RU2009127846A - Антитела к рецептору инсулинподобного фактора роста i и их применения - Google Patents
Антитела к рецептору инсулинподобного фактора роста i и их применения Download PDFInfo
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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Abstract
1. Антитело, обладающее способностью к связыванию с IGF-IR и являющееся гликозилированным сахарной цепью на Asn297, где антитело отличается тем, что количество остатков фукозы в сахарной цепи составляет от 20 до 50%. ! 2. Антитело, обладающее способностью к связыванию с IGF-IR и являющееся гликозилированным сахарной цепью на Asn297, где антитело отличается тем, что количество остатков фукозы в сахарной цепи составляет от 20 до 50%, а количество NGNA составляет 1% или менее и/или количество N-концевой альфа-1,3-галактозы составляет 1% или менее. ! 3. Антитело, обладающее способностью к связыванию с IGF-IR и являющееся гликозилированным сахарной цепью на Asn297, где антитело отличается тем, что количество остатков фукозы в сахарной цепи составляет от 20 до 50% и представляет собой химерное, гуманизированное или человеческое антитело. ! 4. Антитело, обладающее способностью к связыванию с IGF-IR и являющееся гликозилированным сахарной цепью на Asn297, где антитело отличается тем, что количество остатков фукозы в сахарной цепи составляет от 20 до 50%, а количество NGNA составляет 1% или менее и/или количество N-концевой альфа-1,3-галактозы составляет 1% или менее и представляет собой химерное, гуманизированное или человеческое антитело. ! 5. Антитело по п.1, отличающееся тем, что оно обладает одним или несколькими свойствами, выбранными из группы, включающей: ! а) соотношение значений IC50, характеризующих ингибирование связывания IGF-I с IGF-IR и ингибирование связывания IGF-II с IGF-IR, составляет от 1:3 до 3:1; ! б) в концентрации 5 нМ ингибирует по меньшей мере на 80%, предпочтительно по меньшей мере на 90% фосфорилирование IGF-IR по данным клеточного анализа фосфорилирования с использ�
Claims (16)
1. Антитело, обладающее способностью к связыванию с IGF-IR и являющееся гликозилированным сахарной цепью на Asn297, где антитело отличается тем, что количество остатков фукозы в сахарной цепи составляет от 20 до 50%.
2. Антитело, обладающее способностью к связыванию с IGF-IR и являющееся гликозилированным сахарной цепью на Asn297, где антитело отличается тем, что количество остатков фукозы в сахарной цепи составляет от 20 до 50%, а количество NGNA составляет 1% или менее и/или количество N-концевой альфа-1,3-галактозы составляет 1% или менее.
3. Антитело, обладающее способностью к связыванию с IGF-IR и являющееся гликозилированным сахарной цепью на Asn297, где антитело отличается тем, что количество остатков фукозы в сахарной цепи составляет от 20 до 50% и представляет собой химерное, гуманизированное или человеческое антитело.
4. Антитело, обладающее способностью к связыванию с IGF-IR и являющееся гликозилированным сахарной цепью на Asn297, где антитело отличается тем, что количество остатков фукозы в сахарной цепи составляет от 20 до 50%, а количество NGNA составляет 1% или менее и/или количество N-концевой альфа-1,3-галактозы составляет 1% или менее и представляет собой химерное, гуманизированное или человеческое антитело.
5. Антитело по п.1, отличающееся тем, что оно обладает одним или несколькими свойствами, выбранными из группы, включающей:
а) соотношение значений IC50, характеризующих ингибирование связывания IGF-I с IGF-IR и ингибирование связывания IGF-II с IGF-IR, составляет от 1:3 до 3:1;
б) в концентрации 5 нМ ингибирует по меньшей мере на 80%, предпочтительно по меньшей мере на 90% фосфорилирование IGF-IR по данным клеточного анализа фосфорилирования с использованием клеток линии НТ29 в среде, содержащей 0,5% инактивированной тепловой обработкой фетальной телячьей сыворотки (FCS) и 10 нМ человеческий IGF-I, по сравнению с фосфорилированием по данным такого же анализа без использования антитела;
в) не обладает IGF-IR-стимулирующей активностью (отсутствие передачи сигнала, отсутствие IGF-1-подобной активности), измеряемой по фосфорилированию РКВ при применении в концентрации 10 мкМ в клеточном анализе фосфорилирования с использованием клеток линии 3Т3, имеющих 400000-600000 молекул IGF-IR на клетку, в среде, содержащей 0,5% инактивированной тепловой обработкой фетальной телячьей сыворотки (FCS) по сравнению с фосфорилированием в таком же анализе без использования антитела.
6. Антитело по п.2, отличающееся тем, что оно обладает одним или несколькими свойствами, выбранными из группы, включающей:
а) соотношение значений IC50, характеризующих ингибирование связывания IGF-I с IGF-IR и ингибирование связывания IGF-II с IGF-IR, составляет от 1:3 до 3:1;
б) в концентрации 5 нМ ингибирует по меньшей мере на 80%, предпочтительно по меньшей мере на 90% фосфорилирование IGF-IR по данным клеточного анализа фосфорилирования с использованием клеток линии НТ29 в среде, содержащей 0,5% инактивированной тепловой обработкой фетальной телячьей сыворотки (FCS) и 10 нМ человеческий IGF-I, по сравнению с фосфорилированием по данным такого же анализа без использования антитела;
в) не обладает IGF-IR-стимулирующей активностью (отсутствие передачи сигнала, отсутствие IGF-1-подобной активности), измеряемой по фосфорилированию РКВ при применении в концентрации 10 мкМ в клеточном анализе фосфорилирования с использованием клеток линии 3Т3, имеющих 400000-600000 молекул IGF-IR на клетку, в среде, содержащей 0,5% инактивированной тепловой обработкой фетальной телячьей сыворотки (FCS) по сравнению с фосфорилированием в таком же анализе без использования антитела.
7. Антитело по п.3, отличающееся тем, что оно обладает одним или несколькими свойствами, выбранными из группы, включающей:
а) соотношение значений IC50, характеризующих ингибирование связывания IGF-I с IGF-IR и ингибирование связывания IGF-II с IGF-IR, составляет от 1:3 до 3:1;
б) в концентрации 5 нМ ингибирует по меньшей мере на 80%, предпочтительно по меньшей мере на 90% фосфорилирование IGF-IR по данным клеточного анализа фосфорилирования с использованием клеток линии НТ29 в среде, содержащей 0,5% инактивированной тепловой обработкой фетальной телячьей сыворотки (FCS) и 10 нМ человеческий IGF-I, по сравнению с фосфорилированием по данным такого же анализа без использования антитела;
в) не обладает IGF-IR-стимулирующей активностью (отсутствие передачи сигнала, отсутствие IGF-1-подобной активности), измеряемой по фосфорилированию PKB при применении в концентрации 10 мкМ в клеточном анализе фосфорилирования с использованием клеток линии 3Т3, имеющих 400000-600000 молекул IGF-IR на клетку, в среде, содержащей 0,5% инактивированной тепловой обработкой фетальной телячьей сыворотки (FCS) по сравнению с фосфорилированием в таком же анализе без использования антитела.
8. Антитело по п.4, отличающееся тем, что оно обладает одним или несколькими свойствами, выбранными из группы, включающей:
а) соотношение значений IC50, характеризующих ингибирование связывания IGF-I с IGF-IR и ингибирование связывания IGF-II с IGF-IR, составляет от 1:3 до 3:1;
б) в концентрации 5 нМ ингибирует по меньшей мере на 80%, предпочтительно по меньшей мере на 90% фосфорилирование IGF-IR по данным клеточного анализа фосфорилирования с использованием клеток линии НТ29 в среде, содержащей 0,5% инактивированной тепловой обработкой фетальной телячьей сыворотки (FCS) и 10 нМ человеческий IGF-I, по сравнению с фосфорилированием по данным такого же анализа без использования антитела;
в) не обладает IGF-IR-стимулирующей активностью (отсутствие передачи сигнала, отсутствие IGF-1-подобной активности), измеряемой по фосфорилированию РКВ при применении в концентрации 10 мкМ в клеточном анализе фосфорилирования с использованием клеток линии 3Т3, имеющих 400000-600000 молекул IGF-IR на клетку, в среде, содержащей 0,5% инактивированной тепловой обработкой фетальной телячьей сыворотки (FCS) по сравнению с фосфорилированием в таком же анализе без использования антитела.
9. Антитело по п.1, отличающееся тем, что оно содержит в качестве гипервариабельных участков (CDR) следующие последовательности:
а) тяжелую цепь антитела, содержащую в качестве CDR CDR1 (ак 31-35), CDR2 (ак 50-66) и CDR3 (ак 99-107) последовательности, представленной в SEQ ID NO:1 или 3;
б) легкую цепь антитела, содержащую в качестве CDR CDR1 (ак 24-34), CDR2 (ак 50-56) и CDR3 (ак 89-98) последовательности, представленной в SEQ ID NO:2 или 4.
10. Антитело по п.2, отличающееся тем, что оно содержит в качестве гипервариабельных участков (CDR) следующие последовательности:
а) тяжелую цепь антитела, содержащую в качестве CDR CDR1 (ак 31-35), CDR2 (ак 50-66) и CDR3 (ак 99-107) последовательности, представленной в SEQ ID NO:1 или 3;
б) легкую цепь антитела, содержащую в качестве CDR CDR1 (ак 24-34), CDR2 (ак 50-56) и CDR3 (ак 89-98) последовательности, представленной в SEQ ID NO:2 или 4.
11. Антитело по п.3, отличающееся тем, что оно содержит в качестве гипервариабельных участков (CDR) следующие последовательности:
а) тяжелую цепь антитела, содержащую в качестве CDR CDR1 (ак 31-35), CDR2 (ак 50-66) и CDR3 (ак 99-107) последовательности, представленной в SEQ ID NO:1 или 3;
б) легкую цепь антитела, содержащую в качестве CDR CDR1 (ак 24-34), CDR2 (ак 50-56) и CDR3 (ак 89-98) последовательности, представленной в SEQ ID NO:2 или 4.
12. Антитело по п.4, отличающееся тем, что оно содержит в качестве гипервариабельных участков (CDR) следующие последовательности:
а) тяжелую цепь антитела, содержащую в качестве CDR CDR1 (ак 31-35), CDR2 (ак 50-66) и CDR3 (ак 99-107) последовательности, представленной в SEQ ID NO:1 или 3;
б) легкую цепь антитела, содержащую в качестве CDR CDR1 (ак 24-34), CDR2 (ак 50-56) и CDR3 (ак 89-98) последовательности, представленной в SEQ ID NO:2 или 4.
13. Применение антитела по пп.1-12 для приготовления фармацевтической композиции.
14. Фармацевтическая композиция, включающая антитело по любому из пп.1-12.
15. Применение антитела по пп.1-12 для приготовления фармацевтической композиции для лечения рака.
16. Применение антитела п.1 для приготовления фармацевтической композиции для лечения рака, где антитело применяют в сочетании с цитотоксическим агентом, его пролекарством или цитотоксической лучевой терапией.
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| Application Number | Priority Date | Filing Date | Title |
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| EP06026651.7 | 2006-12-22 | ||
| EP06026651 | 2006-12-22 |
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| RU2009127846A true RU2009127846A (ru) | 2011-01-27 |
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| US (2) | US20080226635A1 (ru) |
| EP (1) | EP2102242A1 (ru) |
| JP (1) | JP2010513352A (ru) |
| KR (2) | KR20120080663A (ru) |
| CN (1) | CN101611059A (ru) |
| AR (1) | AR064620A1 (ru) |
| AU (1) | AU2007338402A1 (ru) |
| BR (1) | BRPI0722062A2 (ru) |
| CA (1) | CA2672715A1 (ru) |
| CL (1) | CL2007003726A1 (ru) |
| CR (1) | CR10810A (ru) |
| EC (1) | ECSP099440A (ru) |
| IL (1) | IL198778A0 (ru) |
| MA (1) | MA31066B1 (ru) |
| MX (1) | MX2009006333A (ru) |
| NZ (1) | NZ576956A (ru) |
| PE (1) | PE20081832A1 (ru) |
| RU (1) | RU2009127846A (ru) |
| TW (1) | TW200833712A (ru) |
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| WO2009041613A1 (ja) | 2007-09-26 | 2009-04-02 | Chugai Seiyaku Kabushiki Kaisha | 抗体定常領域改変体 |
| US9266967B2 (en) | 2007-12-21 | 2016-02-23 | Hoffmann-La Roche, Inc. | Bivalent, bispecific antibodies |
| US20090162359A1 (en) | 2007-12-21 | 2009-06-25 | Christian Klein | Bivalent, bispecific antibodies |
| CN102356092B (zh) | 2009-03-20 | 2014-11-05 | 霍夫曼-拉罗奇有限公司 | 双特异性抗-her抗体 |
| TWI504409B (zh) | 2009-03-25 | 2015-10-21 | Genentech Inc | 新穎抗－α５β１抗體及其用途 |
| US20100247484A1 (en) * | 2009-03-31 | 2010-09-30 | Heinrich Barchet | Combination therapy of an afucosylated antibody and one or more of the cytokines gm csf, m csf and/or il3 |
| EP2236139A1 (en) * | 2009-03-31 | 2010-10-06 | F. Hoffmann-La Roche AG | Combination therapy of erlotinib with an anti-IGF-1R antibody, which does not inhibit binding of insulin to the insulin receptor |
| CN102369215B (zh) | 2009-04-02 | 2015-01-21 | 罗切格利卡特公司 | 包含全长抗体和单链Fab片段的多特异性抗体 |
| KR20110124368A (ko) | 2009-04-07 | 2011-11-16 | 로슈 글리카트 아게 | 이중특이적 항―ｅｒｂｂ―２／항―ｃ―ｍｅｔ 항체 |
| BRPI1010297A2 (pt) | 2009-04-07 | 2017-06-06 | Roche Glycart Ag | anticorpos biespecíficos trivalentes. |
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| AU2007338402A1 (en) | 2008-07-03 |
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| NZ576956A (en) | 2011-07-29 |
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| CN101611059A (zh) | 2009-12-23 |
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