ZA200703528B - Immunotherapeutic formulations with Interleukin-2-neutralising capacity - Google Patents
Immunotherapeutic formulations with Interleukin-2-neutralising capacity Download PDFInfo
- Publication number
- ZA200703528B ZA200703528B ZA200703528A ZA200703528A ZA200703528B ZA 200703528 B ZA200703528 B ZA 200703528B ZA 200703528 A ZA200703528 A ZA 200703528A ZA 200703528 A ZA200703528 A ZA 200703528A ZA 200703528 B ZA200703528 B ZA 200703528B
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- South Africa
- Prior art keywords
- immune response
- elicit
- response against
- therapeutic formulation
- hil
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Classifications
-
- 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
-
- 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
- A61K39/0005—Vertebrate antigens
-
- 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
- A61K39/0005—Vertebrate antigens
- A61K39/0011—Cancer 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
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/55—IL-2
-
- 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
- A61K2039/60—Medicinal preparations containing antigens or antibodies characteristics by the carrier linked to the antigen
- A61K2039/6031—Proteins
- A61K2039/6068—Other bacterial proteins, e.g. OMP
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Immunology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Organic Chemistry (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Microbiology (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Oncology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CU20040261A CU23297A1 (es) | 2004-11-16 | 2004-11-16 | Formulaciones inmunoterapã0/00uticas para la inducciã"n de autoanticuerpos bloqueadores de la uniã"n de interleucina-2 a su receptor. su uso en el tratamiento del cã ncer |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ZA200703528B true ZA200703528B (en) | 2008-06-25 |
Family
ID=40122436
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ZA200703528A ZA200703528B (en) | 2004-11-16 | 2007-05-02 | Immunotherapeutic formulations with Interleukin-2-neutralising capacity |
Country Status (25)
| Country | Link |
|---|---|
| US (1) | US20090274647A1 (ja) |
| EP (2) | EP2112160B1 (ja) |
| JP (1) | JP5227028B2 (ja) |
| KR (1) | KR101240457B1 (ja) |
| CN (1) | CN101061136B (ja) |
| AR (1) | AR051494A1 (ja) |
| AT (1) | ATE525393T1 (ja) |
| AU (1) | AU2005306186B2 (ja) |
| BR (1) | BRPI0518007A (ja) |
| CA (1) | CA2588573C (ja) |
| CR (1) | CR9097A (ja) |
| CU (1) | CU23297A1 (ja) |
| EA (1) | EA012072B1 (ja) |
| GE (1) | GEP20105039B (ja) |
| HK (1) | HK1113374A1 (ja) |
| MA (1) | MA29044B1 (ja) |
| MX (1) | MX2007005808A (ja) |
| MY (1) | MY162106A (ja) |
| PE (1) | PE20061172A1 (ja) |
| SG (1) | SG122897A1 (ja) |
| TN (1) | TNSN07187A1 (ja) |
| TR (1) | TR200704213T2 (ja) |
| TW (1) | TWI433853B (ja) |
| WO (1) | WO2006053508A1 (ja) |
| ZA (1) | ZA200703528B (ja) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2009542592A (ja) * | 2006-07-06 | 2009-12-03 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフツング | Ｉｌ−２媒介性免疫応答の有効性を高める組成物および方法 |
| US10114018B2 (en) | 2014-04-22 | 2018-10-30 | INSERM (Institut National de la Santé et de la Recherche Médicale) | IL-2 peptide derivatives, and uses thereof for the diagnosis and treatment of an autoimmune disease |
| TW201722989A (zh) * | 2015-10-23 | 2017-07-01 | 輝瑞大藥廠 | 抗il-2抗體及其組合物及用途 |
| CU20210021A7 (es) * | 2021-03-30 | 2022-11-07 | Ct Inmunologia Molecular | Composicones vacunales depletantes de factores de crecimiento hematopoyéticos para el tratamiento de enfermedades inflamatorias |
Family Cites Families (25)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5939832A (ja) * | 1982-08-28 | 1984-03-05 | Ajinomoto Co Inc | モノクロ−ナル抗体ならびにその製法、使用法 |
| EP0111344A2 (en) * | 1982-12-13 | 1984-06-20 | Sloan-Kettering Institute For Cancer Research | Anti-interleukin-2 monoclonal antibodies |
| US4569790A (en) * | 1984-03-28 | 1986-02-11 | Cetus Corporation | Process for recovering microbially produced interleukin-2 and purified recombinant interleukin-2 compositions |
| US5643565A (en) * | 1985-09-20 | 1997-07-01 | Chiron Corporation | Human IL-2 as a vaccine adjuvant |
| WO1991001146A1 (en) * | 1989-07-14 | 1991-02-07 | Praxis Biologics, Inc. | Cytokine and hormone carriers for conjugate vaccines |
| HUT60768A (en) * | 1990-03-16 | 1992-10-28 | Sandoz Ag | Process for producing cd25 fixing molecules |
| CU22302A1 (es) * | 1990-09-07 | 1995-01-31 | Cigb | Secuencia nucleotidica codificante para una proteina de la membrana externa de neisseria meningitidis y uso de dicha proteina en preparados vacunales |
| US5830452A (en) * | 1990-11-20 | 1998-11-03 | Chiron Corporation | Method for enhancing the anti-tumor therapeutic index of interleukin-2 |
| JPH10147952A (ja) | 1996-11-18 | 1998-06-02 | Komatsu Ltd | ブルドーザのドージング装置 |
| US20040156824A1 (en) * | 1996-12-23 | 2004-08-12 | Epstein Alan L. | Vasopermeability enhancing peptide of human interleukin-2 and immunoconjugates thereof |
| CA2219961C (en) * | 1998-01-09 | 2010-06-01 | The University Of Southern California | Vasopermeability enhancing peptide of human interleukin-2 and immunoconjugates thereof |
| CU22731A1 (es) * | 1998-02-05 | 2002-02-28 | Centro Inmunologia Molecular | Anticuerpo monoclonal que reconoce el oligosacárido ácido siálico n´glicolilado-galactosa-glucosa (ngcneu-gal-glu) en tumores malignos y composiciones farmacéuticas que los contienen |
| US6168785B1 (en) * | 1998-07-16 | 2001-01-02 | Institut Pasteur | Biological applications of new peptides of IL-2 and derivatives and use as therapeutic agents |
| PL200919B1 (pl) * | 1999-02-12 | 2009-02-27 | Lexigen Pharm Corp | Zastosowanie kompozycji czynnika hamującego angiogenezę i czynnika przeciwnowotworowego, kompozycja terapeutyczna do leczenia nowotworów i zestaw do traktowania komórki nowotworowej |
| AU2001259253A1 (en) * | 2000-04-26 | 2001-11-07 | National Jewish Medical And Research Center | Product and process for regulation of t cell responses |
| CU23011A1 (es) * | 2000-11-03 | 2004-12-17 | Ct Ingenieria Genetica Biotech | Método de obtención de estructuras antigénicas quemétodo de obtención de estructuras antigénicas que potencian la reactividad cruzada específica y su potencian la reactividad cruzada específica y su uso en formulaciones uso en formulaciones |
| CU23077A1 (es) * | 2000-12-06 | 2005-08-17 | Centro Inmunologia Molecular | Composicion vacunal que contiene factor de crecimiento transformante (tgf-alfa). su uso en la terapia de enfermedades malignas |
| CU22979A1 (es) * | 2000-12-08 | 2004-09-09 | Centro Inmunologia Molecular | Combinación inmunoterapéutica para el tratamiento de tumores que sobre-expresan receptores con actividad quinasa en residuos de tirosina |
| CU22999A1 (es) * | 2001-12-04 | 2004-10-12 | Centro Inmunologia Molecular | Método de tratamiento de enfermedades malignas e infecciosas crónicas |
| WO2002087304A2 (de) * | 2001-04-30 | 2002-11-07 | Frohnhofen, Wilfried | Il2-peptide; von interleukin 2 abgeleitete peptide und peptid-dimere |
| US6906169B2 (en) * | 2001-05-25 | 2005-06-14 | United Biomedical, Inc. | Immunogenic peptide composition comprising measles virus Fprotein Thelper cell epitope (MUFThl-16) and N-terminus of β-amyloid peptide |
| ITMI20012527A1 (it) | 2001-11-30 | 2003-05-30 | Unihart Corp | Proteine di fusione contenenti peptidi tlp |
| JP4364643B2 (ja) * | 2001-11-30 | 2009-11-18 | アメリカ合衆国 | 前立腺特異抗原のペプチドアゴニストおよびその使用 |
| US20040208869A1 (en) * | 2003-01-30 | 2004-10-21 | Medimmune, Inc. | Uses of anti-integrin alphanubeta3 antibody formulations |
| US7569215B2 (en) * | 2003-07-18 | 2009-08-04 | Massachusetts Institute Of Technology | Mutant interleukin-2 (IL-2) polypeptides |
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2004
- 2004-11-16 CU CU20040261A patent/CU23297A1/es unknown
-
2005
- 2005-11-15 AR ARP050104787A patent/AR051494A1/es not_active Application Discontinuation
- 2005-11-15 PE PE2005001336A patent/PE20061172A1/es not_active Application Discontinuation
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- 2005-11-16 MX MX2007005808A patent/MX2007005808A/es active IP Right Grant
- 2005-11-16 SG SG200507053A patent/SG122897A1/en unknown
- 2005-11-16 GE GEAP200510066A patent/GEP20105039B/en unknown
- 2005-11-16 WO PCT/CU2005/000009 patent/WO2006053508A1/es active Application Filing
- 2005-11-16 EP EP09164216.5A patent/EP2112160B1/en active Active
- 2005-11-16 US US11/719,326 patent/US20090274647A1/en not_active Abandoned
- 2005-11-16 MY MYPI20055353A patent/MY162106A/en unknown
- 2005-11-16 AT AT05811052T patent/ATE525393T1/de not_active IP Right Cessation
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- 2005-11-16 KR KR1020077010317A patent/KR101240457B1/ko not_active IP Right Cessation
- 2005-11-16 TW TW094140326A patent/TWI433853B/zh not_active IP Right Cessation
- 2005-11-16 AU AU2005306186A patent/AU2005306186B2/en not_active Ceased
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2007
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- 2007-05-04 CR CR9097A patent/CR9097A/es not_active Application Discontinuation
- 2007-05-15 TN TNP2007000187A patent/TNSN07187A1/fr unknown
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