Classifications

• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
  • C07K7/04—Linear peptides containing only normal peptide links
  • C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P9/00—Drugs for disorders of the cardiovascular system
  • A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
  • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
  • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
  • C07K16/28—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
  • A61K39/00—Medicinal preparations containing antigens or antibodies
  • A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
  • A61K39/00—Medicinal preparations containing antigens or antibodies
  • A61K2039/57—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
  • A61K38/00—Medicinal preparations containing peptides
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
  • A61K39/00—Medicinal preparations containing antigens or antibodies
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K2317/00—Immunoglobulins specific features
  • C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
  • C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K2317/00—Immunoglobulins specific features
  • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
  • C07K2317/52—Constant or Fc region; Isotype

Definitions

• Figure 7C is a series of photomicrographs showing the absence of IgM and complement C3 or C4 within the microvilli of P8-treated animals.
• Representative cryosections of intestinal tissues were harvested following intestinal RL
• Panels i-viii are IgM CM"22 reconstituted RAG-l " mice without pretreatment with P S (panels i-iv) or with P8 (panels v-viii).
• Panels represent cryosections from the intestines of WT without P8 (panels ix - xii) or pretreated with P8 (panels xiii - xvi).
• Figure 14 shows the (A) nucleic acid sequence (SEQ ID NO: 53; Genbank Accession no. NM_005964) and (B) amino acid sequence (SEQ ID NO: 54; Genbank Accession no. NP_005955) of human non-muscle myosin heavy chain II-B (hNMHC-IIB).
• Figure 15 shows the (A) nucleic acid sequence (SEQ ID NO: 55; Genbank
• the coding sequences need not be contiguous to one another so long as the expressed sequences ultimately process to produce the desired protein.
• An expression control sequence operatively linked to a coding sequence is ligated such that expression of the coding sequence is achieved under conditions compatible with the expression control sequences.
• expression control sequences refers to nucleic acid sequences that regulate the expression of a nucleic acid sequence to which it is operatively linked. Expression control sequences are operatively linked to a nucleic acid sequence when the expression control sequences control and regulate the transcription and, as appropriate, translation of the nucleic acid sequence.
• an isolated nucleic acid can comprise an IgM CM"22 (or 22A5 IgM) heavy chain variable region nucleotide sequence having a nucleotide sequence as shown in Figure 1 A (SEQ ID NO: 1), or a sequence, which is at least 80%, 90%, 95%, 96%, 97%, 98%o, or 99% identical to SEQ ID NO: 1.
• a nucleic acid molecule may comprise the heavy chain CDR1 nucleotide sequence of SEQ ID NO: 3, or a portion thereof. Further, the nucleic acid molecule may comprise the heavy chain CDR2 nucleotide sequence of SEQ ID NO: 5, or a portion thereof.
• the nucleic acid molecule comprises a light chain CDRl nucleotide sequence of SEQ ID NO: 9, or portion thereof, and a light chain CDR2 nucleotide sequence of SEQ ID NO: 11 , or portion thereof.
• the nucleic acid molecules of the present invention may comprise light chain sequences, e.g. SEQ ID NOs: 7, 9 or 11, or combinations thereof, or encompass nucleotides having at least 80%, 90%, 95%, 96%, 97 %, 98%, and 99% sequence identity to SEQ ID NOs: 7, 9 or 11.
• Further nucleic acid molecules may comprise light chain sequences, which hybridize under stringent conditions, e.g.
• Chimeric antibodies e.g. mouse-human monoclonal antibodies
• Chimeric antibodies can be produced by recombinant DNA techniques known in the art. For example, a gene encoding the Fc constant region of a murine (or other species) monoclonal antibody molecule is digested with restriction enzymes to remove the region encoding the murine Fc, and the equivalent portion of a gene encoding a human Fc constant region is substituted, (see Robinson et al., International Patent Publication PCT/US86/02269; Akira, et al., European Patent Application 184,187; Taniguchi, M., European Patent Application 171,496; Mo ⁇ ison et al., European Patent Application 173,494; Neuberger et al., International Application WO 86/01533; Cabilly et al.
• the method includes: altering the sequence, e.g., by substitution or deletion of one or more residues, of a pathogenic immunoglobulin, e.g., altering the sequence of a non-conserved region, or a domain or residue described herein, and testing the altered polypeptide for the desired activity.
• the modified natural immunoglobulin may have a reduced ability to activate complement. For example, one or more of the amino acid residues involved in complement binding and/or activation are mutated.
• a change e.g., decrease in the level of binding between the natural IgM antibody and the antigen or the component of the complement pathway in the presence of the test compound relative to that detected in the absence of the test compound indicates that the test compound is an inhibitor of the interaction between the natural IgM antibody and the antigen or the component of the complement pathway.
• the method can further include pre-treating the natural IgM antibodies with one or more test compounds.
• the pre-treated natural IgM antibodies can then be injected into mice deficient in natural immunoglobulins.
• the methods is perfo ⁇ ried in vitro.
• the contacting step is effected in vivo.
• the antigen is myosin.
• the aliquots of derivatized beads are then washed, "pooled” (i.e., recombined), and the pool of beads is again divided, with each aliquot being placed in a separate reaction vessel.
• Another activated amino acid is then added to each aliquot of beads. The cycle of synthesis is repeated until a desired peptide length is obtained.
• Activated cells are hybridized with fusion partner myeloma cells in the presence of PEG and grown in HAT-selective medium.
• Hybridomas are screened for IgM secreting clones by ELISA , and positive wells are expanded for purification of IgM.
• Twenty-two IgM-secreting hybridoma clones were analyzed by pooling an equal amount of IgM product from each of the clones.
• Treatment of antibody-deficient mice with the pooled IgM restored injury similar to that seen with pooled IgM from serum. This finding confirmed that the pathogenic IgM was among the twenty-two hybridomas produced.

Landscapes

• Chemical & Material Sciences (AREA)
• Health & Medical Sciences (AREA)
• Organic Chemistry (AREA)
• General Health & Medical Sciences (AREA)
• Life Sciences & Earth Sciences (AREA)
• Medicinal Chemistry (AREA)
• Immunology (AREA)
• Proteomics, Peptides & Aminoacids (AREA)
• Molecular Biology (AREA)
• Biochemistry (AREA)
• Genetics & Genomics (AREA)
• Biophysics (AREA)
• Chemical Kinetics & Catalysis (AREA)
• Pharmacology & Pharmacy (AREA)
• Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
• Animal Behavior & Ethology (AREA)
• Engineering & Computer Science (AREA)
• Public Health (AREA)
• Veterinary Medicine (AREA)
• Bioinformatics & Cheminformatics (AREA)
• General Chemical & Material Sciences (AREA)
• Vascular Medicine (AREA)
• Urology & Nephrology (AREA)
• Cardiology (AREA)
• Heart & Thoracic Surgery (AREA)
• Pain & Pain Management (AREA)
• Rheumatology (AREA)
• Peptides Or Proteins (AREA)
• Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
• Micro-Organisms Or Cultivation Processes Thereof (AREA)
• Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
• Preparation Of Compounds By Using Micro-Organisms (AREA)

Priority Applications (8)

Applications Claiming Priority (4)

Publications (2)

Family

ID=34922704

Family Applications (1)

Country Status (9)

Cited By (2)

Families Citing this family (5)

Family Cites Families (60)

• 2005
  • 2005-03-01 CA CA002560066A patent/CA2560066A1/en not_active Abandoned
  • 2005-03-01 DE DE602005026260T patent/DE602005026260D1/de not_active Expired - Lifetime
  • 2005-03-01 JP JP2007501869A patent/JP5557982B2/ja not_active Expired - Fee Related
  • 2005-03-01 AT AT05723931T patent/ATE498010T1/de not_active IP Right Cessation
  • 2005-03-01 EP EP05723931A patent/EP1725659B1/en not_active Expired - Lifetime
  • 2005-03-01 AU AU2005219839A patent/AU2005219839B9/en not_active Ceased
  • 2005-03-01 WO PCT/US2005/006276 patent/WO2005085288A2/en not_active Ceased
  • 2005-03-01 US US11/069,834 patent/US7442783B2/en not_active Expired - Lifetime
  • 2005-03-01 EP EP10185693.8A patent/EP2290077B1/en not_active Expired - Lifetime
• 2006
  • 2006-08-31 IL IL177825A patent/IL177825A/en not_active IP Right Cessation
• 2008
  • 2008-10-28 US US12/259,767 patent/US20090176966A1/en not_active Abandoned
• 2011
  • 2011-02-01 JP JP2011019668A patent/JP5618852B2/ja not_active Expired - Fee Related
• 2013
  • 2013-04-09 US US13/859,054 patent/US9657060B2/en not_active Expired - Fee Related
• 2014
  • 2014-04-24 JP JP2014089965A patent/JP2014155497A/ja active Pending
• 2015
  • 2015-07-23 US US14/806,924 patent/US9914751B2/en not_active Expired - Lifetime
• 2017
  • 2017-05-08 US US15/588,933 patent/US20170342109A1/en not_active Abandoned

Also Published As

Similar Documents

Legal Events