WO2005053742A1 - 抗体組成物を含有する医薬 - Google Patents
抗体組成物を含有する医薬 Download PDFInfo
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- WO2005053742A1 WO2005053742A1 PCT/JP2004/018441 JP2004018441W WO2005053742A1 WO 2005053742 A1 WO2005053742 A1 WO 2005053742A1 JP 2004018441 W JP2004018441 W JP 2004018441W WO 2005053742 A1 WO2005053742 A1 WO 2005053742A1
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- Prior art keywords
- antibody
- linked
- fucose
- antibody composition
- sugar chain
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
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- 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
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/04—Antineoplastic agents specific for metastasis
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
Definitions
- the present invention relates to a total N-glycoside-linked complex type sugar chain that binds to the Fc region contained in the antibody composition, of the sugar chain in which fucose is not bound to N-acetyltylcolasamine at the reducing end of the sugar chain.
- antibody composition ratio is 50% or more, relates to a pharmaceutical comprising a combination of at least one agent.
- ADCC activity Antibody-dependent cytotoxic activity
- NK cells induce strong ADCC activity through FcyRIIIa, a type of Fey receptor on cells.
- the FcyRIIIa gene has a functional polymorphism at the 158th amino acid, and the 158th amino acid has Valine (hereinafter referred to as Val) Fc ⁇ Rllla more than Phenylalanine (hereinafter referred to as Phe) FcyRIIIa Induces strong ADCC activity [Journal of Clinical Investigation. Clin. Invest.), 100, 1059-1070 (1997)].
- glycoproteins such as antibodies are linked to asparagine (N-glycoside-linked sugar chains) and sugar chains linked to serine, threonine, etc. (0-glycosyl-linked sugars) depending on the mode of binding to the protein part. Chains).
- N- glycoside-linked sugar chain the following structural formula have a common core structure underlying shown in (I) [Biochemical Experimental Methods 2 3 - glycoprotein sugar chain research methods (Gakkai Shuppan Center) Reiko Takahashi Hen (1989 Year) ] .
- Antibody molecules are composed of tetramers in which two heavy and two light chains are associated.
- a sugar chain having the above core structure is bound to asparagine at position 297 from the N-terminus existing in the Fc region of the heavy chain.
- fucose may be added to the non-reducing terminal side at the 6-position of N-acetyldarcosamine, galactose, sialic acid, and the reducing terminal N-acetyldarcosamine, respectively.
- These components are not homogeneous and vary with the antibody-producing cells [Trends Biotechnol., 15, 26-32 (1997)].
- An object of the present invention is to provide a drug using an antibody composition having a high therapeutic effect and at least one drug.
- the present invention relates to the following (1) to (14).
- an antibody composition is proportion 50% or more, a pharmaceutical including a combination of at least one agent.
- an antibody composition is proportion 50% or more, a medicament for administration in combination with at least one agent.
- Fucose binds to ⁇ -acetyl dalcosamine at the reducing end of the sugar chain in the total ⁇ -daricoside bond complex type sugar chain in which the antibody composition binds to the Fc region contained in the antibody composition.
- the sugar chain to which fucose is not bonded is a sugar chain in which the 1-position of the fucose is not bonded to the 6-position of ⁇ ⁇ -glycidylcosamine at the reducing end of ⁇ -glycoside-linked complex type sugar chain.
- the medicament according to any one of the above (1) to (7).
- cytokine is a cytokine selected from IFN-V, IL-2 and IL-15.
- a drug comprising a combination of an antibody composition having a sugar chain content of not less than 50% and at least one drug, a total ⁇ -daricoside binding complex that binds to the Fc region contained in the antibody composition
- antibodies sets the proportion of the chain is 50% or more Pharmaceuticals for the simultaneous or sequential administration of the composition and at least one agent.
- the drug in combination refers to fucose at the reducing end of glycine-linked glycoside of glycine-linked glycoside, which is bound to the Fc region contained in the antibody composition.
- a drug is prepared by separately preparing an antibody composition having an unbound sugar chain ratio of 50% or more and at least one drug, and simultaneously or sequentially administering these drugs in combination.
- a mixture of the respective drug components In the mixture prepared by mixing the respective drug components, among the total ⁇ ⁇ -glycoside-linked complex-type sugar chains binding to the Fc region contained in the antibody composition, ⁇ -acetylmethylcolasamine at the reducing end of the sugar chain was added.
- a fusion antibody in which at least one drug is bound to an antibody composition in which the ratio of sugar chains to which fucose is not bound is ⁇ )% or more is also included.
- the ratio of sugar chains in which fucose is not linked to N-acetyltyl glucosamine at the sugar chain reducing end, of all N-daricoside-linked complex type sugar chains that bind to the Fc region contained in the antibody composition refers to that the fucose is not bound to N-acetyldarcosamine at the reducing end of the sugar chain with respect to the total number of all N-glycoside-linked complex type sugar chains that bind to the Fc region contained in the composition.
- the ratio of the sugar chain is preferably such that the 1-position of fucose is not a-bonded to the 6-position of N-acetyldarcosamine at the reducing end of the sugar chain.
- a sugar chain in which fucose is not bonded to N-acetyldarcosamine at the N-glycoside-linked complex type sugar chain reducing terminal is defined as the N-glycoside-linked complex type sugar chain reducing terminal at the N-glycoside-linked complex type sugar chain reducing end.
- -Acetyl danolecosamine refers to a sugar chain that is not ⁇ - linked. Specifically, position 1 of the fucose is ⁇ - linked to position 6 of ⁇ -acetyldarcosamine of the ⁇ -glycoside-linked complex type sugar chain. If not linked, sugar chains can be mentioned.
- the antibody composition of the present invention includes any composition as long as it contains an antibody molecule having an ⁇ -daricoside-linked complex type sugar chain in the Fc region.
- An antibody molecule is a tetramer in which two types of heavy chains and light chains (hereinafter, referred to as H chains and L chains, respectively) are associated with two molecules of each. About one-fourth of the N-terminal side of the H chain and about one-half of the N-terminal side of the L chain (each more than 100 amino acids) are called V regions, and are rich in diversity and can bind to antigens. Directly involved. Most of the part other than the V region is called the C region.
- Antibody molecule is C region IgG by homology, I g M, IgA, IgD , are BunYasushi to each class of IgE.
- the IgG class by homology C region are further classified into subclasses IgGl ⁇ I g G4.
- the H chain is divided into four immunoglobulin domains, VH, CH1, CH2, and CH3, from the N-terminal side.
- Can be Structural unit comprising CH2 and CH 3 after the hinge region is called Fc region, N- glycoside-linked sugar chain is attached. This region is the region where Fc receptors, traps, etc. bind (Immunology Illustrated, Original 5th Edition, published February 10, 2000, Nankodo Edition, Introduction to Antibody Engineering, January 25, 1994) First edition, Citizen Library).
- the sugar chains of glycoproteins such as antibodies can be linked to asparagine (N-glycoside-linked sugar chains) and sugar chains linked to serine, threonine, etc. (0-glycosyl-glycoside), depending on the mode of binding to the protein part. )
- N-glycoside-linked sugar chain has a basic common core structure represented by the following structural formula (I) [Biochemical Experimental Method 23—Glycoprotein Glycan Research Method (Society Press Center), edited by Reiko Takahashi ( 1989)]. .
- the terminal of the sugar chain binding to asparagine is called a reducing end, and the opposite side is called a non-reducing terminal.
- any one having a core structure of the above structural formula (I) may be used, but a high mannose type in which only mannose is bonded to the non-reducing end of the core structure, and a non-core structure having a core structure It has one or more parallel branches of galactose-N-acetyldarcosamine (hereinafter referred to as Gal-GlcNAc) at the reducing end, and sialic acid and piecing at the non-reducing end of Gal-GlcNAc.
- Gal-GlcNAc galactose-N-acetyldarcosamine
- complex-type (complex type) having a structure such as N-acetyldarcosamine, and a hybrid type having both high-mannose type and complex type branches on the non-reducing end side of the core structure.
- the Fc region of the antibody molecule has a region in which N-daricoside-linked sugar chains bind one by one, two sugar chains are bound per antibody molecule. Since the N-darcoside-linked sugar chain that binds to the antibody molecule includes any sugar chain containing the core structure represented by the structural formula (I), two N-darcoside-linked sugar chains that bind to the antibody are included. Has many combinations of sugar chains.
- the antibody composition according to the present invention may be composed of an antibody molecule having a single sugar chain structure or an antibody having a plurality of different sugar chain structures as long as the effects of the present invention can be obtained. It may be composed of molecules.
- Antibody molecules include any molecules that contain the Fc region of the antibody. Specific examples include an antibody, an antibody fragment, and a fusion protein containing an Fc region.
- Antibodies include hybridoma cells prepared from spleen cells of immunized animals by immunizing animals with the antigen. And an antibody produced by a gene recombination technique, that is, an antibody obtained by introducing an antibody expression vector containing an antibody gene into a host cell. Specific examples include antibodies produced by humans and hybridomas, humanized antibodies, human antibodies, and the like. Hybridomas have a desired antigen specificity, obtained by cell fusion of B cells obtained by immunizing a mammal other than human with an antigen and myeloma cells derived from mice, rats, and the like. A cell that produces a monoclonal antibody.
- humanized antibody examples include a human chimeric antibody and a human CDR-grafted antibody.
- the human chimeric antibody is composed of a non-human animal H chain V region (hereinafter also referred to as HV or VH) and an antibody L chain V region (hereinafter also referred to as LV or VL) and a human antibody H chain C region (hereinafter referred to as LV or VL).
- HV or VH non-human animal H chain V region
- LV or VL antibody L chain V region
- LV or VL human antibody H chain C region
- CL human antibody L chain C region
- any animal such as a mouse, a rat, a hamster, and a rabbit can be used as long as it can produce a hybridoma.
- the human chimeric antibody is obtained by obtaining cDNAs encoding VH and VL from a hybridoma producing a monoclonal antibody, and inserting the cDNAs into host cell expression vectors having genes encoding human antibodies CH and CL, respectively.
- the expression vector can be produced by constructing a human-type chimeric antibody expression vector and introducing it into a host cell.
- a human immunoglobulin (hereinafter referred to as hlg) may be any so long as it belongs to, but it is preferable that the hlgG class, hI g Gl, hIgG2 belonging more hlgG class, Any of the subclasses hIgG3 and hIgG4 can be used.
- the CL of the human chimeric antibody any CL belonging to hlg may be used, and a ⁇ class or L class can be used. .
- the human CDR-grafted antibody refers to an antibody obtained by grafting the amino acid sequences of CDRs of VH and VL of a non-human animal to the human body at appropriate positions of VH and VL of a human antibody.
- the human CDR-grafted antibody is constructed by constructing a cDNA encoding a V region obtained by grafting the VH and VL CDR sequences of a non-human animal antibody to the VH and VL CDR sequences of any human antibody,
- a human CDR-grafted antibody expression vector is constructed by inserting each into a host cell expression vector having a gene encoding the CL of a human antibody, and the expression vector is introduced into a host cell to obtain the human CDR.
- the transplant antibody can be expressed and manufactured.
- the CH of human CDR-grafted antibody may be any so long as it belongs to the hlg but it is preferable that the hlgG class, further hI g belonging to hlgG class Gl, hIgG2, MgG3, any of subclasses such MgG4 Can be used.
- the CL of the human CDR-grafted antibody may be any CL as long as it belongs to hlg, and a ⁇ class or ⁇ class can be used.
- Human antibody originally refers to an antibody that naturally exists in a human body, but human antibody phage libraries and human antibodies produced by recent advances in genetic engineering, cytology, and developmental engineering technologies Also included are antibodies obtained from transgenic non-human animals or human antibody transgenic plants. .
- Antibodies present in the human body can be obtained, for example, by isolating human peripheral blood lymphocytes, infecting them with an EB virus, etc., immortalizing them, and cloning the cells to produce the antibody-producing lymphocytes.
- the antibody can be purified.
- the human antibody phage library 1 is a library in which antibody fragments such as Fab and single-chain antibodies are expressed on the phage surface by introducing an antibody gene prepared from human B cells into the phage gene. From the library, a phage expressing an antibody fragment having a desired antigen-binding activity can be recovered using the binding activity to the substrate on which the antigen is immobilized as an index.
- the antibody fragment can be further converted to a human antibody molecule consisting of two complete L chains and two complete L chains by genetic engineering techniques.
- a human antibody transgenic non-human animal refers to an animal in which a human antibody gene has been integrated into cells. Specifically, it is possible to produce a human antibody transgenic non-human animal by introducing a mouse antibody gene from a mouse embryonic stem cell, transplanting the embryonic stem cell into the early embryo of another mouse, and then developing the embryonic stem cell. it can. In addition, a human antibody transgenic non-human animal can be prepared by introducing a human antibody gene into a fertilized egg of an animal and generating the fertilized egg. Human antibody transgenic methodA method for producing human antibodies from non-human animals is to obtain human antibody hybridomas by the normal hybridoma production method used in mammals other than humans, and to culture human antibodies in culture. Antibodies can be accumulated.
- Transgenic non-human animals include porcupines, sheep, goats, pigs, porcupines, mice, rats, chickens, monkeys, and egrets.
- the antibody fragment refers to a fragment containing at least a part of the Fc region of the antibody.
- the Fc region refers to a region on the C-terminal side of the whole H chain, a CH2 region and a CH3 region. At least a part of the Fc region preferably refers to a fragment containing the CH2 region, more preferably a region containing the first aspartic acid present in the CH2 region.
- Antibody fragments include H chain monomers, H chain dimers, and the like.
- the Fc region in the present invention includes a natural type and its mutant type.
- a fusion protein having a part of the Fc region is a substance obtained by fusing an antibody or a fragment of the antibody containing a part of the Fc region of an antibody with a protein such as an enzyme or a cytokine (hereinafter referred to as an Fc fusion protein).
- the proportion of sugar chains in which fucose is not linked to N-acetyldarcosamine at the sugar chain reducing end is low. 50% or more, preferably 60% or more, more preferably 70% or more, still more preferably 80% or more, particularly preferably 90% or more, and binds to the Fc region contained in the antibody composition. It is most preferred that all of the N-glycoside-linked complex-type sugar chains to be used are sugar chains in which fucose is not linked to N-acetyltyldarcosamine at the reducing end of the sugar chain.
- the proportion of sugar chains in which fucose is not linked to N-acetyldarcosamine at the reducing end of the sugar chain The higher the, the higher the antibody composition has the higher antibody-dependent cytotoxic activity.
- the ratio of sugar chains in which fucose is not bound to N-acetyltylcolasamine at the reducing end of sugar chains contained in a composition comprising an antibody molecule having an N-glycoside-linked complex type sugar chain in the Fc region is determined by the ratio of the antibody From the molecule Using known methods such as hydrazinolysis and enzymatic digestion [Biochemical Experimental Method 23—Glycoprotein Glycosylation Research Method (Academic Press Center), edited by Reiko Takahashi (1989)], the sugar chains are released and the released sugar chains are released. Can be determined by fluorescent labeling or isotope labeling, and separating the labeled sugar chains by one of the methods of mouth chromatography. In addition, the released sugar chains can be determined by analysis by the HPAED-PAD method [Journal 'Op' Liquid 'Chromatography (J. Liq. Chromatogr.), 6, 1577 (1983)]. Can be.
- high therapeutic effects include, for example, a high level of cytotoxic activity 1 ".
- cytotoxic activity of the antibody composition include antibody-dependent cytotoxic activity (hereinafter abbreviated as ADCC), Nematode-dependent cytotoxicity (monoclonal antibodies), activity to suppress the growth of antigen-expressing cells by binding to antigens, etc.
- the growth-suppressing activity includes inducing apoptosis and inducing differentiation of target cells. Also include those that promote cell growth [Cancer Research 60, 7170 (2000), Nature's Medicine (Nature Medicine) 1, 644 (1995), Cell Growth Differ. 3, 401 (1992)].
- ADCC activity means that in vivo, an antibody bound to a cell surface antigen such as a tumor cell activates an effector cell through the binding of an antibody Fc region to an Fc receptor present on the effector cell surface. , which refers to the activity of damaging tumor cells, etc. [Monoclonal Antibodies: Principles and Applications, Wiley-Liss, Inc., Capter 2.1 ( 1995)]. Effector cells include immune cells such as natural killer cells, macrophages, monocytes, dendritic cells, and granulocytes. Fc receptor is Fco; receptor I, Fc E receptor I,?
- Fcy receptor Ilia is mainly expressed on natural killer cells and is one of the important Fc receptors for ADCC activity [monoclonal 'Antibodies: Principles'and' practice ( Monoclonal Antibodies: principles and practice), Thirdiidition, Acad. Press, 1996 (hereinafter abbreviated as "monoclonal 'Antibodies')".
- the proportion of sugar chains in which fucose is not bound to N-acetylglycosamine at the reducing end of sugar chains is 50% of all complex N-glycoside-linked sugar chains that bind to the Fc region of the antibody molecule. % Of the total N-glycoside-linked complex type glycan that binds to the Fc region of the antibody molecule, indicating that the antibody composition exhibits a higher therapeutic effect than when the antibody composition alone is administered alone.
- the combination of an antibody composition in which the proportion of sugar chains in which fucose is not bound to N-acetylsyllucosamine is 50% or more and at least one or more drugs results in a case where the antibody composition is administered alone. A drug that exerts a therapeutic effect that is higher than the therapeutic effect that is exhibited.
- the medicament of the present invention is characterized in that, among all N-glycoside-linked complex-type sugar chains that bind to the Fc region of an antibody molecule, a sugar chain in which fucose is not linked to N-acetyltyldarcosamine at the reducing end of the sugar chain. It shows a higher therapeutic effect than a drug comprising a combination of an antibody composition having a ratio of less than 50% and at least one drug.
- the medicament of the present invention can have a smaller amount of drug than when the drug is used alone, and can reduce the side effects of concern when a high dose of the drug alone is administered to a patient.
- Cells that are resistant to lectins that recognize an ⁇ -linked sugar chain structure include antibody compositions such as yeast, animal cells, insect cells, and plant cells.
- a hybridoma resistant to a lectin that recognizes a sugar chain structure in which the 6-position of ⁇ -glycidyl-linked glycan at the reducing end of ⁇ -glycidyl-linked glycan and the 1-position of fucose is ⁇ -linked Cells
- host cells for producing human antibodies and humanized antibodies transgenic for producing human antibodies, embryonic stem cells and fertilized egg cells for producing non-human animals, transgenic for producing human antibodies Examples include plant callus cells, myeloma cells, and cells derived from transgenic non-human animals for producing plants.
- Myeloma cells can be used as fusion cells when producing hybridoma cells.
- a transgenic non-human animal can be immunized with an antigen, and the spleen cells of the animal can be removed and used to produce hybridoma cells.
- Lectin I A cell having this resistance is a cell whose growth is not inhibited even when cell culture is performed by giving an effective concentration of lectin to a culture medium.
- lectin effective concentration that does not inhibit growth yo be appropriately determined according to each cell line bur normally 10 ⁇ ⁇ / ⁇ 1 ⁇ 10. 0 ⁇ ⁇ ⁇ 1, preferably 0. 5 ⁇ 2. 0m g / ml.
- the effective concentration of lectin when a mutation is introduced into the parent cell is not less than the concentration at which the parent cell cannot grow normally, preferably the same concentration as that at which the parent cell cannot grow normally, more preferably 2%.
- the concentration refers to a concentration of up to 5 times, more preferably 10 times, and preferably 20 times or more.
- the parent cell is a cell before any treatment, that is, a cell before performing the step of selecting a1,6-fucose / lectin-resistant cells used in the present invention, because the above-mentioned enzyme activity is reduced or deleted.
- a1,6-fucose / lectin-resistant cells used in the present invention because the above-mentioned enzyme activity is reduced or deleted.
- the parent cell is not particularly limited, but specific examples of the parent cell of various cell lines include the following cells.
- NS0 cells Parent cells of NS0 cells are described in the literature such as BIO / TECHNOLOGY, 10, 169 (1992), and Biotechnology 'Bioengineering (Biotechnol. Bioeng.), 73, 261, (2001). NS0 cells. Also, there are ⁇ 0-9 cells registered with the RIKEN Cell Development Bank (RCB0213), or substrains obtained by adapting these strains to a growth medium. ⁇
- SP2 / 0-Agl4 cells include, for example, Journal of Immunology (J. Immunol '.), 126, 317 (1981), Nature, 276, 269 (1978), and Human Antibody.
- SP2 / 0-Agl4 cells described in the literature such as Ibodies and Hypridomas (Human Antibodies and Hybridomas), 3, 129 (1992).
- SP2 / 0-Agl4 cells registered with the ATCC (ATCC CRL-1581), or a substrain (ATCC CRL-15S1.1.1) obtained by adapting these strains to a medium in which they can grow, may also be mentioned.
- CHO-K1 strain ATCC CCL-61
- DUXB11 strain ATCCCRL-9096
- Pro-5 strain ATCC CRL-1781
- commercially available CHO-S strain Lif etechnologies Cat # ll 6 l 9
- sub-cell lines obtained by naturalizing these cell lines to viable medium may be mentioned.
- GIL 16Ag. 20 cells include cell lines established from Y3 / Agl. 2.3 cells (ATCC CRL-1631). Specific examples thereof include YB2 / 3HL. ⁇ 2.Gil. 16Ag described in documents such as J. Cell. Biol., 93, 576 (1982) and Methods Enzymol., 73 ⁇ 1 (1981). 20 cells. Also, there are YB2 / 3HL. P2.Gil. 16Ag. 20 cells (ATCC CRL-1662) registered with the ATCC, or substrains obtained by adapting these strains to a medium capable of growing.
- any lectin that can recognize the sugar chain structure can be used. All lectins are included.
- lentil lectin LCA Li l Agglutinin from Lens Cul inari s
- enduma lectin PSA Pea Lectin from Pi sum sativum
- fava bean lectin VFA Agglutinin from Vicia f aba
- phyllo Chawantakelectin ML Lectin from Aleuria aurantia
- al, 6-fucose / lectin-resistant cells may be any cells as long as their growth is not inhibited in the presence of a certain effective concentration of lectin.
- at least one of the following proteins may be used.
- a cell whose activity is lower or deleted than that of the parent cell line is exemplified.
- GDP-fucose synthase Intracellular sugar nucleotide GDP-an enzyme protein involved in the synthesis of fucose
- T includes any enzyme involved in the synthesis of sugar nucleotide GDP-fucose, which is a source of fucose to sugar chains in the cell. Enzymes that affect synthesis and the like.
- GDP-fucose an intracellular sugar nucleotide
- the de novo synthetic pathway or the salvage synthetic pathway Therefore, all enzymes involved in these synthetic pathways are included in GDP-fucose synthase.
- GDP-fucose synthase involved in the de novo synthesis pathway includes GDP-mannose 4-dehydratase (GDP-mannose 4-dehydratase; hereinafter referred to as GMD), GDP-keto-6-deoxymannose 3, 5-epimerase , 4-reductase (GDP-keto-deoxymannose 3,5-epimerase, 4-reductase; hereinafter referred to as Fx).
- GMD GDP-beta-L-fucose pyrophosphorylase
- Fucokinase Fucokinase
- Examples of GMD include GMD having the amino acid sequence represented by SEQ ID NO: 1, 2, or 3.
- Examples of the enzyme that affects the synthesis of the intracellular sugar nucleotide GDP-fucose include those that affect the activity of the enzyme involved in the above-described synthesis pathway of the intracellular sugar nucleotide GDP-fucose and the substances that serve as substrates for the enzyme. Enzymes that affect structure are also included.
- a 1,6-Fucose-modifying enzyme includes any enzyme that participates in the reaction in which the 6-position of N-glycidyl-linked complex-type sugar chain reducing terminal N-acetyldarcosamine and the 1-position of fucose are ⁇ -linked. Included.
- the enzyme involved in the reaction in which the 6-position of ⁇ ⁇ -glycidyl-linked glycan at the reducing end of ⁇ -acetyldarcosamine and the 1-position of fucose are ⁇ -linked is the ⁇ -glycoside-linked glycan at the reducing end of glycan.
- Any enzyme that affects the reaction in which the 6-position of acetyl gnorecosamine and the 1-position of fucose are ⁇ -linked is included. Specific examples include al, 6-fucosyltransferase and Hi-L-fucosidase.
- the ⁇ , 6-fucosyltransferase is represented by SEQ ID NO: 4 or 5: ⁇ 1,6-fucosyltransferase having a amino acid sequence is exemplified.
- the enzyme which affects the reaction in which the 6-position of ⁇ ⁇ -acetyldarcosamine at the reducing end of ⁇ -glycoside-linked complex type sugar chain and the 1-position of fucose are ⁇ -linked includes the ⁇ -glycoside-linked complex type sugar described above.
- Enzyme that affects the activity of the enzyme involved in the reaction in which the position 1 of fucose binds to position 6 of fucose at the 6-position of ⁇ -acetyldarcosamine at the chain reduction terminal, or that affects the structure of the substrate substance of the enzyme are also included.
- the GDP-fucose transport protein includes any protein involved in the transport of the intracellular sugar nucleotide GDP-fucose to the Golgi apparatus, and specifically includes the GDP-fucose transporter.
- proteins that influence the reaction of transporting the intracellular sugar nucleotide GDP-fucose into the gonoresi are also included in the GDP-fucose transport protein, and specifically, the above-mentioned intracellular sugar nucleotide GDP-fucose Golgi ⁇ : Proteins that affect the activity of proteins involved in transport to the cell or that affect expression.
- any method can be used as long as ⁇ 1,6-fucose lectin-resistant cells can be selected.
- Specific examples include the above-described techniques for reducing or deleting the activity of a protein. Techniques for deleting the above-mentioned proteins that reduce their activity include:
- Nadogaa de are (W00 2/3 11 4 0 , 003/085107, W003 / 085118).
- a genomic gene of an enzyme involved in sugar chain modification in which fucose is linked to ⁇ -position at position 6 of N-acetyldarcosamine at the reducing end of N-glycoside-linked complex type sugar chain is knocked out.
- the Itoda vesicle in which the genomic gene has been knocked out has a fucose at position 6 of N-acetylacetylcosamine at the reducing end of the N-glycoside-linked complex type sugar chain using the method described below.
- Cells in which the genomic gene of an enzyme involved in sugar chain modification in which position 1 is ⁇ - linked are knocked out.
- cells in which a genomic gene has been knocked out include cells in which all or part of a target gene has been deleted from the genome.
- any method can be used, as long as the desired genome can be modified, but a genetic engineering method is preferable.
- a specific method there is a method of reducing or deleting the activity of the above-mentioned enzyme.
- a method for selecting a lectin-resistant cell line that recognizes a sugar chain structure in which the 6-position of ⁇ ⁇ -acetyltilcosamine at the reducing end of ⁇ -glycoside-linked glycan and the 1-position of fucos, as described above, is used.
- cells in which the genomic gene of an enzyme involved in glycosylation, in which fucose is linked to position 6 of ⁇ -acetyldarcosamine at the reducing end of ⁇ -daricoside-linked complex type glycan, are knocked out are selected. can do.
- Examples of the antibody composition in the present invention include an antigen expressed on a cell associated with a disease, or an antibody composition against an antigen associated with pathogenesis such as proliferation or metastasis of a cell associated with a disease.
- an antigen expressed on a cell associated with a disease or an antibody composition against an antigen associated with pathogenesis such as proliferation or metastasis of a cell associated with a disease.
- CCR4 CC chemokine receptor 4
- PTHrP parathyroid hormone-related protein
- basic fibroblast Cell growth factor fibroblast growth factor 8
- basic fibroblast growth factor receptor fibroblast growth factor 8 receptor
- epithelial fibroblast growth factor receptor EGFR
- epithelial cell adhesion molecule EpCam
- Insulin-like growth factor insulin-like growth factor receptor
- PMSA vascular endothelial cell growth factor
- RSV respiratory syncytial virus
- IL-5 receptor ⁇ chain, etc.
- Antibody compositions are included.
- anti-GD2 antibody Anti 'Cancer' Research (Anticancer Res.), 13, 331 (1993)]
- anti-GD3 antibody Anti-GD3 antibody
- Cancer 'Imology Immunotherapy Cancer Immunol. Immunother.
- anti-GM2 antibody Anti-GM2 antibody
- Cancer Res. Cancer Res.
- anti-HER2 antibody Proceedings Op. The National Academy of Sciences (Proc. Natl. Acad. Sci.
- ADCC activity can be measured by an in vitro measurement system such as 51 Cr release method, lactate dehydrogenase (LDH) release method, flow cytometry, or an in vivo evaluation system using an animal model.
- an in vitro measurement system such as 51 Cr release method, lactate dehydrogenase (LDH) release method, flow cytometry, or an in vivo evaluation system using an animal model.
- LDH lactate dehydrogenase
- Drugs used in combination with the antibody composition having a ratio of 50% or more include cytokines, proteins such as antibodies, small molecule drugs, biological response modifiers (hereinafter referred to as BRMs), and the like.
- Cytokines include interleukins (ILs), colony stimulating factors (CSFs), interferons (IFNs), tumor necrosis factors (TFs), chemokines, or combinations thereof.
- IL-2, IL-15, IFN-a and IFN-2 ⁇ are mentioned.
- Low molecular drugs include amifostine (ethyol), cisplatin (ci spl at in), dacanolevadine (DTIC) [dacarbazine (DTIC)], and dactinomycin
- Examples of the antibody include the above-mentioned antibodies.
- BRMs in the present invention include BCG, anaerobic corynebacterium, bacterial preparations such as muramyl dipeptide, trehalose dimycolic acid, pyran copolymer, MVE, poly I: C, pyrimidine, thymosin, thymulin, thymopoesin, picibanil, fucoidan. , Krestin and the like.
- the effect of the medicament of the present invention can be examined, for example, by using an ilim cytotoxicity assay system.
- an ilim cytotoxicity assay system As an example of the system for measuring the activity of the itoda cyst of ii i ⁇ , there is a system for measuring ADCC activity.
- ADCC activity was impaired by contacting antigen-expressing target cells with effector cells such as peripheral blood mononuclear cells, monocytes, macrophages, and granulocytes from humans or other animals in the presence of antibodies. It can be measured by detecting the degree of the target cell and quantifying it.
- the degree of impaired target cells, 51 Cr release assay, a method of detecting the enzymatic activity of the target cells can be detected Te detection methods such as [Koyo' by flow cytometer.
- the immunocompetent cells of the present invention in the ADCC activity measurement system The effect of the substance to be activated or the substance having antitumor activity can be determined by adding these substances to the ADCC activity measurement system or by preliminarily preserving these substances in target cells, effector cells, or both. It can be measured by observing the effect of a period of exposure on ADCC activity.
- the effect of the medicament of the present invention can also be examined by measuring iiLJd ⁇ antitumor activity using an animal model.
- xenograft models in which cultured cell lines derived from human cancer tissues are transplanted into immunodeficient mice such as nude mice, and syngeneic transplant models in which cultured mouse cancer cell lines are transplanted into wild-type mice having a normal immune system And so on.
- Xenograft models can be prepared by implanting human cancer cell lines into various sites such as subcutaneous, intradermal, intraperitoneal, and intravenous sites of immunodeficient mice such as nude mice.
- the single administration of an antibody By comparing the effects of the single administration of an antibody, the single administration of a substance that activates immunocompetent cells or a substance having antitumor activity with the above-described animal model, and the effects of the medicament of the present invention, The antitumor effect of the drug can be evaluated.
- the medicament of the present invention can be administered alone, it is usually mixed with one or more pharmacologically acceptable carriers, and any of the well-known drugs well known in the technical field of pharmaceutics is used. It is desirable to provide it as a pharmaceutical preparation produced by the method.
- intravenous administration can be preferably used.
- Dosage forms include sprays, capsules, tablets, granules, syrups, emulsions, suppositories, injections, ointments, tapes and the like.
- Formulations suitable for oral administration include emulsions, syrups, capsules, tablets, powders, granules and the like.
- Liquid preparations such as emulsions and syrups include water, sugars such as sucrose, sorbitol, fructose, glycols such as polyethylene glycol and propylene glycol, oils such as sesame oil, olive oil, soybean oil, p-hydroxybenzoic acid. It can be produced by using preservatives such as acid esters, flavors such as stomach berry, and flavors such as permint as additives.
- Capsules, tablets, powders, granules, etc. are excipients such as lactose, pudose, sucrose, mannitol, disintegrants such as starch and sodium alginate, lubricants such as magnesium stearate, talc, polyvinyl It can be produced using a binder such as alcohol, hydroxypropylcellulose and gelatin, a surfactant such as fatty acid ester, and a plasticizer such as glycerin as additives.
- Formulations suitable for parenteral administration include injections, suppositories, sprays and the like.
- the injection is prepared using a carrier comprising a salt solution, a pudose solution, or a mixture of the above.
- Suppositories are prepared using carriers such as lactic acid, hydrogenated fats or carboxylic acids.
- Sprays are also prepared using the drug itself or a carrier that does not irritate the oral and respiratory mucosa of the recipient and disperses the drug as fine particles to facilitate absorption.
- the carrier include lactose and glycerin.
- preparations such as aerosols and dry powders are possible.
- the components exemplified as carotenoids in oral preparations can also be added.
- Dose or frequency of administration is 0. 1 ⁇ 20m g / k g the desired therapeutic effect, administration method, treating period, age, as different forces through adult dose of antibody per amount by weight, or the like.
- the dose of the drug used in combination with the antibody is the same or lower than that used alone for clinical use.
- FIG. 1 shows the enhancing effect of various cytokines on ADCC activity of KM2760-1 and KM3060.
- the vertical axis represents cytotoxic activity (%).
- the medulla shows no cytotoxicity, the mouth shows the addition of IL-2, and the hatched lines show the cytotoxic activity when IL-15 is added.
- Figure 2 illustrates the enhancement effects of various cytokines on the ADCC activity of KM 3 0 65 and Rituxan.
- the vertical axis represents cytotoxic activity (%).
- the garden shows no cytokine addition
- the mouth shows IL-2 addition
- the shaded lines show the Itoda cyst damage activity when IL-15 is added.
- Figure 3 shows the enhancing effect of various cytokines on the ADCC activity of KM 3 0 65 and Rituxan.
- the vertical axis represents cytotoxic activity (%).
- the country indicates the absence of cytokines
- the mouth indicates IFN-addition force [1]
- the hatched lines indicate the cytotoxic activity when IFN-7 was added.
- Example 1 Combined effect of anti-CCR4 antibody and cytokine on in vitro cytotoxicity
- KM2760-1 is an anti-CCR4 chimeric antibody produced from the cell line KM2760-1 # 58-35-16 obtained by introducing an anti-CCR4 chimeric antibody-expressing strain into the rat myeloma cell line YB2 / 0 cells.
- the KM2760-1 # 58-35-16 strain has lectin resistance, and the content of sugar chains to which fucose does not bind in the total sugar chains of KM2760-1 is 87%.
- KM306O is an anti-CCR4 chimeric antibody produced from cell line 5-03 obtained by introducing an anti-CCR4 chimeric antibody-expressing strain into the CH0 / DG44 cell line.
- ⁇ has no lectin resistance, and the content of sugar chains to which fucose is not bound in the total sugar chains of ⁇ 3060 ⁇ is 8%.
- KM2760-1 and ⁇ 3060 have the same amino acid sequence, and have the same antigen binding activity.
- a healthy person's venous rainbow (50 mL) was collected, and heparin sodium (Shimizu Pharmaceutical Co., Ltd.) (0.5 mL) was added and mixed gently. This was centrifuged (400 g, 20 minutes) using a MONO-POLY separation solution (manufactured by Dainippon Pharmaceutical Co., Ltd.) according to the instruction manual to separate a mononuclear cell layer. After washing by centrifugation three times with RPMI1640-FCS (5) medium, the cells were resuspended in the same medium at a concentration of 3 ⁇ 10 6 cells / mL to obtain an effector cell solution.
- MONO-POLY separation solution manufactured by Dainippon Pharmaceutical Co., Ltd.
- the fefecta single cell solution obtained in the above (a) was dispensed at 50 / i L into a 96-well U-bottom plate (Falcon). Further RPMIIMO - FCS diluted following solutions (5) was added in 50 / L, and allowed to stand 5% C0 in 2 Inki Yubeta ⁇ trowel 3 days. (1) 13 ⁇ 43 ⁇ 411640—Fuji 5 (5) only (control with no added site force)
- G418 (manufactured by Nacalai Tesque) containing at 0. 5 mg / mL RPMIIMO- FCS ( 10) medium (manufactured by RPMI1640 medium (GIBCO BRL, Inc. containing 10% FCS)) and CCR4 / EL4 cells (CCR4 gene cultured in the introduction Mouse thymoma cells, W001 / 64754) were washed with RPMIIMO-FCS (5) medium (RPI1640 medium containing 5% FCS (GIBCO BRL)) by centrifugation and suspension, and then RPMI1640-FCS (5 ) 2 x 10 5 cells AnL was prepared with the medium and used as the target cell solution.
- Cytotoxic activity (%) [(Absorbance of specimen) spontaneous release of effector cells 1 (Absorbance of spontaneous release of target cells and cells)] / [(Absorbance of total release of target cells) 1 (Spontaneous release of target cells) Absorbance)] X 100
- Figure 1 shows the results. ADCC activity of KM2760-1 without cytokine was higher than that of KM3060, but was further enhanced by cytokine addition. This result indicates that, among all N-daricoside-linked complex-type sugar chains that bind to the Fc region contained in the antibody composition, of the sugar chains in which fucose is not bound to N-acetyldarcosamine at the reducing end of the sugar chain.
- the high ADCC activity of the antibody composition with a proportion of 50% or more indicates that the cytokine further increases.
- Example 2 Combined effect of anti-CD20 antibody and cytokine on iiL ⁇ iii ⁇ cytotoxicity
- Example 1 The effect of the combination of the cytokine CD20 human chimeric pile KM3065 (W003 / 55993) and the commercially available anti-CD20 human chimeric antibody Rituxan (Genentech) and cytokine on in vitro cytotoxic activity was described in Example 1. Was measured according to the method described above. .
- Cytokines are IL-2, IL-15 (all manufactured by Peprotech, final concentration Ing / mL), IFN- ⁇ (Peprotech, final concentration lOOng / mL), IFN- ⁇ (R & D Systems, final concentration lOOng) / mL) was used.
- KM 3 0 65 is an anti-CD20 chimeric antibody produced from the cell line KM3065 obtained by introducing the anti-CD20 chimeric antibody expression strain rat myeloma cell line YB2 / 0 cells.
- KM3065 strain has lectin resistance, KM3065 The content of sugar chains to which fucose is not bound in the total sugar chains is 96%. On the other hand, the content of sugar chains that do not bind to fucose in all sugar chains of Rituxan is 6%.
- KM3065 and Rituxan have the same amino acid sequence, and have the same antigen binding activity.
- FIGS. 2 and 3 show the results.
- the ADCC activity of KM3065 without cytokine was higher than that of Rituxan, but was further enhanced by the addition of cytokine. This result indicates that, among all N-glycoside-linked complex-type sugar chains that bind to the Fc region contained in the antibody composition, sugar chains in which fucose is not linked to N-acetyldarcosamine at the sugar chain reducing end.
- the high ADCC activity of the antibody composition having a ratio of 50% or more indicates that the cytokine further increases.
- the ratio of sugar chains in which fucose is not linked to N-acetyldarcosamine at the reducing end of the sugar chain is 50%.
- a medicament using the antibody composition and at least one drug is expected to have a high therapeutic effect.
Abstract
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