IL178042A - Pharmaceutical compositions containing anti-alpha5beta1 antibodies for inhibiting cancer cell proliferation - Google Patents
Pharmaceutical compositions containing anti-alpha5beta1 antibodies for inhibiting cancer cell proliferationInfo
- Publication number
- IL178042A IL178042A IL178042A IL17804206A IL178042A IL 178042 A IL178042 A IL 178042A IL 178042 A IL178042 A IL 178042A IL 17804206 A IL17804206 A IL 17804206A IL 178042 A IL178042 A IL 178042A
- Authority
- IL
- Israel
- Prior art keywords
- cancer
- antibody
- pharmaceutical composition
- cell
- integrin
- Prior art date
Links
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- A61K39/00—Medicinal preparations containing antigens or antibodies
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2839—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily
- C07K16/2842—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily against integrin beta1-subunit-containing molecules, e.g. CD29, CD49
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- A—HUMAN NECESSITIES
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- A61K38/00—Medicinal preparations containing peptides
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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
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/39558—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against tumor tissues, cells, antigens
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal 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
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
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- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Epidemiology (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Oncology (AREA)
- Molecular Biology (AREA)
- Mycology (AREA)
- Genetics & Genomics (AREA)
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- Biomedical Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (6)
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| US62504904P | 2004-11-03 | 2004-11-03 | |
| US65109805P | 2005-02-07 | 2005-02-07 | |
| US65751405P | 2005-02-28 | 2005-02-28 | |
| PCT/US2005/009939 WO2005092073A2 (en) | 2004-03-24 | 2005-03-24 | Use of anti-alpha5beta1 antibodies to inhibit cancer cell proliferation |
Publications (2)
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| IL178042A0 IL178042A0 (en) | 2006-12-31 |
| IL178042A true IL178042A (en) | 2011-05-31 |
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| IL178042A IL178042A (en) | 2004-03-24 | 2006-09-12 | Pharmaceutical compositions containing anti-alpha5beta1 antibodies for inhibiting cancer cell proliferation |
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| JP (1) | JP4857259B2 (enExample) |
| KR (1) | KR20070009637A (enExample) |
| AT (1) | ATE531388T1 (enExample) |
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| CA (1) | CA2560508A1 (enExample) |
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| ES (1) | ES2376556T3 (enExample) |
| IL (1) | IL178042A (enExample) |
| NO (1) | NO20064794L (enExample) |
| NZ (1) | NZ549893A (enExample) |
| WO (1) | WO2005092073A2 (enExample) |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| HUE066795T2 (hu) | 2006-03-15 | 2024-09-28 | Alexion Pharma Inc | Paroxysmalis nocturnalis haemoglobinuriában szenvedõ betegek kezelése egy komplement inhibitorral |
| CA2646611A1 (en) * | 2006-03-21 | 2008-05-22 | Genentech, Inc. | Combinatorial therapy |
| WO2007114851A1 (en) * | 2006-04-04 | 2007-10-11 | The Board Of Trustees Of The University Of Illinois | Methods and compositions to induce cell death of invasive tumors |
| CA2652886A1 (en) * | 2006-05-24 | 2007-11-29 | Bayer Schering Pharma Aktiengesellschaft | High affinity human and humanized anti-.alpha.5.beta.1 integrin function blocking antibodies with reduced immunogenicity |
| WO2008061377A1 (en) * | 2006-11-22 | 2008-05-29 | Centre Hospitalier De L'universite De Montreal | Novel receptor for cd40l and uses thereof |
| WO2009018226A2 (en) * | 2007-07-27 | 2009-02-05 | Facet Biotech Corporation | Pharmaceutical combinations comprising a tyrosine kinase inhibitor and an antibody against integrin alpha 1 beta 5 (cd49e) |
| AR066170A1 (es) * | 2007-09-26 | 2009-07-29 | Genentech Inc | Anti integrina alfa 5 beta 1 |
| AU2009212442C1 (en) * | 2008-02-05 | 2014-07-17 | Bristol-Myers Squibb Company | Alpha 5 - beta 1 antibodies and their uses |
| US20120114667A1 (en) | 2008-12-23 | 2012-05-10 | Medimmune Limited | TARGETED BINDING AGENTS DIRECTED TO a5BETA1 AND USES THEREOF |
| MA33210B1 (fr) * | 2009-03-25 | 2012-04-02 | Genentech Inc | Nouveaux anticorps anti-a5b1 et leurs utilisations |
| US20110319335A1 (en) | 2010-06-23 | 2011-12-29 | Xiaodong Feng | Combined administration of integrin receptor antagonists for anti-angiogenic therapy |
| SG10201604104PA (en) | 2011-10-25 | 2016-07-28 | Prothena Therapeutics Ltd | Antibody formulations and methods |
| US8946159B2 (en) | 2011-12-22 | 2015-02-03 | California Northstate College Of Pharmacy, Llc | Administration of an antagonist of α5β1 for anti-angiogenesis and cancer treatment |
| NO2760138T3 (enExample) | 2012-10-01 | 2018-08-04 | ||
| WO2018204374A1 (en) | 2017-05-02 | 2018-11-08 | Merck Sharp & Dohme Corp. | Formulations of anti-lag3 antibodies and co-formulations of anti-lag3 antibodies and anti-pd-1 antibodies |
| JOP20190260A1 (ar) | 2017-05-02 | 2019-10-31 | Merck Sharp & Dohme | صيغ ثابتة لأجسام مضادة لمستقبل الموت المبرمج 1 (pd-1) وطرق استخدامها |
| KR20210089215A (ko) | 2018-11-07 | 2021-07-15 | 머크 샤프 앤드 돔 코포레이션 | 항-lag3 항체 및 항-pd-1 항체의 공동-제제 |
| WO2025106725A2 (en) * | 2023-11-15 | 2025-05-22 | Morphic Therapeutic, Inc. | HUMAN ANTI-α5β1 ANTIBODIES AND USES THEREOF |
| WO2025106724A2 (en) * | 2023-11-15 | 2025-05-22 | Morphic Therapeutic, Inc. | USE OF ANTI-α5β1 ANTIBODIES IN THE TREATMENT OF PULMONARY HYPERTENSION AND HEART FAILURE |
Family Cites Families (36)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4704366A (en) | 1984-06-22 | 1987-11-03 | Bio-Rad Laboratories, Inc. | Process for binding IgG to protein A |
| JPS61134325A (ja) | 1984-12-04 | 1986-06-21 | Teijin Ltd | ハイブリツド抗体遺伝子の発現方法 |
| US5618920A (en) | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US4801687A (en) | 1986-10-27 | 1989-01-31 | Bioprobe International, Inc. | Monoclonal antibody purification process using protein A |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| WO1992015683A1 (en) | 1991-03-06 | 1992-09-17 | MERCK Patent Gesellschaft mit beschränkter Haftung | Humanized and chimeric monoclonal antibodies |
| CA2078539C (en) | 1991-09-18 | 2005-08-02 | Kenya Shitara | Process for producing humanized chimera antibody |
| GB9125979D0 (en) | 1991-12-06 | 1992-02-05 | Wellcome Found | Antibody |
| AU684041B2 (en) | 1992-02-19 | 1997-12-04 | Schering Corporation | Cloning and expression of humanized monoclonal antibodies against human interleukin-4 |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| US5677181A (en) | 1992-10-29 | 1997-10-14 | The Australian National University | Angiogenesis inhibitory antibodies |
| US5536814A (en) | 1993-09-27 | 1996-07-16 | La Jolla Cancer Research Foundation | Integrin-binding peptides |
| US5981478A (en) | 1993-11-24 | 1999-11-09 | La Jolla Cancer Research Foundation | Integrin-binding peptides |
| WO1995022618A1 (en) | 1994-02-22 | 1995-08-24 | Dana-Farber Cancer Institute | Nucleic acid delivery system, method of synthesis and uses thereof |
| DE69516351T2 (de) * | 1994-09-21 | 2000-12-07 | Matsushita Electric Industrial Co., Ltd. | Sekundäre Lithium Feststoffbatterie |
| US5705154A (en) | 1995-03-08 | 1998-01-06 | Schering Corporation | Humanized monoclonal antibodies against human interleukin-4 |
| JP2001527513A (ja) | 1996-03-15 | 2001-12-25 | デュポン ファーマシューティカルズ カンパニー | スピロ環インテグリン阻害剤 |
| US5922676A (en) | 1996-09-20 | 1999-07-13 | The Burnham Institute | Methods of inhibiting cancer by using superfibronectin |
| US5846536A (en) | 1996-10-04 | 1998-12-08 | The Regents Of The University Of California | Restoration of normal phenotype in cancer cells |
| EP0896002A4 (en) | 1997-01-29 | 2005-02-02 | Toray Industries | CHIMERIC PROTEINS, THEIR HETERODIMER COMPLEXES AND BLOOD PLATE REPLACEMENT |
| US6171586B1 (en) * | 1997-06-13 | 2001-01-09 | Genentech, Inc. | Antibody formulation |
| WO1999037329A1 (en) * | 1998-01-22 | 1999-07-29 | Astrazeneca Ab | Pharmaceutical formulation comprising an antibody and a citrate buffer |
| WO1999055913A2 (en) | 1998-04-27 | 1999-11-04 | Sidney Kimmel Cancer Center | Reduced complexity nucleic acid targets and methods of using same |
| US6852318B1 (en) | 1998-05-08 | 2005-02-08 | The Regents Of The University Of California | Methods for detecting and inhibiting angiogenesis |
| AU746662B2 (en) * | 1998-05-08 | 2002-05-02 | Regents Of The University Of California, The | Methods for detecting and inhibiting angiogenesis |
| EP1204764A2 (en) | 1999-08-11 | 2002-05-15 | EOS Biotechnology, Inc. | Methods of screening for angiogenesis modulators |
| JP4787447B2 (ja) | 2000-01-20 | 2011-10-05 | メルク・シャープ・エンド・ドーム・コーポレイション | αｖインテグリン受容体拮抗薬 |
| CA2397665A1 (en) | 2000-01-24 | 2001-07-26 | Merck & Co., Inc. | Alpha v integrin receptor antagonists |
| US7740841B1 (en) * | 2000-01-28 | 2010-06-22 | Sunnybrook Health Science Center | Therapeutic method for reducing angiogenesis |
| US20040259152A1 (en) | 2000-02-22 | 2004-12-23 | Richard Murray | Novel methods of diagnosing and screening for modulators of tissue remodeling and treating related diseases |
| EP1418943A1 (en) | 2001-02-14 | 2004-05-19 | Protein Design Labs, Inc. | Methods of diagnosis of angiogenesis, compositions and methods of screening for angiogenesis modulators |
| KR20110140143A (ko) | 2002-11-26 | 2011-12-30 | 애보트 바이오테라퓨틱스 코포레이션 | 혈관형성을 조절하는 α5β1 인테그린에 대한 키메라성 및 인간화 항체 |
| US7276589B2 (en) * | 2002-11-26 | 2007-10-02 | Pdl Biopharma, Inc. | Chimeric and humanized antibodies to α5β1 integrin that modulate angiogenesis |
| EP1625165A2 (en) | 2003-04-03 | 2006-02-15 | Protein Design Labs, Inc. | Inhibitors of integrin alpha5beta1 and their use for the control of tissue granulation |
| CN1816356A (zh) * | 2003-05-14 | 2006-08-09 | 免疫原公司 | 药物缀合物组合物 |
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2005
- 2005-03-24 EP EP05744016A patent/EP1755659B1/en not_active Expired - Lifetime
- 2005-03-24 AU AU2005226736A patent/AU2005226736B2/en not_active Ceased
- 2005-03-24 JP JP2007505204A patent/JP4857259B2/ja not_active Expired - Fee Related
- 2005-03-24 US US11/090,331 patent/US7662384B2/en not_active Expired - Fee Related
- 2005-03-24 AT AT05744016T patent/ATE531388T1/de active
- 2005-03-24 CA CA002560508A patent/CA2560508A1/en not_active Abandoned
- 2005-03-24 ES ES05744016T patent/ES2376556T3/es not_active Expired - Lifetime
- 2005-03-24 NZ NZ549893A patent/NZ549893A/en not_active IP Right Cessation
- 2005-03-24 KR KR1020067021955A patent/KR20070009637A/ko not_active Ceased
- 2005-03-24 DK DK05744016.6T patent/DK1755659T3/da active
- 2005-03-24 BR BRPI0509177-2A patent/BRPI0509177A/pt not_active IP Right Cessation
- 2005-03-24 WO PCT/US2005/009939 patent/WO2005092073A2/en not_active Ceased
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2006
- 2006-09-12 IL IL178042A patent/IL178042A/en not_active IP Right Cessation
- 2006-10-23 NO NO20064794A patent/NO20064794L/no not_active Application Discontinuation
-
2009
- 2009-12-18 US US12/642,687 patent/US20100291111A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
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| AU2005226736A1 (en) | 2005-10-06 |
| EP1755659A2 (en) | 2007-02-28 |
| EP1755659B1 (en) | 2011-11-02 |
| HK1101348A1 (en) | 2007-10-18 |
| NZ549893A (en) | 2010-05-28 |
| ES2376556T3 (es) | 2012-03-14 |
| WO2005092073A3 (en) | 2006-08-10 |
| CA2560508A1 (en) | 2005-10-06 |
| US7662384B2 (en) | 2010-02-16 |
| JP4857259B2 (ja) | 2012-01-18 |
| NO20064794L (no) | 2006-10-23 |
| AU2005226736B2 (en) | 2009-11-26 |
| BRPI0509177A (pt) | 2007-09-18 |
| US20100291111A1 (en) | 2010-11-18 |
| JP2007530584A (ja) | 2007-11-01 |
| US20050260210A1 (en) | 2005-11-24 |
| DK1755659T3 (da) | 2012-02-27 |
| KR20070009637A (ko) | 2007-01-18 |
| WO2005092073A2 (en) | 2005-10-06 |
| IL178042A0 (en) | 2006-12-31 |
| EP1755659A4 (en) | 2008-08-20 |
| ATE531388T1 (de) | 2011-11-15 |
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