JP2010500871A - 成熟セルトリ細胞およびその使用 - Google Patents
成熟セルトリ細胞およびその使用 Download PDFInfo
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- JP2010500871A JP2010500871A JP2009522979A JP2009522979A JP2010500871A JP 2010500871 A JP2010500871 A JP 2010500871A JP 2009522979 A JP2009522979 A JP 2009522979A JP 2009522979 A JP2009522979 A JP 2009522979A JP 2010500871 A JP2010500871 A JP 2010500871A
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| JPH09512015A (ja) * | 1994-04-13 | 1997-12-02 | リサーチ・コーポレイション・テクノロジーズ・インコーポレイテッド | セルトーリ細胞および同種移植片または異種移植片を用いる疾患処置方法 |
| WO2004113516A1 (en) * | 2003-06-24 | 2004-12-29 | Diabcell Pty Limited | Porcine islets cultured with porcine sertoli cells for xenotransplantation |
Family Cites Families (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5545223A (en) * | 1990-10-31 | 1996-08-13 | Baxter International, Inc. | Ported tissue implant systems and methods of using same |
| US5958404A (en) * | 1994-04-13 | 1999-09-28 | Research Corporation Technologies, Inc. | Treatment methods for disease using co-localized cells and Sertoli cells obtained from a cell line |
| US5849285A (en) * | 1994-04-13 | 1998-12-15 | Research Corporation Technologies, Inc. | Autoimmune disease treatment with sertoli cells and in vitro co-culture of mammal cells with sertoli cells |
| US5759536A (en) * | 1994-05-27 | 1998-06-02 | University Technology Corporation | Use of fas ligand to supress T-lymphocyte-mediated immune responses |
| MX9706062A (es) * | 1995-02-08 | 1997-10-31 | Yamanouchi Europ Bv | FORMAS DE DOSIFICACION ORAL CONTENIENDO UN ANTIBIOTICO DE beta -LACTAMA. |
| US5830460A (en) * | 1995-03-13 | 1998-11-03 | University Of South Florida | Sertoli cells as transplantation facilitator for cell transplantation |
| US20040086494A1 (en) * | 1996-10-07 | 2004-05-06 | John Constance Mary | Immune privileged cells for delivery of proteins and peptides |
| US20020065212A1 (en) * | 1996-11-08 | 2002-05-30 | Selawry Helena P. | Methods of treating disease using sertoli cells and allografts or xenografts |
| ES2338076T3 (es) * | 1998-11-06 | 2010-05-03 | Sertoli Technologies, Inc. | Produccion de un factor biologico y creacion de un entorno inmunologicamente privilegiado usando celulas de sertoli alteradas geneticamente. |
| CA2355675C (en) * | 1998-12-15 | 2006-07-04 | Universidad Nacional Autonoma De Mexico | Process and device for facilitating the implantation of biological material |
| US6303355B1 (en) * | 1999-03-22 | 2001-10-16 | Duke University | Method of culturing, cryopreserving and encapsulating pancreatic islet cells |
| US6365385B1 (en) * | 1999-03-22 | 2002-04-02 | Duke University | Methods of culturing and encapsulating pancreatic islet cells |
| ES2272482T3 (es) * | 2000-01-20 | 2007-05-01 | Diabcell Pty Limited | Preparacion y xenotransplante de islotes porcinos. |
| US6790441B1 (en) * | 2000-06-13 | 2004-09-14 | University Of South Florida | Sertoli cells as biochambers |
| US20040014212A1 (en) * | 2000-10-17 | 2004-01-22 | Elliott Robert Bartlett | Preparation and xenotransplantation or porcine islets |
| KR20030096381A (ko) * | 2001-05-11 | 2003-12-24 | 오쏘-맥네일 파머슈티칼 인코퍼레이티드 | 동물에 사용하기 위한 면역 조절장치 |
| US20050118145A1 (en) * | 2003-07-03 | 2005-06-02 | Jannette Dufour | Compositions containing sertoli cells and myoid cells and use thereof in cellular transplants |
| US20060182722A1 (en) * | 2005-02-11 | 2006-08-17 | Hering Bernhard J | Methods and materials for isolating isogenic islet cells |
-
2007
- 2007-07-27 AU AU2007278850A patent/AU2007278850B2/en not_active Ceased
- 2007-07-27 CA CA002658951A patent/CA2658951A1/en not_active Abandoned
- 2007-07-27 WO PCT/US2007/074623 patent/WO2008014470A2/en not_active Ceased
- 2007-07-27 EP EP07813488A patent/EP2046351A2/en not_active Withdrawn
- 2007-07-27 US US12/375,159 patent/US20090191167A1/en not_active Abandoned
- 2007-07-27 JP JP2009522979A patent/JP2010500871A/ja active Pending
-
2013
- 2013-11-27 JP JP2013245122A patent/JP2014074041A/ja not_active Ceased
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH09512015A (ja) * | 1994-04-13 | 1997-12-02 | リサーチ・コーポレイション・テクノロジーズ・インコーポレイテッド | セルトーリ細胞および同種移植片または異種移植片を用いる疾患処置方法 |
| WO2004113516A1 (en) * | 2003-06-24 | 2004-12-29 | Diabcell Pty Limited | Porcine islets cultured with porcine sertoli cells for xenotransplantation |
Non-Patent Citations (3)
| Title |
|---|
| JPN6012056880; Teng Y, et al.: 'Isolation and culture of adult Sertoli cells and their effects on the function of co-cultured alloge' Chinese Medical Journal Vol. 118, No. 22, 20051120, p. 1857-1862 * |
| JPN6012056882; Yang H, et al.: 'Co-encapsulation of Sertoli enriched testicular cell fractions further prolongs fish-to-mouse islet' Transplantation Vol. 67, No. 6, 19990327, p. 815-820 * |
| JPN6012056886; Francavilla S, et al.: 'Fas and Fas ligand expression in fetal and adult human testis with normal or deranged spermatogenesi' The Journal of Clinical Endocrinology & Metabolism Vol. 85, No. 8, 200008, p. 2692-2700 * |
Also Published As
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|---|---|
| AU2007278850B2 (en) | 2013-06-06 |
| EP2046351A2 (en) | 2009-04-15 |
| WO2008014470A3 (en) | 2008-09-18 |
| US20090191167A1 (en) | 2009-07-30 |
| AU2007278850A1 (en) | 2008-01-31 |
| WO2008014470A2 (en) | 2008-01-31 |
| CA2658951A1 (en) | 2008-01-31 |
| JP2014074041A (ja) | 2014-04-24 |
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