Oxford University Press, NY, U. S. Patent No. 6,355,245. In some embodiments, the anti-C5 antibody may cross-block the binding of another antibody that intersects with or binds to an epitope within a human component C5 protein. In some embodiments, the anti-C5 antibody may cross-block the binding of an antibody that intersects with or binds to an epitope within a human complement component C5 protein. The peptide fragment may be a fragment of a human complement component C5 protein having the amino acid sequence shown in any of SEQ ID NOs: 1-11. For example, the peptide fragment may contain or consist of the following amino acid sequence: VIDHQGTKSSKCVRQKVEGSS (SEQ ID NO: 5). As used herein, the term "cross-blocking antibody" refers to an antibody that reduces the amount of anti-C5 antibody binding to an epitope on a complement component C5 protein compared to the amount of anti-C5 antibody binding to the epitope in the absence of the antibody. Suitable methods for determining whether a first antibody cross-blocks the binding of a second antibody to an epitope are known in the art. For example, cross-blocking antibodies can be detected in the presence and absence of a test antibody (produced by the hybridoma cell line ATCC designation HB-11625; see U. S. Patent No. definable. 5G1 in the absence of test antibody. 5G1 in the presence of test antibody compared to binding of antibody 1. Low binding of antibody 1 indicates that the test antibody is a cross-blocking antibody. Methods for identifying an epitope to which a specific antibody (e.g., an anti-C5 antibody) binds are known in the art. For example, the binding epitope of an anti-C5 antibody of an antibody is a complement component of the C5 protein that has several (e.g., three, four, five, six, seven, eight, nine, 10, 15, 20, or 30 or more) intersecting peptide fragments ( For example, SEQ can be defined by measuring binding to several intersecting fragments. Subsequently, each of the different intersecting peptides binds to a unique address on a solid support, for example, individual wells of a multi-well analysis plate. The anti-C5 antibody is then challenged by contacting each of the peptides in the assay plate for a period of time and under conditions that allow binding of the antibody to its epitope. Unbound anti-C5 antibody is removed by washing each well. Next, a detectably labeled secondary antibody that binds to an anti-C5 antibody when present in one well of the plate is contacted with each of the wells, and unbound secondary antibody is removed by washing steps. The presence or amount of detectable signal produced by detectably labeled secondary antibody in a well is an indication that the anti-C5 antibody has bound to the specific peptide fragment associated with the well. See, for example, the specific epitope to which the Harlow and Lane antibody binds can also be identified using BIAcore chromatographic techniques (see, e.g., Pharmacia BIAtechnology Handbook, "Epitope 160:20191-8). The anti-C5 antibodies described herein may have activity in blocking the production or activity of the C5a and/or C5b active fragments of a complement C5 protein (e.g., a human C5 protein). Through this blocking effect, anti-C5 antibodies inhibit, for example, the proinflammatory effects of C5a and the production of the C5b-9 membrane attack complex (MAC) on the surface of a cell. Anti-C5 antibodies capable of blocking the production of C5a, such as Moongkarndi et al. (1982) Immunobiol. In some embodiments, an anti-C5 antibody or antigen binding fragment thereof enhances the binding ability of a C5 protein to the human complement component C3b (e.g., C3b located on an AP or CP C5 convertase complex) by greater than 50% (e.g., 55, In embodiments, upon binding of a C5 protein, an anti-C5 antibody or antigen binding fragment thereof may reduce the ability of a C5 protein to bind to the human complement component C4b (e.g., C4b present on a CP C5 convertase complex) by more than 50%. Methods of determining whether an antibody can block the production or activity of C5a and/or C5b active fragments of a complement component C5 protein or its binding to complement component C4b or C3b are known in the art and are described at 340 . (See also below. ) In some embodiments, an anti-C5 antibody binds to an amino terminal region of the alpha chain of a complement component C5 protein, but does not bind to free C5a. Epitopes for an anti-C5 antibody in the amino-terminus region of the alpha chain include, for example, epitopes in the human sequence VIDHQGTKSSKCVRQKVEGSS (SEQ ID NO: 5). In some embodiments, the compound contains and/or the antibody is eculizumab (Soliris®; Alexion Pharmaceuticals, Inc. , Cheshire, CT). (See, e.g., Kaplan (2002) Curr Opin Investig In some embodiments not according to the present invention, the compound comprises and/or the antibody is pexelizumab (Alexion Pharmaceuticals, Inc.). , Cheshire, CT). (See, for example, the following embodiments relating to Whiss C5 inhibitors are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, the C5 inhibitor is an antibody that binds to C5a (sometimes referred to herein as "an anti-C5a antibody"). In some embodiments, the antibody binds to C5a but not full-length C5. As described above, the proform of C5, a 1676 amino acid residue precursor protein, is processed by a series of proteolytic cleavage events. The first 18 peptides (numbered -18 to -1) form a signal peptide that is cleaved from the precursor protein. The remaining 1658 amino acid protein is split in two places to form alpha and beta chains. The first cleavage occurs between amino acid residues 655 and 656. The second cleavage occurs between amino acid residues 659 and 660. The two cleavage states result in the formation of three distinct polypeptide fragments: (i) a fragment containing amino acids 1 to 655, referred to as the beta chain; (ii) amino acids tetrapeptide fragment referred to as the alpha chain. Alpha chain and beta chain polypeptide fragments are linked together by disulfide bonds and form the mature C5 protein. CP or AP C5 convertase activates mature C5 by cleaving the alpha chain between residues 733 and 734, resulting in the release of the C5a fragment (amino acids 660 to 733). The remainder of mature C5 is fragment C5b, which contains residues 734 to 1658 of the alpha chain disulfide linked to the beta chain. In vivo, C5a is rapidly metabolized by a serum enzyme, carboxypeptidase B, to a 73 amino acid form that has lost the carboxyterminal arginine residue, termed "C5a des-Arg". Accordingly, in some embodiments, an antibody that binds to C5a also binds to discharged C5a. In some embodiments, an antibody that binds to C5a does not bind to discharged C5a. In some embodiments, the C5 inhibitor is an antibody that binds to a neoepitope found on C5a, i.e., an epitope that becomes vulnerable upon release of C5a from the alpha chain fragment of mature C5. Antibodies that bind to C5a (eg, a neo-epitope found on C5a) are known in the art as methods for producing such antibodies. For example, an antibody that binds to C5a, such as PCT Publication No. WO C5a neoepitope specific antibody may have context specificity. In another example, an antibody that binds to C5a is a commercial C5a neoepitope-specific antibody, such as, but not limited to, sc-52633 (Santa Cruz Biotechnology, Inc.). , Santa Cruz, California), , ab11877 (Abcam, Cambridge, Massachusetts), and HM2079 (clone 2952; HyCult Biotechnology, the Netherlands). In some embodiments, an antibody that binds to C5a may cross-block the binding of any of the above-mentioned C5a neoepitope-specific antibodies. In some embodiments, the C5 inhibitor may be an antibody that binds to a mammalian (e.g., human) C5a protein. For example, the antibody can bind to a human C5a protein having the following amino acid sequence: TLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTE CCVVASQLRANISHKDMQLGR (SEQ ID NO:12). The antibody can bind to human C5a at an epitope in or intersecting the following amino acid sequence: CCYDGACVNNDETCEQRAAR (SEQ ID NO:13); KCCYDGACVNNDETCEQR (SEQ ID NO:14); VNNDETCEQR (SEQ ID NO:15); VNNDET (SEQ ID NO:16); AARISLGPR (SEQ ID NO:17); CCYDGACVNNDETCEQRAA (SEQ ID NO:18); CCYDGACVNNDETCEQRA (SEQ ID NO:19); CCYDGACVNNDETCEQR (SEQ ID NO:20); CCYDGACVNNDETCEQ (SEQ ID NO:21); CCYDGACVNNDETCE (SEQ ID NO:22); CYDGACVNNDETCEQRAAR (SEQ ID NO:23); YDGACVNNDETCEQRAAR (SEQ ID NO:24); or CYDGACVNNDETCEQRAAR (SEQ ID NO:25). In some embodiments, an antibody is directed against a human C5a protein or its fragment containing at least four adjacent amino acid sequences (e.g., at least four, five, six, seven, as shown in any of the following SEQ ID NOs: 12- can be connected. Methods for generating additional C5a protein fragments and suitable C5a specific antigen binding sites that bind to an antibody disclosed herein, e.g., U. S. Patent No. It is claimed at 4,686,100. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, binding of an antibody to C5a can inhibit the biological activity of C5a. Methods of measuring C5a activity include, for example, chemotaxis assays, RIAs, or ELISAs (see, e.g., Ward and Zvaifler (1971) J Clin Invest. In embodiments, binding of an antibody to C5a can inhibit the interaction between C5a and C5aR1. Suitable methods for detecting and/or measuring the interaction between C5a and C5aR1 (in the presence and absence of an antibody) are known in the art and include, for example, binding of detectably labeled (e.g., radioactively labeled) C5a to C5aR1-expressing peripheral blood mononuclear cells in the presence and absence of an antibody. can be evaluated in its absence. A decrease in the amount of detectably labeled C5a bound to C5aR1 in the presence of antibody compared to the amount of binding in the absence of antibody is an indication that the antibody inhibits the interaction between C5a and C5aR1. In some embodiments, binding of an antibody to C5a can inhibit the interaction between C5a and C5L2 (see below). Methods for detecting and/or measuring the interaction between C5a and C5L2 are known in the art and are described, e.g., see Ward (2009) J). In some embodiments, the C5 inhibitor binds to C5b (sometimes referred to herein as "an anti-C5b antibody"). In some embodiments, the antibody binds to C5b but not full-length C5. The structure of C5b is described above and also, for example, as described by Müller-Eberhard, C5b combines with C6, C7 and C8 to form the C5b-8 complex on the surface of the target cell. The protein complex formed during the series of combinations includes C6, C7 and C8). Upon binding of a few C9 molecules, the membrane attack complex (MAC, C5b-9 terminal complement component (TCC)) is formed. When sufficient numbers of MACs penetrate target cell membranes, the openings that form (MAC pores) mediate rapid osmotic lysis of target cells. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, binding of an antibody to C5b can inhibit the interaction between C5b and C6. In some embodiments, binding of the antibody to C5b may inhibit the association or activity of the C5b-9 MAC-TCC. In some embodiments, binding of an antibody to C5b can inhibit complement-dependent cell lysis (e.g., in vitro and/or in-vivo). Suitable methods for assessing whether an antibody inhibits complement-dependent lysis include, for example, hemolytic assays and other functional assays to detect the activity of soluble C5b-9. For example, a decrease in the ability of complement to lyse cells in the presence of an antibody is described by Kabat and Mayer (eds. ), “Experimental Immunochemistry, 2nd Edition,” 135-240, analysis, or a conventional variation of this analysis, e.g., Hillmen et al. It can be measured by the chicken erythrocyte hemolysis method described in (2004) N Engl J Med 350(6):552. Antibodies that bind to C5b are also known in the art, as are methods for making such antibodies. See, for example, U. S. Patent No. 6,355,245. Commercially available anti-C5b antibodies are available from a number of vendors, such as Hycult ab46168). The CS inhibitor may be an antibody that binds to a mammalian (eg, human) form of CSb. For example, the antibody can bind to a portion of a human CSb protein that has the following amino acid sequence: NFIGYKNFKNF EITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSET AVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPG SGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLN TGEQTAELVSDSVWLNIEEK CGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVAL AAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANA DDSQENDEPCKEIL (SEQ ID NO: 4). The antibody can bind to a portion of a human CSb protein having the following amino acid sequence: HNINE NGSFKENS QYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLE NTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKD NLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGG GFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNY KMTDKNFL GRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEA SHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKA LVEGVDQLFTDYQIKDGHVILQLNSIPSS DFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAA CKCVEADCG QMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKY KATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYN FSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC (SEQ ID NO:26). The antibody is directed against the human CSb protein or its adjacent at least four amino acids (e.g., at least four, five, six, seven, eight, nine, 10, 11, 12, one amino acid) as shown in SEQ ID NO:4 or SEQ ID NO:26. It can bind to the fragment containing the acid sequence. Additional exemplary subfragments of human C5b or C5a that can bind to a C5 inhibitor antibody, such as U. S. Patent No. It is disclosed in No. 6,355,245. The inhibitor may be an antibody that binds to the C5a polypeptide (e.g., the human C5a polypeptide having the amino acid sequence shown in SEQ ID NO: 12). The inhibitor may be an antibody that specifically binds to a C5b polypeptide. Methods for determining whether a particular agent is a human complement component C5 inhibitor are disclosed herein and are known in the art. For example, the concentration and/or physiological activity of C5a and C5b in a body fluid can be measured by methods well known in the art. Methods for measuring C5a concentration or activity include, for example, chemotaxis assays, RIAs or ELISAs (see Complement Inflamm. 8:328-340). For C5b, hemolytic assays or assays for soluble C5b-9 can be used as discussed here. Other analyzes known in the art may also be used. Using these or other appropriate types of assays, candidate agents capable of inhibiting human complement component C5, such as an anti-C5 antibody, can be screened to identify compounds useful in the methods described herein and to determine appropriate dosage levels of such compounds. Methods for detecting inhibition of expression of mRNA or protein (e.g., inhibition of expression of human C5 protein or expression of an mRNA encoding human C5 protein) are well known in the art of molecular biology and include, for example, Northern blot, RT-PCR (or quantitative RT-PCR) for mRNA. ) techniques and, for protein detection, Western blot, dot blot or ELISA techniques. (See, for example, Sambrook et al. (1989) "Molecular Cloning: A Laboratory Manual, 2nd Edition," Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N. Y. ) Methods for determining whether a candidate compound inhibits the cleavage of human C5 into C5a and C5b forms are known in the art and are, for example, described in Moongkarndi et al. (1982) Inhibition of the human complement component C5 may also reduce a subject's ability to cellularize complement in body fluids. Such reductions in the cytolyzing ability of complement can be measured by methods well known in the art, such as a conventional hemolytic assay such as the hemolysis assay described by Kabat and Mayer (eds), "Experimental 135-139" or a conventional variation of the assay such as the erythrocyte hemolysis method. Pharmaceutical Compositions and Formulations. Compositions containing a complement inhibitor (e.g., a human complement component C5 antibody, e.g., an anti-C5 antibody or antigen binding fragment thereof, or an interferon alpha antibody), e.g., to treat aHUS, CAPS, Degos disease, or TMA It can be formulated as a pharmaceutical composition for the purpose of regulating the drug. Pharmaceutical compositions will generally contain a pharmaceutically acceptable carrier. As used herein, it refers to and includes all solvents, dispersing media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like. The compositions may contain a pharmaceutically acceptable salt, such as an acid addition salt or a base addition salt (see, e.g., Berge et al. (1977)J. Pharm. Sci. 66:1-19). The compositions can be formulated according to standard methods. Pharmaceutical compounding is a well-established technique and also, for example, Gennaro (2000) “Remington: The Science and Practice al. (1999) "Pharmaceutical Dosage Forms and Drug Delivery Systems," 7th Edition, Edition (ISBN: 091733096X). In some embodiments, a composition may be formulated, for example, as a buffered solution at a suitable concentration and suitable for storage at 2-8°C. In some embodiments, a composition may be formulated for storage at a temperature below 0°C (e.g., -20°C or -80°C). Pharmaceutical compositions can take various forms. These forms include, for example, liquid, semi-solid, and solid dosage forms, such as liquid solutions (e.g., injectable and non-infusable solutions), dispersions or suspensions, tablets, pills, powders, liposomes, and suppositories. The preferred form depends in part on the intended mode of administration and therapeutic setting. For example, compositions containing an anti-CS antibody for systemic or local delivery may be in the form of injectable or non-infusable solutions. Accordingly, the compositions may be formulated for administration by a parenteral mode (e.g., intravenous, subcutaneous, intraperitoneal, or intramuscular injection). As used herein, "parenteral administration", "parenterally administered" and other grammatically equivalent expressions refer to modes of administration other than enteral and topical administration, generally by injection, and include, but are not limited to, intravenous, intranasal, intraocular, pulmonary, These include intramuscular, intraarterial, intrathecal, intracapsular, intraorbital, intracardiac, intradermal, intrapulmonary, intraperitoneal, intratracheal, subcutaneous, subcuticular, intraarticular, subcapsular, subarachnoid, intraspinal, epidural, intracerebral, intracranial, intracarotid and intrasternal injection and infusion (see below). Compositions may be formulated as a solution, microemulsion, dispersion, liposome, or other ordered structure suitable for stable storage at high concentration. Sterile injectable solutions can be prepared by combining the required amount of an antibody disclosed herein in a suitable solvent with one or a combination of the ingredients listed above, followed by filter sterilization, if necessary. In general, dispersions are prepared by incorporating an inhibitor of human complement component 05 described herein (e.g., an anti-CS antibody) into a sterile vehicle containing a basic dispersion medium of those enumerated above and other desired ingredients. In the case of sterile powders for the preparation of sterile injectable solutions, methods for the preparation include vacuum drying and freeze drying producing a powder of the antibody disclosed herein and any additional desired ingredients from a previously sterile filtered solution thereof. Suitable fluidity of a solution can be maintained, for example, by maintaining the required particle size in the state of dispersion by the use of a coating, e.g. lecithin, and by the use of surfactants. Prolonged absorption of injectable compositions can be achieved by including in the composition a reagent that delays absorption, such as monostearate salts and gelatin. The C5 inhibitor (e.g., an anti-C5 antibody or antigen binding fragment thereof) or the interferon alpha inhibitor may be prepared with a carrier that will protect the compound against rapid release, such as a controlled release formulation that includes implants and microencapsulated delivery systems. Biodegradable, biocompatible polymers, such as ethylene vinyl acetate, polyanhydrides, polyglycolic acid, collagen, polyorthoesters and polylactic acid, can be used. Many methods for the preparation of such formulations are known in the art. (See, for example, J. R. Robinson (1978) "Sustained and Controlled Release Drug Delivery Systems," Marcel Dekker, Inc. , New York. ) An inhibitor disclosed herein may be formulated in a composition suitable for intrapulmonary regulation (e.g., nebulizer regulation) in a mammal, such as a human. Methods for preparing such compositions are known in the art and, for example, U. S. Patent formulations and suitable systems for applying the formulations, for example, U. S. No. It is disclosed in No. 5,997,848. A human C5 inhibitor disclosed herein (e.g., an anti-C5 antibody or antigen binding fragment thereof) may be modified, for example, with a moiety that improves its stabilization and/or retention in the circulation, e.g., in blood, serum, or other tissues. The stabilization fraction increases the stability or retention of the antibody to at least 1.5 Nucleic acid inhibitors of human complement C5 (e.g., an antisense nucleic acid or siRNA) described herein are used as part of a gene therapy protocol to deliver nucleic acids that can be used to express and produce agents intracellularly. It can be incorporated into a gene structure to be used. Expression constructs of such components can be administered in any biologically effective carrier, e.g., in any formulation or composition that can effectively deliver the component gene into cells in vivo. Approaches involve insertion of the gene of interest into viral vectors, recombinant bacterial or eukaryotic plasmids, including recombinant retroviruses, adenoviruses, adeno-associated viruses, lentiviruses, and herpes simplex virus-1 (HSV-1). Viral vectors can transfect cells directly; Plasmid DNA can be delivered, for example, with the help of cationic liposomes (lipofectin) or derivatives (e.g., antibody conjugates), polylysine conjugates, gramicidin S, artificial viral envelopes or other such intracellular carriers, as well as by direct injection of the gene construct or CaPO4 precipitation. was performed in vivo. (See also “EX vivo Approaches,” below. ") Examples of suitable retroviruses include pLJ, pZIP, pWE, and pEM and are described by Danos and Mulligan ( et al.) of skill in the art. (Science uses vectors obtained (see, e.g., Berkner et al. (1988) BioTechniques 6:616; 155). Suitable adenoviral vectors derived from the Ad type 5 dl324 adenovirus strain or other strains of adenovirus (e.g., Ad2, Ad3, Ad7, and the like) are known to those skilled in the art. Another vector system useful for transferring the gene in question is adeno-associated virus (AAV). See, for example, Flotte et al. (1992) Am. J. Multiple (e.g., two, three, four, five, six, seven, eight, nine, or 10 or more) inhibitor(s) (e.g., one human or more than one C5 inhibitor) may be formulated together. For example, a C5-specific siRNA and an anti-C5 antibody can be formulated together. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, an inhibitor of human complement disclosed herein (e.g., an inhibitor of human C5 such as an anti-C5 antibody or antigen binding fragment thereof) is used to treat a complement-related disorder (e.g., APS, CAPS, aHUS, Degos disease, HELLP syndrome, etc.) It may be formulated with one or more additional active agents useful for treating or ameliorating a symptom of any of the described complement-related disorders. For example, an anti-C5 antibody may be formulated with an antihypertensive, an anticoagulant, and/or steroid (e.g., a corticosteroid). Examples of anticoagulants include, for example, warfarin (Coumadin), aspirin, heparin, fenindione, fondaparinux, idraparinux, and thrombin inhibitors (for example, argatroban, Iepirudin, bivalirudin, or dabigatran). An inhibitor of human CS (e.g., an anti-CS antibody, an anti-CSa antibody, or an anti-CSb antibody) may also include a fibrinolytic agent for the treatment of CAPS (e.g., ancrod, s-aminocaproic acid, antiplasmin-α1, prostacyclin and defibrotide) or an anti-cytokine agent. Anti-cytokine agents include, for example, antibodies or soluble receptors that bind to and modulate the activity of the cytokine (e.g., a pro-inflammatory cytokine such as TNF). Examples of anti-cytokine agents include, for example, a TNF inhibitor such as a soluble TNF receptor (e.g., etanercept; Enbrel®) or an anti-TNF antibody (e.g., infliximab; Remicade®). In some embodiments, the inhibitor may be formulated for use with or with an anti-CD20 agent such as rituximab (Rituximab; Biogen Idec, Cambridge, MA). In some embodiments, the inhibitor of human CS may be formulated for administration to a subject in conjunction with intravenous immunoglobulin therapy (IVIG), red blood cell transfusion, plasmapheresis, or plasma exchange. If an inhibitor of human CS is used in combination with a second active agent, or if two or more inhibitors of human CS are to be used (e.g., an anti-CSa antibody and an anti-CSb antibody), the agents may be formulated separately or together. For example, the respective pharmaceutical compositions can be mixed and administered together, for example, immediately prior to administration, or can be administered separately, for example, at the same or at different times (see below). As described above, a composition may be formulated such that it contains a therapeutically effective amount of a human CS (e.g., an anti-CS antibody or antigen binding fragment thereof), or the composition may be formulated to contain a subtherapeutic amount of the inhibitor and a subtherapeutic amount of one or more additional active agents. ie the total components are therapeutically effective to treat a complement-related disorder. In some embodiments, a composition may be formulated to contain two or more inhibitors of human CS at each sub-therapeutic dose, such that the inhibitors in total are therapeutic for treating a complement-related disorder such as aHUS, CAPS, Degos disease, or HELLP syndrome. It is at an effective concentration. Methods for determining a therapeutically effective dose (e.g., a therapeutically effective dose of an anti-CS antibody) are known in the art and are disclosed herein. Methods for Producing an Antibody Suitable methods for producing an antibody (e.g., an anti-C5 antibody, an anti-C5a antibody, and/or an anti-C5b antibody) or antigen binding fragments thereof in accordance with the disclosure are known in the art (see, e.g., Patent No. 6,355,245) and described herein. For example, monoclonal anti-C5 antibodies can be produced using cells expressing the complement component C5, a C5 polypeptide, or an antigenic fragment of the C5 polypeptide (e.g., a C5a or C5b) as an immunogen, thus providing a pathway in animals from which antibody-producing cells and therefore monoclonal antibodies can be isolated. immune response occurs. The sequence of such antibodies can be determined, and antibodies or variants thereof have been produced by recombinant techniques. Recombinant techniques can be used to produce monoclonal antibodies that can bind to the human complement component C5, as well as chimeric, CDR-grafted, humanized and fully human antibodies based on the sequence of polypeptides. In addition, antibodies derived from recombinant libraries ("phage antibodies") can be selected, for example, based on target specificity, using C5-expressing cells or polypeptides derived therefrom as decoys to isolate antibodies or polypeptides. The production and isolation of non-human and chimeric anti-C5 antibodies are within the scope of the expert. Recombinant DNA technology can be used to modify one or more characteristic features of antibodies produced in non-human cells. Thus, chimeric antibodies can be made to reduce its immunogenicity in diagnostic or therapeutic applications. Moreover, immunogenicity can be minimized by humanization of antibodies by CDR grafting and optionally by framework modification. See U. S. Patent NOs. Antibodies can be obtained from animal serum, or, in the case of monoclonal antibodies or fragments thereof, produced in cell culture. Recombinant DNA technology can be used to produce antibodies according to established procedures including procedures in bacterial or preferably mammalian cell culture. The selected cell culture system preferentially secretes antibody product. In another embodiment, a process disclosed herein to produce an antibody uses a host transformed with a hybrid vector, e.g., E. coli or a mammalian cell. The vector contains one or more expression cassettes comprising a promoter operatively linked to a first DNA sequence encoding a signal peptide linked to the appropriate reading frame for a second DNA sequence encoding the antibody protein. The antibody protein is then collected and isolated. Optionally, the expression cassette may include a promoter operatively linked to polycistronic (e.g., bicistronic) DNA sequences encoding antibody proteins each individually operably linked to a signal peptide in the appropriate reading frame. In vitro propagation of hybridoma cells or mammalian host cells is performed using conventional standard culture media (e.g., Dulbecco's Modified Eagle Medium (DMEM) or RPMI 1640 medium), optionally amended with a mammalian serum (e.g., fetal calf serum), trace elements, and growth sustaining media. is performed in appropriate culture media containing supplements (e.g., feeder cells, e.g., normal mouse peritoneal exudate cells, spleen cells, bone marrow macrophages, 2-aminoethanol, insulin, transferrin, low-density lipoprotein, oleic acid, and the like). Proliferation of host cells, which are bacterial cells or yeast cells, is carried out in a similar manner in suitable culture media known in the art. For example, suitable culture media for bacteria include media LE, NZCYM, NZYM, NZM, Terrific Broth, SOB, SOC, 2 xYT or M9 Minimal media. For yeast, suitable culture media include media YPD, YEPD, Minimal media, or Complete Minimal Loss media. In vitro production provides relatively pure antibody preparations and enables scale-up production to yield large quantities of the desired antibodies. Techniques for culturing bacterial cells, yeast, plant or mammalian cells are well known in the art and include homogeneous suspension culture (e.g., in an airlift reactor or in a continuous stirrer reactor) and homogeneous suspension culture (e.g., in corrugated fibers, microcapsules, agarose microbeads, or ceramics). It contains immobilized or compacted cell culture (on cartridges). Large amounts of the desired antibodies can also be obtained by growing mammalian cells in vivo. To this end, hybridoma cells producing the desired antibody can be injected into histocompatible mammals to cause the growth of antibody-producing tumors. Optionally, animals are prepared with a hydrocarbon, especially mineral oils, such as pristane (tetramethyl-pentadecane), prior to injection. After one to three weeks, antibodies are isolated from the body fluids of these mammals. For example, hybridoma cells obtained by fusion of appropriate myeloma cells with antibody-producing spleen cells from Balb/c mice or transfected cells derived from the hybridoma cell line Sp2/0 producing the desired antibodies were introduced into Balb/c mice optionally pretreated with pristane. It is injected intraperitoneally. After one to two weeks, the acidic fluids are removed from the animals. described in Cold Spring Harbor, the entire disclosure of which is incorporated herein by reference. Techniques for the preparation of recombinant antibody molecules are described in USA 97(2):722-727, supra. Cell culture supernatants are screened for desired antibodies by immunofluorescent staining of cells expressing complement component C5, preferably by immunoblot, by an enzyme immunoassay, such as a sandwich assay or a dot assay, or a radioimmunoassay. For the isolation of antibodies, immunoglobulins in culture supernatants or acidic broth may be concentrated by, for example, precipitation with ammonium sulfate, dialysis against hygroscopic material, such as polyethylene glycol, filtration through selective membranes, or the like. When necessary and/or desired, antibodies can be prepared by conventional chromatography methods, such as gel filtration, ion-exchange chromatography, DEAE-chromatography on cellulose, and/or (immuno-)affinity chromatography, for example, a ore derived from a complement component C5-expressing cell line. with more than one surface polypeptide or with Protein-A or -G, purified by affinity chromatography. Another embodiment provides a process for preparing a bacterial cell line secretory antibodies directed against a C5 protein in a suitable mammal. For example, a rabbit is immunized with samples collected from tissue or cells expressing C5 or C5 polypeptide or fragments thereof. A phage display library produced from the immunized rabbit is constructed and aligned against the desired antibodies according to methods well known in the art (e.g., methods described in various references). Hybridoma cells secreting monoclonal antibodies are also disclosed. Preferred hybridoma cells are genetically stable, express monoclonal antibodies of the desired specificity as described herein, and are propagated from deep-frozen cultures by thawing and propagation in vitro or in vivo as ascites. A process is provided for the preparation of a hybridoma cell line that expresses monoclonal antibodies against a complement component C5 protein. In this process, a suitable mammal, such as a Balb/c mouse, is coated with one or more polypeptides or antigenic fragments of C5, or with one or more polypeptides or antigenic fragments derived from a C5-expressing cell, C5-expressing cell, or as described above. is immunized with an antigenic carrier containing a purified polypeptide. Antibody-producing cells of the immunized mammal are grown briefly in culture or fused with cells of a suitable myeloma cell line. The hybrid cells obtained in fusion are cloned and cell clones that secrete the desired antibodies are selected. For example, spleen cells from Balb/c mice immunized with a C5-expressing Chronic Lymphocytic Leukemia (CLL) cell line are fused with cells of the myeloma cell line PAI or myeloma cell line Sp2/0-Ag14. The resulting hybrid cells are then screened for expression of the desired antibodies and positive hybridoma cells are cloned. Methods for preparing a hybridoma cell line are by injecting subcutaneously and/or intraperitoneally an immunogenic composition containing human C5 protein (or an immunogenic fragment thereof) several times, e.g., four to six times, over several months, e.g., two or four months. It involves immunizing Balb/c mice. Spleen cells from immunized mice are removed two to four days after the last injection and fused with cells of the myeloma cell line PAI in the presence of a fusion promoter, preferably polyethylene glycol. Preferably, myeloma cells are fused in a solution containing about 30% to about 50% polyethylene glycol with a molecular weight of about 4000, a three- to twenty-fold excess of spleen cells from immunized mice. After fusion, cells are propagated at regular intervals to prevent normal myeloma cells from outgrowing the desired hybridoma cells in appropriate culture media supplemented with a selection medium, e.g., HAT medium, as described supra. Antibodies and fragments thereof may be "chimeric". Chimeric antibodies and their antigen-binding fragments contain fragments from two or more different species (e.g., mouse and human). Chimeric antibodies can be produced with mouse variable regions of the desired specificity spliced to human constant domain gene segments (e.g., U. S. Patent No. 4,816,567). In this way, non-human antibodies can be modified to make them more suitable for human clinical application (e.g., methods for treating and preventing a complement-related disorder in a human subject). Monoclonal antibodies of the present disclosure are particularly useful in humans as therapeutic agents because they are not cleared from the circulation as quickly as antibodies to non-human (e.g., mouse) antibodies and typically provoke an adverse immune reaction. Methods of preparing humanized antibodies are generally well known in the art. For example, humanization can be achieved essentially by substituting the CDRs of Winter and co-workers (see, e.g., Jones CDRs or CDR sequences for the corresponding sequences of a human antibody). See also, for example, Staelens et al. (2006) Mol Immunol humanized forms are multivariate derived from a non-human species (donor antibody), such as a mouse, rat, rabbit or non-human primate, where the multivariate (CDR) region residue of the recipient antibody has the desired specificity, affinity and binding capacity. These are human antibodies modified with a region residue (receptor antibody). In some cases, framework region residues of the human immunoglobulin are also replaced by corresponding non-human residues (also called "back mutations"). In addition, it can be used to diversify. The properties of a humanized antibody are also affected by the choice of the human framework. Furthermore, humanized and chimerized antibodies can be modified to include residues not present in the recipient antibody or donor antibody to further improve antibody properties, e.g., affinity or effector function. Full human antibodies are also provided in the description. The term "human antibody" includes antibodies having variable and constant regions derived from human germline immunoglobulin sequences (if present). Human antibodies may contain amino acid residues that are not encoded by human germline immunoglobulin sequences (e.g., mutations introduced by random or site-specific mutagenesis in vitro or by somatic mutation in vivo). However, the term "human antibody" does not include antibodies grafted onto human framework sequences of CDR sequences derived from the germline of another mammalian species, such as a mouse (i.e., humanized antibodies). Fully human or human antibodies can be derived from human cells from transgenic mice carrying human antibody genes (carrying variable (V), variable (D), accession (J), and constant (C) exons. For example, it is currently possible to generate transgenic animals (e.g., mice) that are capable of producing a full repertoire of human antibodies upon immunization in the absence of endogenous immunoglobulin production. (See, for example, Jakobovits et al. (1993) Proc. Natl. Acad. Mouse strains can be engineered to contain gene sequences from unrearranged human immunoglobulin genes. The human sequences can encode both heavy and light chains of human antibody and will function correctly in mice that have undergone rearrangement to provide a broad antibody repertoire similar to that in humans. Transgenic mice can be immunized with the target protein (e.g., a complement component C5 protein, fragments thereof, or cells expressing the C5 protein) to generate specific antibodies and a diverse sequence of their coding RNA. Nucleic acids encoding the antibody chain components of such antibodies can be cloned from the animal into an imaging vector. Typically, separate populations of nucleic acids encoding heavy and light chain sequences are cloned and then the separate populations are recombined upon insertion into the vector, meaning that any given copy of the vector receives a random combination of a heavy and a light chain. The vector is designed to express antibody chains so that they can be assembled and displayed on the external surface of an imaging package containing the vector. For example, the antibody chain can be expressed as fusion proteins carrying a phage coat protein from the outer surface of the phage. The display packets can then be scanned for the appearance of antibodies binding to a target. Additionally, human antibodies can be derived from phage display libraries, creating synthetic phage libraries using randomized combinations of their regions. By selection on fully human antibodies to the antigen, the V-regions can be made quite human-like in structure. See, for example, U. S. Patent NOs. No. 6,794,132, for the production of human antibodies. See also Mendez et al. (1998) Nature European Patent No. EP 0 463 151 B1. In an alternative approach, GenPharm International, Inc. Others, including , have utilized a “minilocus” approach. In the minilocus approach, an exogenous lg locus is mimicked by introducing fragments (individual genes) from the lg locus. Thus, one or more VH genes, one or more DH genes, one or more JH genes, a mu constant region, and a second constant region (preferably a gamma constant region) are constructed in a construct to insert into a mammal. This approach, for example U. S. Patent No: 5,545,807; In some embodiments, de-immunized anti-CS antibodies or antigen binding fragments thereof are provided. De-immunized antibodies or antigen-binding fragments thereof have been modified to make the antibody or antigen-binding fragment thereof non-immunogenic or less immunogenic to a given species (e.g., a human). De-immunization can be achieved by modifying the antibody or its antigen binding fragment using any of a variety of techniques known to those skilled in the art (see, e.g., PCT Publication No. by identifying potential T cell epitopes and/or B cell epitopes within the amino acid sequence of the WO antibody or its antigen binding fragment and removing one or more of the potential T cell epitopes and/or B cell epitopes from the antibody or its antigen binding fragment, for example using recombinant techniques. -can be immunized. The modified antibody or antigen-binding fragment thereof can optionally be produced and tested to identify one or more of the desired biological activities, e.g., antibodies or antigen-binding fragments thereof that have retained binding affinity but have low immunogenicity. Methods for identifying potential T cell epitopes and/or B cell epitopes include methods known in the art, e.g., computational methods (see, e.g., WO, in vitro or in silico techniques, and biological assays or physical methods (e.g., determination of binding of peptides to MHC molecules, determining the binding of peptide:MHC complexes to T cell receptors from the species to receive the antibody or its antigen-binding fragment, testing the protein or peptide portions thereof using transgenic animals with MHC molecules of the species to receive the antibody or its antigen-binding fragment, or It can be carried out using transgenic animals reconstituted with immune system cells taken from the same species (testing, etc.) In various embodiments, de-immunized anti-CS antibodies, de-immunized antigen binding fragments, Fab, Fv, scFv, Fab' and F(ab')2, monoclonal antibodies, murine antibodies, engineered antibodies (e.g., chimeric, single chain, CDR-grafted, humanized, fully human antibodies, and artificially selected antibodies), synthetic antibodies, and semi-synthetic antibodies. A recombinant DNA is produced containing a spacer encoding for a heavy chain variable domain and/or a light chain variable domain of the cell line expressing an anti-CS antibody or a CS protein. The term DNA includes coding single-stranded DNAs, double-stranded DNAs composed of these DNAs and their complementary DNAs, or these complementary (single-stranded) DNAs themselves. In addition, anti-CS antibodies can be enzymatically or enzymatically engineered to contain DNA encoding a heavy chain variable domain and/or a light chain variable domain, the authentic DNA sequence containing a heavy chain variable domain and/or a light chain variable domain, or a mutant thereof. can be synthesized chemically. A mutant of authentic DNA is a DNA encoding a heavy chain variable domain and/or a light chain variable domain of the above-mentioned antibodies in which one or more amino acids have been deleted, inserted, or replaced with one or more other amino acids. Preferably, in humanization and expression optimization applications, the modification(s) are outside the CDRs of the heavy chain variable domain and/or light chain variable domain of the antibody. The term mutant DNA also includes silent mutations in which one or more nucleotides are replaced by other nucleotides carrying new codons coding for the same amino acid(s). The term mutant sequence also includes a degenerate sequence. Degenerate sequences are degenerate in the sense of the genetic code when an unlimited number of nucleotides are replaced by other nucleotides without causing a change in the originally encoded amino acid sequence. To achieve an optimal expression of such degenerate sequences, their different restriction sites and/or a heavy chain murine variable domain and/or a light chain murine variable domain, the specific host, in particular E. coli may be useful due to the frequency of specific codons preferred by it. The term mutant is intended to include a DNA mutant obtained by in vitro mutagenesis of authentic DNA according to methods known in the art. For assembly of fully tetrameric immunoglobulin molecules and expression of chimeric antibodies, recombinant DNA inserts encoding the heavy and light chain variable domains are fused with the corresponding DNAs encoding the heavy and light chain constant domains, then transferred into suitable host cells, e.g., hybrid vectors after fusion. . In certain embodiments, recombinant DNAs containing a spacer for a human constant domain and a heavy chain murine variable domain such as y1, y2, y3 or y4 may be used. Preferably, recombinant DNAs containing a spacer encoding for a light chain murine variable domain of an antibody fused to K, a human constant domain K, or N are also provided. Another embodiment is where the heavy chain variable domain and the light chain variable domain optionally include a signal sequence that facilitates processing of the antibody in the host cell and/or a peptide and/or a cleavage site and/or a peptide spacer and/or an agent that facilitates purification of the antibody. Accordingly, the monoclonal antibodies or antigen binding fragments of the disclosure are naked antibodies or antigen binding fragments that are not conjugated with other agents, such as a therapeutic agent or detectable label. Alternatively, the monoclonal antibody or antigen binding fragment encodes an agent, e.g., a cytotoxic agent, a small molecule, a hormone, an enzyme, a growth factor, a cytokine, a riboenzyme, a peptidomimetic, a chemical, a prodrug, A nucleic molecule containing the sequences may be conjugated with a detectable label (e.g., an NMR or X-ray contrast agent, fluorescent molecule, etc.) In some embodiments, an anti-C5 antibody or antigen binding fragment (e.g., Fab, Fv, single-chain scFv, Fab', and F(ab')2) is linked to a molecule that extends the half-life of the antibody or antigen binding fragment (see above). . Several possible vector systems are accessible for expression of cloned heavy chain and light chain genes in mammalian cells. One class of vectors relies on the integration of desired gene sequences into the host cell genome. Cells with stably integrated DNA simultaneously harbor drug resistance genes, such as E. co/igpt (Mulligan and Berg ( or Tn5 neo (Southern and Berg (1982) Mol. Appl. Genet. 1:327). The selectable marker gene can be ligated to the DNA gene sequences to be expressed or introduced into the same cell by cotransfection (Wigler et al. (1979) Cell 16:77). A second class of vectors utilizes DNA elements that confer autonomous replication capacities to an extrachromosomal plasmid. These vectors can be derived from animal viruses, such as bovine papillomavirus (Sarver et al.). (1982) Proc. Natl. Acad. Since an immunoglobulin cDNA consists only of sequences representing the mature mRNA encoding an antibody protein, additional gene expression elements that regulate gene transcription and RNA processing are required for the synthesis of immunoglobulin mRNA. These elements may include splicing signals, transcription promoters, inducible promoters, enhancers, and termination signals. cDNA expression vectors containing these elements were prepared by Okayama and Berg (1983) Mol. Cell Biol. 3:280; Cepko et al. Contains what is described. As is evident from the description, antibodies that bind to human complement components (e.g., antibodies that bind to C5, C5b, or C5a) can be used in therapies that include combination therapies (e.g., therapies for a complement-related disorder) as well as in monitoring disease progression. In therapeutic embodiments of the present disclosure, bi-specific antibodies are contemplated. Bispecific antibodies are monoclonal, preferably human or humanized antibodies that have specificity to bind to at least two different antigens. Currently, one of the context specificities is for the human complement protein C5 antigen and the other is for any other antigen. Methods for making bi-specific antibodies are within the scope of those skilled in the art. Traditionally, recombinant production of bispecific antibodies can be fused to immunoglobulin constant domain sequences with antibody variable domains bearing the co-binding specificities (antibody-antigen junctions) of two immunoglobulin heavy chain/light chain pairs where the two heavy chains have different specificities. Fusion preferably occurs with an immunoglobulin heavy chain constant domain containing at least part of the hinge, CH2 and CH3 regions. DNAs encoding the immunoglobulin heavy chain fusions and, if desired, the immunoglobulin light chain are inserted into separate expression vectors and cotransfected into a suitable host organism. For additional details illustrating currently known methods for producing bispecific antibodies, see Tutt et al. (1991)J. Immunol. 147:60. Bispecific antibodies also include cross-linked or heteroconjugate antibodies. Heteroconjugate antibodies can be made using any suitable cross-linking method. Suitable crosslinking agents are known in the art and are available through several crosslinking techniques. S. Patent No. It is described in No. 4,676,980. Various techniques for making and isolating bispecific antibody fragments directly from recombinant cell culture are also described. For example, bi-specific antibodies have been produced using leucine zippers. (See, for example, Kostelny et al. (1992)J. Immunol can bind to Fab' parts of different antibodies. Antibody homodimers can be reduced at the hinge region to form monomers and subsequently re-oxidized to form antibody heterodimers. Apart from this method, the "dual antibody" technology described by antibody homodimers 6448 has provided an alternative mechanism for making bi-specific antibody fragments. The fragments contain a heavy chain variable domain (VH) linked to a light chain variable domain (VL) by a linker that is too short to allow pairing between two domains on the same chain. Accordingly, the VH and VL domains of one fragment are forced to pair with the complementary VL and VH domains of another fragment, thus creating two antigen-binding domains. Another strategy to make bi-specific antibody fragments with the use of single-chain Fv (scFv) dimers has also been reported. (See, for example, Gruber et al. (1994)J. Immunol. It contains a pair of tandem Fd segments (Vn-CH1-Vn-Cn1) that form the antigen binding site. Linear antibodies can be bi-specific or mono-specific. The stated non-inventive disclosure is also described in Wu et al. (2007) Nat Biotechnol is designed so that two different light chain variable domains (VLs) from two different parent antibodies are linked in tandem, either directly or via a short linker, with recombinant DNA techniques followed by the light chain constant domain. Methods for producing DVD-Ig molecules from two parent antibodies are also described, for example, PCT Publication NOs. It is disclosed in WO 08/024188 and WO 07/024715. Methods and Treatment References in Examples The compositions described above (e.g., any of the C5 inhibitors described herein or pharmaceutical compositions thereof) are useful inter alia for treating or preventing various complement-related disorders (e.g., AP-related disorders or CP-related disorders) in a subject. The compositions may be administered to a subject, e.g., a human subject, in part, using a variety of methods depending on the route of administration. The route may be, for example, intravenous injection or infusion (IV), subcutaneous injection (SC), intraperitoneal (IP), intraocular or intramuscular injection. Certain inhibitors, such as small molecules, may be administered orally to a subject. Administration can be achieved, for example, by local infusion, injection or an implant. Implant membranes, such as sialastic membranes, may be of a porous, non-porous or gelatinous material containing fibres. The implant may be configured for sustained or periodic release of the composition. (See, for example, U. S. The fluid may be dispersed via an implantable device connected to, for example, osmotic pumps, biodegradable implants, electrodiffusion systems, electroosmosis systems, vapor pressure pumps, electrolytic pumps, effervescent pumps, piezoelectric pumps, erosion-based systems, or electromechanical systems. An appropriate dose of a complement inhibitor described herein (e.g., a C5 inhibitor such as an anti-C5 antibody) capable of treating or preventing a complement-related disorder in a subject is determined, including, for example, the age, sex, and weight of the subject to be treated, and the particular inhibitor compound used. It may depend on various factors. For example, a different dose of an anti-C5 antibody may be required to treat a subject with RA compared to the dose of a C5-specific siRNA molecule required to treat the same subject. Other factors affecting the dose administered to the subject include, for example, the type and severity of the complement-related disorder. For example, a subject with RA may require administration of a different dosage of an anti-C5 antibody than a subject with AMD. Other factors may include, for example, other medical disorders concurrently or previously affecting the subject, the subject's general health, the subject's genetic predisposition, diet, timing of regulation, rate of secretion, drug combination, and any other additional therapeutics administered to the subject. It should further be understood that a specific dosage and treatment regimen for any particular subject will depend on the judgment of the treating practitioner (e.g., physician or nurse). An antibody disclosed herein may be administered as a fixed dose or at one milligram per kilogram (mg/kg) dose. In some embodiments, the dose may also be selected to reduce or prevent the production of antibodies or other host immune responses against one or more of the antibodies active in the composition. While not intended to be restrictive in any way, exemplary dosages of an antibody include, for example, 1-100 µg/kg, 0. Exemplary dosages of 5-50 antibodies are 0, 0 without restriction. 1 µg/kg, 0. 5 µg/kg, 1. 0 ug/kg contains 8 mg/kg. Additional exemplary dosage amounts and schedules are provided herein (see, e.g., Tables 1 and 2). A pharmaceutical composition may contain a therapeutically effective amount of an inhibitor of a component disclosed herein (e.g., a C5 inhibitor such as an anti-C5 antibody). Such effective amounts can readily be determined by one of ordinary skill in the art, based in part on the effect of the inhibitor administered and, when more than one agent is used, the combinatorial effect of the antibody and one or more additional active agents. A therapeutically effective amount of an antibody disclosed herein also depends on factors such as the disease state, age, sex, and weight of the individual and whether the antibody (and one or more additional active agents) induces a desired response in the individual, such as improvement of at least one condition parameter, e.g. Improvement of at least one symptom of a complement-related disorder may vary depending on the ability to elicit it. For example, a therapeutically effective amount of an antibody that binds to C5a and Cb5 can inhibit (reduce the severity or eliminate the occurrence) and/or prevent a particular disorder and/or any of the symptoms of the particular disorder known in the art or disclosed herein. A therapeutically effective amount is also an amount in which any toxic or detrimental effects of the composition are outweighed by its therapeutically beneficial effects. Appropriate human doses of a C5 inhibitor described herein (e.g., an anti-C5 antibody) may also be evaluated, for example, in Phase I dose-escalation studies. See, for example, the following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. Similar terms used are intended to mean an amount of an agent (e.g., a C5 inhibitor) that will produce the desired biological or medical response (e.g., an improvement in one or more symptoms of a complement-related disorder). In some embodiments, a composition disclosed herein contains a therapeutically effective amount of an anti-C5 antibody. In some embodiments, a composition disclosed herein comprises a therapeutically effective amount of an siRNA that specifically binds to and promotes the inactivation of C5 mRNA in a mammalian cell. In some embodiments, a composition disclosed herein contains a therapeutically effective amount of an antibody that specifically binds C5a. In some embodiments, the composition includes any of the antibodies disclosed herein and one or more (e.g., three, four, five, six, seven, eight, nine, 10, or 11 or more) additional therapeutic agents such that the composition as a whole is therapeutically effective. Contains. For example, a composition may include an anti-C5 antibody and an immunosuppressive agent as described herein, wherein the antibody and agent are each at a concentration that, when combined, is therapeutically effective for treating or preventing a complement-related disorder in a subject. The toxicity and therapeutic efficacy of these compounds can be determined by known pharmaceutical procedures in cell cultures or experimental animals (e.g., animal models of any complement-related disorders described herein). These procedures can be used, for example, to determine the LD50 (lethal dose for 50% of the population) and the ED50 (therapeutically effective dose for 50% of the population). The dose ratio between toxic and therapeutic effects is the therapeutic index, which can be expressed as the LD50/ED50 ratio. A complement inhibitor that exhibits a high therapeutic index (e.g., a C5 inhibitor such as an anti-C5 antibody, an anti-C5a antibody, or a nucleic acid that binds and promotes inactivation of C5 mRNA in a mammalian cell) is preferred. When using compounds that exhibit toxic side effects, care should be taken to design a delivery system that targets these compounds to the affected tissue site and minimizes potential damage to normal cells, thereby reducing side effects. Data from cell culture analyzes and animal studies can be used to formulate a dosage range for use in humans. The dosage of such an inhibitor generally falls within a range of circulating concentrations of the inhibitor that include ED 50 with little or no toxicity. Dosage may vary within this range depending on the dosage form administered and route of administration used. The therapeutically effective dose for a C5 inhibitor (e.g., an anti-C5 antibody or an anti-C5a antibody) used as described herein (e.g., for treating or preventing a complement-associated disorder) can be initially estimated from cell culture analyses. A dose may be formulated in animal models to achieve a circulating plasma concentration range that includes the IC 50 (i.e., the concentration of test compound that achieves a half-maximal inhibition of symptoms) as determined in cell culture. This information can be used to more precisely determine beneficial doses in humans. Levels in plasma can be measured, for example, by high-performance liquid chromatography or by ELISA. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, the methods may be performed in conjunction with other therapies for complement-related disorders. For example, the composition may also be administered to a subject before or after plasmapheresis, IVIG therapy, plasma infusion, or plasma exchange. See, for example, Appel et al. (2005) J Am. Soc Nephrol. anti-C5 antibody or an anti-C5a antibody) is not administered in conjunction with IVIG. In some embodiments, the composition may also be administered to a subject before or after a kidney transplant. Exemplary methods for introducing an organ (e.g., a kidney) or tissue are provided herein, along with exemplary dosing schedules for an anti-C5 antibody. As used herein, a "subject" can be any mammal. For example, a subject could be a human, a nonhuman primate (e.g., monkey, baboon, or chimpanzee), a horse, a cow, a pig, a sheep, a goat, a dog, a cat, a rabbit, a guinea pig, a desert It could be a shrew, a hamster, a rat or a mouse. In some embodiments, the subject is an infant (e.g., a human infant). In some embodiments, the subject is a female. As used herein, "person in need of prevention," "person in need of treatment," or a physician, a nurse, or a nurse practitioner; Refers to someone who may appropriately benefit from a treatment given by a veterinarian in the case of non-human mammals (such as treatment with a composition comprising a complement inhibitor (an anti-C5 antibody, an anti-C5 antibody that binds and promotes the inactivation of a C5 mRNA in a mammalian cell). - a C5 inhibitor such as a C5a antibody or a nucleic acid (e.g., a siRNA or antisense nucleic acid). As discussed above, the complement inhibitors disclosed herein (e.g., a C5 inhibitor such as an anti-C5 antibody) can be used to treat a variety of complement-related disorders, such as AP-related disorders and/or CP-related disorders. These disorders include, without limitation, rheumatoid arthritis (RA); antiphospholipid antibody syndrome; lupus nephritis, ischemia-reperfusion injury; atypical hemolytic uremic syndrome (aHUS); typical or infectious hemolytic uremic syndrome (tHUS); dense deposit disease (DDD); neuromyelitis optica (NMO); multifocal motor neuropathy (MMN); multiple sclerosis (MS); macular degeneration (e.g., age-related macular degeneration (AMD)); hemolysis, elevated liver enzymes and low platelets (HELLP) syndrome; thrombotic thrombocytopenic purpura (TTP); spontaneous fetal loss; Pauci-immune vasculitis; epidermolysis bullosa; recurrent fetal loss; and traumatic brain injury. (See, e.g., Holers. The complement-related disorder described herein includes a cardiovascular disorder, myocarditis, a cerebrovascular disorder, a peripheral (e.g., musculoskeletal) vascular disorder, a renovascular disorder, a mesenteric/enteric vascular disorder, vasculitis, Henoch-Schönlein purpura nephritis, vasculitis associated with systemic lupus erythematosus, vasculitis associated with rheumatoid arthritis, immune complex vasculitis, Takayasu disease, dilated cardiomyopathy, diabetic angiopathy, Kawasaki disease (arthritis), venous gas embolus (VGE) and restenosis following stent placement, rotational atherectomy and percutaneous transluminal coronary artery disease. Disorders associated with a complement-related vascular disorder such as angioplasty (PTCA), without limitation, MG, CAD, dermatomyositis, Graves' disease, atherosclerosis, Alzheimer's disease, systemic inflammatory response, sepsis, septic shock, spinal cord injury, glomerulonephritis, Hashimoto's thyroiditis, type I Includes diabetes, psoriasis, pemphigus, AIHA, catastrophic APS (CAPS). As used herein, a subject who is "at risk for developing a complement-related disorder" (e.g., an AP-related disorder or a CP-related disorder) is subject to one or more (e.g., two, three, four, five) treatments for developing the disorder. A subject has six, seven, eight or more risk factors. Risk factors will vary depending on the particular complement-related disorder but are well known in the medical art. For example, risk factors for the development of DDD include, for example, susceptibility to developing the condition, i.e. family history of the condition, or, for example, the gene encoding complement factor H (CFH), complement factor H-related 5 (CFHR5) and/or complement component C3 (C3). It involves a genetic predisposition to develop the condition, such as one or more mutations in it. This type of DDD, as well as methods for determining whether a subject carries one or more of the mutations, are described by Zipfel et al. (2006) "The role of complement in membranoproliferative glomerulonephritis," In: Complement and Kidney Disease, Springer, Berlin, pages 199. Thus, a person at risk for developing DDD may be, for example, someone who has one or more DDD-associated mutations in the gene encoding CFH or someone who has a family history of developing the disease. Risk factors for TTP are well known in the art and include, for example, a predisposition to develop the disease, i.e., a genetic predisposition to develop the condition, such as, for example, a family history or one or more mutations in the ADAMTS 13 gene. ADAMTS 13 mutations associated with TTP are described in detail, for example, by Levy et al. (2001) is examined. Risk factors for TTP also include cancer, bacterial infections Bartonella sp. Conditions or agents known to precipitate TTP or TTP relapse include, but are not limited to, infections, viral infections (e.g., HIV and Kaposi's sarcoma virus), pregnancy, or surgery. See, for example, Avery et al. (1998) American Journal of Hematology 58:148-149 and Tsai, supra). TTP or TTP relapse has also been associated with the use of certain therapeutic agents (drugs), such as ticlopidine, FK506, corticosteroids, tamoxifen or cyclosporine. These manifestations of TTP may then occur where appropriate, for example, in a person at risk for developing "infection-associated TTP", for example, someone who has one or more TTP-associated mutations in the ADAMTS13 gene. A person who is at risk for developing a relapsing form of TTP may be, for example, someone who has TTP and has an infection, is pregnant, or has had surgery. Risk factors for aHUS are well known in the art and include, for example, predisposition to develop the condition, i.e. a family history of the condition, or one or more mutations, for example in complement Factor H (CFH), membrane cofactor protein (MCP; CD46), C4b. binding protein, complement factor B (CFB) or complement factor I (CFI) involves a genetic predisposition to the development of the condition. (See, for example, Warwicker et al. supra. ) Risk factors also include, for example, infection with Streptococcus pneumoniae, pregnancy, cancer, exposure to anti-cancer agents (e.g., quinine, mitomycin C, cisplatin, or bleomycin), exposure to immunotherapeutic agents (e.g., cyclosporine, OKT3, or interferon), anti-cancer agents (e.g., cyclosporine, OKT3, or interferon). -includes exposure to platelet agents (e.g., ticlopidine or clopidogrel), HIV infection, transplantation, autoimmune disease, and combined methylmalonic aciduria and homocystinuria (cblC). See, for example, Constantinescu et Risk factors for HELLP are well known in the medical art and include, for example, multiparous pregnancy, maternal age over 25 years, Caucasian race, occurrence of preeclampsia or HELLP in a previous pregnancy, and history of a poor pregnancy outcome. (See, for example, Sahin et al. A pregnant Caucasian woman who develops preeclampsia during pregnancy may be at risk for developing HELLP syndrome during or after a second pregnancy. Risk factors for CAD are well known in the medical art and include conditions or agents known to precipitate CAD or CAD relapse, such as, but not limited to, neoplasms or infections (e.g., bacterial and viral infections). Conditions known to be associated with the development of CAD include, for example, HIV infection (and AIDS), hepatitis C infection, Mycop/viral pneumonia infection, Epstein-Barr virus (EBV) infection, cytomegalovirus (CMV) infection, rubella, or infectious mononucleosis. Neoplasms associated with CAD include, without limitation, non-Hodgkin lymphoma. These manifestations of CAD may then be referred to, for example, as "infection-associated CAD" or "neoplasm-associated CAD" as appropriate. Thus, a person at risk for developing CAD may be someone who has, for example, an HIV infection, rubella, or a lymphoma. See also Finland and Barnes (Acta) Risk factors for a thrombotic microangiopathy (TMA) are well known in the medical art and include, for example, aHUS, TTP or other conditions associated with TMA such as lupus, cancers, disseminated intravascular coagulation and other coagulopathies, and pre-eclampsia. Risk factors for PCH in the past are well known in the medical art and include PCH or conditions or agents known to precipitate PCH relapse, such as, but not limited to, neoplasms or infections (e.g., bacterial and viral infections) or certain immunizations (e.g., measles immunization). Conditions known to be associated with the development of PCH, such as syphilis (a Treponema pa/Iadium infection), measles, mumps, influenza virus infection, varicella-zoster virus infection, cytomegalovirus (CMV) infection, Epstein-Barr virus (EBV) infection, adenovirus infection, parvovirus B19 infection, Coxsackie A9 infection, Haemophilus influenza infection, Mycop/asma pneumoniae infection, and K/ebsiella pneumoniae Neoplasms associated with PCH include, without limitation, both solid and non-Hodgkin lymphoma, such as myelofibrosis, chronic lymphocytic leukemia (CLL), and non-Hodgkin's lymphoma. Manifestations of hematopoietic neoplasms may be a person at risk for, for example, "infection-associated PCH" or, if appropriate, someone who has, for example, an EBV infection or a lymphoma. Risk factors for MG are well known in the art and include, for example, a family history of predisposition to develop the condition, i.e. familial MG, or a genetic predisposition to develop the condition. For example, some HLA types are associated with an increased risk of developing MG. Risk factors for MG include exposure to or ingestion of certain MG-inducing drugs such as, but not limited to, D-penicillinamine. A subject with one or more previously experienced symptoms may be at risk for deterioration. Thus, a person at risk for developing MG may be, for example, someone with a family history of MG and/or someone who is administered or receiving an MG-inducing drug such as D-penicillamine. As used herein, a subject "at risk for developing CAPS" is a subject who has one or more (e.g., two, three, four, five, six, seven, or eight or more) risk factors for developing the disorder. Approximately 60% of CAPS cases are preceded by a precipitating event such as an infection. Thus, risk factors for CAPS include certain cancers (e.g., stomach cancer, ovarian cancer, lymphoma, leukemia, endometrial cancer, adenocarcinoma, and lung cancer), pregnancy, puerperium, transplantation, primary APS, rheumatoid arthritis (RA), systemic lupus erythematosus. Conditions known to precipitate CAPS include, but are not limited to, (SLE), surgery (e.g. eye surgery), and certain infections. Infections include, for example, parvovirus B19 infection and hepatitis C infection. Thereafter, these manifestations of CAPS, e.g. "cancer-associated CAPS", "transplantation-associated CAPS", a person at risk for developing CAPS, e.g. primary CAPS and/or a cancer known to be associated with CAPS There might be someone who has it. It will be apparent from the above that not all subjects "at risk for developing a complement-related disorder" (e.g., an AP-related disorder or a CP-related disorder) are subjects within those species. A subject is someone who has one or more (e.g., two, three, four, five, six, seven, eight, nine, or 10 or more) symptoms of the disease. The symptoms of these disorders will vary depending on the particular disorder but are known to those skilled in the medical art. For example, symptoms of DDD include one or both hematuria and proteinuria; acute nephritic syndrome; development of drusen and/or visual impairment; acquired partial lipodystrophy and its complications; and the presence of serum C3 nephritic factor (C3NeF), an autoantibody directed against C3bBb, C3 convertase of the alternative complement pathway. (See, for example, Appel et al. (2005), supra). Symptoms of aHUS include, for example, severe hypertension, proteinuria, uremia, lethargy/fatigue, irritability, thrombocytopenia, microangiopathic hemolytic anemia, and renal dysfunction (e.g., acute renal failure). Symptoms of TTP, such as microthrombi, thrombocytopenia, fever, low ADAMTS 13 metalIIoproteinase expression or activity, fluctuating central nervous system abnormalities, renal insufficiency, microangiopathic hemolytic anemia, bruising, purpura, nausea and vomiting (e.g., from ischemia in the gastrointestinal tract or central nervous system involvement). These include chest pain, seizures, and muscle and joint pain due to cardiac ischemia. RA symptoms, for example, include erectile dysfunction, bloating, fatigue, anemia, weight loss, fever, and often paralyzing pain. Some common symptoms of rheumatoid arthritis include joint stiffness upon awakening lasting an hour or more; swelling in a specific finger or wrist joint; swelling of the soft tissue around the joints; and involves swelling on both sides of the joint. Bloating may occur with or without pain and may steadily worsen or remain the same for years before progressing. Symptoms of HELLP are known in the medical art and include, for example, fatigue, epigastric pain, nausea, vomiting, headache, right upper quadrant pain, hypertension, proteinuria, blurred vision, gastrointestinal bleeding, hypodevelopment, paresthesia, elevated liver enzymes/liver damage, anemia (hemolytic anemia) and any of these in combination with low platelet count, pregnancy, or recent pregnancy. (See, for example, symptoms of CAPS are well known in the art and include, for example, histopathological evidence of multiple small obstructions; presence of antiphospholipid antibodies (usually in high titer), vascular thromboses, severe multiple organ dysfunction, malignant hypertension, acute respiratory distress syndrome, disseminated intravascular coagulation, microangiopathic include hemolytic anemia, cystocytes, and thrombocytopenia. CAPS can be distinguished from APS in patients with CAPS who present with severe multiple organ dysfunction or failure, often characterized by rapid, diffuse small vessel ischemia and thromboses predominantly affecting parenchymal organs. In contrast, APS is associated with single venous or arterial medium to large blood vessel occlusions. MG symptoms include, for example, a range of conditions related to fatigue and muscle weakness, including: ptosis (of one or both eyes), diplopia, unstable gait, suppressed or distorted facial expressions, and difficulty chewing, speaking, or swallowing. In some cases a subject may present with partial or complete paralysis of the respiratory muscles. Symptoms of CAD include, for example, pain, fever, pallor, anemia, reduced blood flow to the extremities (e.g., with gangrene), and renal disease or acute renal failure. In some embodiments, symptoms may occur following exposure to cold temperatures. Looking above, it will become apparent that subjects "suspected of having a complement-related disorder" are not all subjects within a species in question. Methods may include identifying a subject as having, suspected of having, or at risk of developing a complement-related disorder. Suitable methods for subject identification are known in the art. For example, appropriate methods for determining whether a human subject has a DDD-associated mutation in a CFH, CFHR5, or CS gene are described in (e.g., sequencing techniques or 2034). The existence of electron dense deposits associated with characteristic DDD is also well known in the art. For example, a general practitioner may obtain electron microscopy from a patient and a subject's kidney and tissue biopsy from the subject. The GP may also examine the tissue by immunofluorescence to detect the presence of CS using an anti-C3 antibody and/or light microscopy to determine if membranoproliferative glomerulonephritis is present. See, for example, Walker et al. (2007) in embodiments, identifying a subject as having DDD may include analyzing a blood sample for the presence of C3NeF. Methods for detecting the presence of C3NeF in blood, such as Schwertz et al. (2001) Pediatr Allergy Immunol. It is explained in 12:166-172. The practitioner can determine whether increased complement activation is present in a subject's serum. Signs of increased complement activation include, for example, a decrease in CH50, an increase in C3, and an increase in CSdg/C3d. See, for example, Appel et al. (2005), supra. In some embodiments, a practitioner may examine a subject's eye for evidence of drusen development and/or other visual pathologies such as AMD. For example, a general practitioner may use tests of retinal function such as, but not limited to, dark adaptation, electroretinography, and electrooculography (see, e.g., Colville et al. (2003) Am J Kidney Dis. 42:E2-5). Methods for identifying a subject who has, is suspected of having, or is at risk for the development of TTP are also known in the art. For example, Miyata et al. Methods for measuring ADAMTS13 activity in a biological sample obtained from a subject, detecting ADAMTS13 activity in the subject within phenotypically normal ranges, as well as the presence of inhibitors of ADAMTS13 (e.g., autoantibodies that bind to ADAMTS13) in a suitably obtained biological sample are known in the art. For example, a serum sample from a patient can be mixed with a serum sample from a subject without TTP to detect the presence of anti-ADAMTS13 antibodies. In another example, immunoglobulin protein can be isolated from patient serum and used in in vitro ADAMTS13 activity assays to determine the presence of an anti-ADAMTS13 antibody. See, for example, Dong et al. (2008) Am J Hematol. It can be determined by evaluating whether the patient carries one or more mutations in the ADAMTS13 gene. Suitable methods for detecting a mutation in the ADAMTS13 gene (e.g., nucleic acid sequencing or DNA sequencing) are known in the art and are, for example, described in Levy et al. , supra; Kokme et al. , supra; Licht et al. , supra; and Noris et al. , explained in supra. Additionally, methods for identifying a subject suspected of having or at risk for the development of aHUS are known in the art. For example, laboratory tests may be performed to determine whether a human subject has thrombocytopenia, microangiopathic hemolytic anemia, or acute renal failure. Thrombocytopenia is defined by a medical professional as one or more of the following: a low platelet count; (ii) a decrease in platelet survival reflecting increased platelet fragmentation in the circulation; and (iii) large platelets observed in a peripheral blood smear, consistent with secondary activation of thrombocytopoiesis. Microangiopathic haemolytic anemia may be diagnosed by a general practitioner as one or more of the following: (i) greater than 10 mg/dL (e.g., Level 6). Hemoglobin concentrations less than 5 mg/dL; (ii) increased serum lactate dehydrogenase (LDH) concentrations (460 U/L); (iii) hyperbilirubinemia, reticulocytosis, circulating free hemoglobin, and low or undetectable haptoglobin concentrations; and (iv) detection of fragmented red blood cells (cystocytes) with an angle typical of burr or helmet cells in a peripheral blood smear with a negative Coombs test. (See, for example, Kaplan et al. (1992) "Hemolytic Uremic Syndrome and Thrombotic Thrombocytopenic Purpura," A subject can also be identified as having aHUS by assessment of blood concentrations of C3 and C4 as a measure of complement activation or dysregulation. Additionally, from the above discussion, a subject may be defined as having genetic aHUS by defining the subject as harboring one or more mutations in a gene associated with aHUS, such as CFI, CFB, CFH, or MCP (supra). Suitable methods for detecting a mutation in a gene include, for example, DNA sequencing and nucleic acid sequencing techniques. (See, e.g., Breslin NatI Acad Sci USA 104:240-245. ) Symptom characteristics of TMA, such as fever, microangiopathic hemolytic anemia (cystocytes in a blood smear), renal failure, thrombocytopenia, and neurological manifestations Methods for diagnosing a subject who has, is suspected to have, or is at risk for developing RA are also medical It is known in the technique. For example, a general practitioner may examine the small joints of the hands, wrists, feet and knees to identify inflammation in a symmetrical distribution. The practitioner may also carry out a number of tests to rule out other types of joint inflammation, including arthritis due to infection or gout. Additionally, rheumatoid arthritis is associated with abnormal antibodies in the bloodstream of affected patients. For example, an antibody referred to as "rheumatoid factor" is found in approximately 80% of patients. In another example, anti-citrulline antibody is present in most patients with rheumatoid arthritis and is thus useful in the diagnosis of rheumatoid arthritis when evaluating patients with unexplained joint inflammation. See, for example, van Venrooij et al. (2008) Ann NY is found in patients with arthritis. See, for example, Benucci et al. (2008) Clin Rheumatol A general practitioner may also examine a subject's red blood cell sedimentation rate to help diagnose RA. The sedimentation rate can be used as a crude measure of inflammation of joints and is generally faster during disease spread and slower during remissions. Another blood test that can be used to measure the degree of inflammation present in the body is C-reactive protein. In addition, joint x-rays can also be used to diagnose a subject having rheumatoid arthritis. As RA progresses, x-rays may show bony abrasions in the joints that are typical of rheumatoid arthritis. Joint x-rays can also help monitor disease progression and joint damage over time. A bone scan, a radioactive testing procedure, can show inflamed joints. Methods for identifying a subject as having, suspected of having, or being at risk of developing HELLP are known in the medical art. Hallmark symptoms of HELLP syndrome include hemolysis, elevated liver enzymes, and low platelet count. Thus, various tests can be performed on blood drawn from a subject to determine the level of hemolysis, the concentration of any of various liver enzymes, and the level of platelets in the blood. For example, the presence of cystocytes and/or elevated free hemoglobin, bilirubin, or serum LDH levels is an indicator of intravascular hemolysis. Routine laboratory testing may be used to determine platelet count as well as blood levels of liver enzymes such as, but not limited to, aspartate aminotransferase (AST) and alanine transaminase (ALT). Suitable methods for identifying a subject as having HELLP syndrome are also described, for example, by Sibai et al. (1993), supra; Martin et al. (1990), supra; Padden (1999), supra; and Gleicher and Buttino (1998) “Principles & Practice explained. Appropriate methods for identifying the subject with MG may be qualitative or quantitative. For example, a general practitioner may examine the status of a subject's motor functions using a physical examination. Other qualitative tests include, for example, an ice pack test, in which an ice pack is applied to a subject's eye (in the case of ocular MG) to determine whether one or more symptoms develop from cold, such as the "sleep test", which is linked to a predisposition for symptoms of GM to develop the rest below. " includes. In some embodiments, quantitative or semi-qualitative tests may be administered by a practicing physician to determine whether a subject has, is suspected to have, or is at risk of developing MG. For example, a medical practitioner may perform a test to detect the presence or amount of autoantibodies associated with MG in a serum sample obtained from a subject. Autoantibodies associated with MG include, for example, antibodies that bind to and modulate the activity of the acetylcholine receptor (AChR), muscle-specific receptor tyrosine kinase (MuSK), and/or striatal protein. (See, for example, Conti-Fine et al. (2006), supra). Suitable assays useful for detecting the presence or amount of an MG-associated antibody in a biological sample are known in the art and are, for example, described in Hoch et al. (2001) Nat Med 7:365- Additional methods for diagnosing MG include electrodiagnostic testing (e.g., single fiber electromyography) and Tensilon (or Includes the edrophonium test. See, for example, and "Guidelines in Electrodiagnostic Medicine." American Association of Electrodiagnostic Medicine,” Muscle Nerve 15:229-253. A subject can be identified as having CAD, which uses an assay to detect the presence or amount (titer) of autoantibodies that bind to antigen I on red blood cells. May be identified as having CAD using one or more of a complete blood cell count (CBC), urinalysis, biochemical studies, and a Coombs test to test for antibodies, monoclonal (for example, monoclonal IgM or For example, biochemical studies can be used to detect the presence of elevated lactase dehydrogenase levels, elevated unconjugated bilirubin levels, low haptoglobin levels, and/or free plasma hemoglobin, all of which may indicate acute hemolysis. Other tests that can be used to detect CAD include determining complement levels in serum. For example, measured plasma complement levels (e.g., O2, CS, and C4) are reduced in CAD due to its consumption during the acute phase of hemolysis. Typical (or infectious) HUS rather than aHUS can often be identified by a prodrome of diarrhea, often bloody in nature, resulting from infection with a shig-toxin-producing microorganism. A subject may be identified as having typical HUS if Shiga toxins and/or serum antibodies to Shiga toxin or LPS are detected in a person's stool. Suitable methods for testing anti-shiga toxin antibodies or LPS are known in the art. For example, methods for detecting antibodies that bind to shiga toxins Stx1 and Stx2 or LPS in humans are described, for example, in Ludwig et al. (2001) J Symptoms of this condition are known to those skilled in the medical art and include, for example, pain, fever, pallor, jaundice, hemoglobinemia, anemia, and renal disease or acute renal failure. In some embodiments, symptoms may occur following exposure to cold temperatures. The methods may include identifying the subject who has, is suspected of having, or is at risk of developing PCH. Suitable methods for subject identification are known in the art. For example, a subject may be identified as PCH using a Donath-Landsteiner test, which is an assay to detect the presence of Donath-Landsteiner antibody in a subject's serum. The procedure requires - (1) serum of the subject; (2) normal serum; and (3) incubating three samples of a mixture of the subject's serum and normal serum with P-antigen expressing blood red cells at 0 to 4°C. The sample is then heated to 37°C and visually inspected for hemolysis. Hemolysis should occur in samples of (1) and (3) if Donath-Landsteiner antibody is present, but (2) can be diagnosed as having PCH using one or more of biochemical studies and a Coombs test. For example, biochemical studies can be used to detect the presence of elevated lactase dehydrogenase levels, elevated unconjugated bilirubin levels, low haptoglobin levels, and/or free plasma hemoglobin, all of which may indicate acute hemolysis. Other tests that can be used to detect PCH include determining complement levels in serum. For example, measured plasma complement levels (e.g., O2, CS, and C4) are reduced in PCH due to consumption during the acute phase of hemolysis. See also, eg, Nordhagen Transfusion 41 (8):1073-4. The composition may be administered to a subject prophylactically to prevent recurrence or recurrence of PCH. For example, a composition disclosed herein may be administered to a subject with a pre-existing Mycoplasma infection or newly diagnosed with a PCH-associated neoplasm to prevent or reduce the severity of recurrence of PCH. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, a CS inhibitor described herein (e.g., an anti-CS antibody) may be administered to a subject as a monotherapy. Alternatively, as described above, the antibody may be administered to a subject with another treatment, such as another treatment for DDD, TTP, aHUS, RA, HELLP, MG, CAD, CAPS, tHUS, Degos disease, or any other complement-related disorder described herein. For example, combination therapy is the administration of one or more additional agents (e.g., anticoagulants, anti-hypertensives, or corticosteroids) that provide a therapeutic benefit to a subject (e.g., a human patient) who has or is at risk of developing DDD (e.g., a human patient). may include administration to a human patient. In some embodiments, the combination therapy may include administering to the subject (e.g., a human patient) a CS inhibitor (e.g., an anti-CS antibody or an anti-CSa antibody) and an immunosuppressive agent such as Remicade® for use in treating RA. In some embodiments, the CS inhibitor and one or more additional active agents are administered at the same time. In other embodiments, a CS inhibitor is administered first and one or more additional active agents are administered second. In some embodiments, one or more additional active agents are administered first and the C5 inhibitor is administered second. A C5 inhibitor described herein (e.g., an anti-C5 antibody) may replace or augment a previously or currently administered therapy. For example, following treatment with an anti-C5 antibody, the administration of one or more additional active agents may be stopped or reduced, e.g., administered at low levels. In some embodiments, the application of previous treatment may be continued. In some embodiments, a prior treatment will be continued until the level of C5 inhibitor (e.g., an anti-C5 antibody or an anti-C5a antibody) reaches a level sufficient to provide a therapeutic effect. The two treatments can be applied in combination. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, a C5 inhibitor may be administered chronically to a patient. For example, a patient being treated chronically with a complement-inhibiting agent (e.g., a C5 inhibitor or a C5a inhibitor) should be administered at a dosing frequency sufficient to maintain a concentration of the agent in the patient's blood that inhibits or substantially inhibits systemic complement activity in the patient. and may be treated with an amount of agent for a period greater than or equal to (for the remainder of 2 weeks). To maintain systemic complement inhibition in a patient, a C5 inhibitor may be administered chronically to the patient, such as once a week, once every two weeks, twice a week, once a day, once a month, or once every three weeks. In some embodiments of any of the methods disclosed herein, the C5 inhibitor may be administered to a patient at an administration frequency and in an amount effective to maintain a concentration of at least: 0 per C5 molecule in the patient's blood. 7 (e.g., at least 0. 8, 0. 9, one, two, three, four, five, six, seven, eight, nine, or 10 or more) bivalent C5 inhibitor (e.g., a whole antibody) molecule(s); or three, four, five, six, seven, eight, nine, or 10 or more) monovalent C5 inhibitor (e.g., a single chain anti-C5 antibody or a Fab fragment of the antibody) molecule(s). For example, in some embodiments, a monovalent anti-C5 antibody (e.g., a single chain antibody or a Fab antibody fragment) may be administered to a patient at a frequency and in an amount effective to maintain a concentration of at least anti-C5 antibody per C5 molecule in the blood. In some embodiments of any of the methods disclosed herein, an anti-C5 antibody is administered to the patient at a frequency and in an amount effective to maintain a concentration of at least excess µg of the antibody per milliliter of the patient's blood. Exemplary chronic dosing strategies are described here (see, e.g., Tables 1 and 2). The following embodiments on this page are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, the C5 inhibitor (or C5a inhibitor) may be administered to a subject even after improvement of one or more symptoms. Monitoring a subject (e.g., a human patient) for a complement-related disorder, as defined herein, means evaluating the subject for a change in a disease parameter, such as an improvement in one or more symptoms of the disease. Such symptoms include any of the symptoms of complement-related disorders described herein. In some embodiments, the evaluation is performed at least 1 hour, day, 20 days or more, or at least 1 week, 2 weeks, 4 weeks, 10 weeks, 13 weeks, weeks or more after an administration. The subject may be evaluated at one or more of the following periods: before starting treatment; during treatment or after one or more elements of the treatment applied. Evaluation may include assessing the need for additional treatment, for example, assessing whether a dosage, frequency of administration, or duration of treatment needs to be changed. This may also include the need to add or remove a selected therapeutic modality, for example, the need to add or remove any of the treatments for any of the complement-related disorders. It can be administered chronically to a patient who requires it in a frequency and in an amount effective to reduce and maintain hemolytic activity. See, for example, Hill et al. (2005)Blood 106(7):2559. In some embodiments, the complement inhibitor may be administered to a patient at a frequency and in an amount effective to maintain serum lactate dehydrogenase (LDH) levels within the normal range for LDH. See Hill et al. (2005) supra. is administered to the patient at a frequency and in an amount effective to maintain a lower serum LDH level. In some embodiments, administration of a C5 inhibitor (e.g., an anti-C5 antibody such as eculizumab) or a C5a inhibitor (e.g., an anti-C5a antibody) results in improvement of one or more of a patient's symptoms within 3, 2, or 1 even. For example, elevated blood pressure in a (chronically treated) aHUS patient treated with an anti-C5 antibody can be reduced to a level that is within 40% of what is normal for the patient's age, race, height, weight, gender, and physical health. The complement inhibitor (e.g., a C5 inhibitor or C5a inhibitor) may be administered to a subject even after the patient has entered clinical remission. Determining clinical remission of a complement-related disorder is within the capabilities of a person skilled in medicine. For example, elements that are predictive of clinical remission for aHUS are described. The disclosure also provides methods for allogeneic organ or tissue transplantation. The method includes implanting an organ or tissue into a patient in need thereof, wherein prior to and following the implantation a C5 inhibitor is administered to the patient at a frequency and in an amount effective to substantially inhibit systemic complement activity in the patient. The C5 inhibitor (e.g., anti-C5 antibody) as described herein is administered at a frequency to maintain a concentration of at least one C5 inhibitor molecule per C5 molecule (e.g., at least one anti-C5 antibody) in the patient's blood. The following embodiments are with the sentence structure of the claims. It is not covered, but is considered useful for understanding the invention. In some embodiments, a monovalent anti-C5 antibody (e.g., a single chain antibody or a Fab antibody fragment) may be administered to a patient in an amount with a frequency effective to maintain a concentration of the monovalent anti-C5 antibody in the blood (more than C5). In some embodiments, the C5 inhibitor (e.g., anti-C5 antibody) may be administered to the patient at a frequency and in an amount to maintain a concentration of µg of the inhibitor (e.g., anti-C5 or more) in the patient's blood. In some embodiments, the anti-C5 antibody (e.g., is administered to the patient in less than an hour. In some embodiments, the methods also include placing the donor organ before contact (e.g., fluid immersion) with a C5 inhibitor (e.g., an anti-C5 antibody such as eculizumab) for a period of time and under conditions that inhibit complement activation in the organ or tissue after transplantation. or tissue. The organ may be, for example, a kidney, heart, lung, limb (e.g. finger or toe) or liver. In some embodiments, the methods may include administering a C5 inhibitor (e.g., an anti-C5 antibody) to the donor patient prior to removal of the organ or tissue for transplantation. The patient may have, be at risk of developing, or be suspected of having aHUS. In some embodiments, at least 700 (e.g., at least 710) of the anti-C5 antibody are administered to the patient. In some embodiments, the anti-C5 antibody is administered chronically to the patient following implantation. For example, anti-C5 antibody may be administered chronically to the patient for at least the following dosing schedule: at least 700 or 1200 or more mg of anti-C5 antibody less than 24 hours after organ or tissue implantation; initial postoperative - four weeks after the transplant dose; at least 700 (e.g., at least 710, more) mg of anti-C5 antibody once during the fifth week; and thereafter for the remainder of the dosing schedule, administer the anti-C5 antibody in a twice-weekly setting, with at least 900 mg of the antibody administered for the first four doses; 1200 mg administered in the fifth week; and 1200 mg thereafter for the remainder of the chronic treatment schedule. It is applied to the patient twice a week. Additional exemplary dosing schedules are provided in Tables 1 and 2. The following embodiments are not covered by the sentence structure of the claims, but are considered useful for understanding the invention. In some embodiments, the methods include administering an immunosuppressant to the patient. Suitable immunosuppressants for use in the methods are ATG or ALG, OKT3, daclizumab, basiliximab, corticosteroids, 15-deoxypergualin, cyclosporines, tacrolimus, azathioprine, methotrexate, mycophenolate mofetil, 6-mercaptopurine, bredinin, brequinar, leflunamide, cyclophosphamide, sirolimus, anti-CD4. monoclonal antibodies, CTLA4-monoclonal antibodies, anti-CD2 monoclonal antibodies, and anti-CD45 antibodies. Types of organs or tissues that can be implanted using the methods described here, such as heart, kidney, lung, pancreas, liver, vascular tissue, eye, cornea, lens, skin, bone marrow, muscle, connective tissue, gastrointestinal tissue, nervous tissue, bone, root. cells include cartilage, hepatocytes and hematopoietic cells. In some embodiments, transplant methods will result in graft extension in the recipient patient for at least one month (e.g., three, four, five, six, seven, even). Ex VIVO approaches. An ex vivo strategy for treating or preventing a complement-associated disorder (e.g., an AP-associated disorder or a CP-associated disorder) described herein involves using a complement inhibitor (e.g., which binds and promotes the inactivation of a CS mRNA in a mammalian cell). This may involve transfecting or transferring one or more cells obtained from a subject with a polynucleotide encoding an anti-CS antibody, anti-CSa antibody, or a nucleic acid (e.g., an siRNA). For example, cells may be transfected with a single vector encoding a heavy and light chain of an anti-CS antibody, or cells may be transfected with a first vector encoding a heavy chain and a second vector encoding a light chain of the antibody. The transfected or transferred cells are then returned to the subject. The cells can be any of several types, including, but not limited to, hematopoietic cells (e.g., bone marrow cells, macrophages, monocytes, dendritic cells, T cells or B cells), fibroblasts, epithelial cells, endothelial cells, keratinocytes, or muscle cells. These cells may serve as a source (e.g., sustained or periodic source) of CS inhibitor (e.g., anti-CS antibody, anti-CSa antibody, or nucleic acid (above)) as long as they survive in the subject. In some embodiments, vectors and/or cells may be configured for inducible or repressible expression of the CS inhibitor (see, e.g., Schockett et al. Preferably the cells are obtained from the subject (autologous), but can potentially be obtained from a subject of the same species as the subject (allogeneic). Suitable methods for obtaining cells from a subject or transferring or transfecting cells are known in the art of molecular biology. For example, the transduction step can be completed by any of the standard pathways used for ex vivo gene therapy, including calcium phosphate, lipofection, electroporation, viral infection (see above), and biolistic gene transfer. (See, for example, Sambrook et al. (supra) and Ausubel et al. (1992), liposomes or polymeric microparticles can be used. Successfully transduced cells can be selected, for example, for expression of the sequence encoding a drug resistance gene. Kits The description not covered by the sentence structure of the claim also includes articles of manufacture or kits containing a container with a label; and one or more complement inhibitors disclosed herein. For example, the kit may contain one or more of an anti-CSa antibody, an anti-CS antibody, and a nucleic acid (e.g., an siRNA or antisense nucleic acid) that binds and promotes the inactivation of a CS mRNA in a mammalian cell. The label indicates that the compound is not associated with DDD, aHUS, TTP, HELLP, RA, AMD, tHUS, MG, CAD, PCH, CAPS, Degos disease, or any other complement pathway-related disorder described herein (e.g., an AP or CP-related disorder). Indicates that it will be administered to a subject who has, is suspected of having, or is at risk of developing a complement-related disorder. The kit may optionally include a means for administering the control composition. For example, the kit may include one or more syringes. The kits may also contain one or more additional active agents, such as any of those described herein. For example, kits may contain one or more corticosteroids, anti-hypertensives, immunosuppressives, and anti-seizure agents. The following examples are intended to illustrate the invention and are not intended to limit it. A human adult patient is defined by a general practitioner as having an inherited form of aHUS. Once a week for four weeks, the patient is administered a composition containing eculizumab at a dose of 900 mg. The patient is then given at least 1200 mg of eculizumab once during the fifth week and then at least 1200 mg of eculizumab twice a week. The patient and the practitioner observe a significant improvement in at least two known symptoms of aHUS during initial treatment. Eculizumab is administered to the patient chronically, even after the general practitioner has determined that aHUS is in remission. A patient weighing around kg is defined by a general practitioner as having aHUS. Once a week for two weeks, the patient is administered a composition containing eculizumab at a dose of at least 600 mg. The patient is then given at least 600 mg of eculizumab once during the third week and at least 600 mg of eculizumab twice weekly thereafter. The patient and the practitioner observe a significant improvement in at least two known symptoms of aHUS during initial treatment. Eculizumab is administered chronically to the patient, even after the general practitioner has determined that aHUS is in remission, to prevent relapse of aHUS in the patient. A human patient weighing around kg is defined by a general practitioner as having CAPS. Once a week for two weeks, the patient is administered a composition containing eculizumab at a dose of at least 600 mg. The patient is then given at least 900 mg of eculizumab once during the third week and at least 900 mg of eculizumab twice weekly thereafter. The patient and the practitioner observe a significant improvement in at least two known symptoms of CAPS during initial treatment. Eculizumab is administered chronically to the patient even after the practitioner has determined that CAPS is in remission to prevent or greatly reduce the likelihood of the patient's CAPS relapse. A patient weighing around 7 kg is defined by a general practitioner as having aHUS. The patient has TMA in his kidneys as a result of aHUS. For one week, the patient is administered a composition containing eculizumab at a dose of at least 300 mg. The patient is then given at least 300 mg of eculizumab every three weeks thereafter and at least 300 mg of eculizumab once during the second week. The patient and the practitioner observe a significant improvement in at least two known symptoms of aHUS during initial treatment. The general practitioner also observes that TMA has dissolved in the patient's kidneys and that new TMA has not appeared while the patient is chronically administered eculizumab. Eculizumab is administered chronically to the patient, even after the GP has determined that aHUS is in remission, to prevent or greatly reduce the likelihood of the patient having a relapse of aHUS and any additional damage to the person's kidneys that could result from a relapse. A human patient in need of a kidney transplant is administered eculizumab intravenously at a dose of 1200 mg less than 24 hours before the transplant operation. An allogeneic kidney is implanted into the patient. Less than 24 hours before the kidney transplant, the patient is administered another 1200 mg of eculizumab. Following the first post-operative dose of eculizumab, the patient is given 900 mg of eculizumab once a week for four weeks. The patient is given 1200 mg of eculizumab at week five after the initial post-operative dose of eculizumab and is then continued on a dosing schedule that includes 1200 mg of eculizumab twice weekly thereafter. The general practitioner observes a significant improvement in the survival of the implanted kidney in the patient. TR TR TR TR TR