LT3472B - Dna encoding a growth factor specific for epithelial cells - Google Patents
Dna encoding a growth factor specific for epithelial cells Download PDFInfo
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- LT3472B LT3472B LTIP667A LTIP667A LT3472B LT 3472 B LT3472 B LT 3472B LT IP667 A LTIP667 A LT IP667A LT IP667 A LTIP667 A LT IP667A LT 3472 B LT3472 B LT 3472B
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- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Dermatology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US30428189A | 1989-01-31 | 1989-01-31 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| LTIP667A LTIP667A (en) | 1995-01-31 |
| LT3472B true LT3472B (en) | 1995-10-25 |
Family
ID=23175833
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| LTIP667A LT3472B (en) | 1989-01-31 | 1993-06-21 | Dna encoding a growth factor specific for epithelial cells |
Country Status (22)
| Country | Link |
|---|---|
| US (8) | US6420531B1 (no) |
| EP (2) | EP1016716A3 (no) |
| JP (6) | JP3298874B2 (no) |
| KR (1) | KR950012805B1 (no) |
| AT (1) | ATE197800T1 (no) |
| AU (2) | AU647732B2 (no) |
| CA (2) | CA2038398C (no) |
| DE (2) | DE69033668T2 (no) |
| DK (1) | DK0555205T3 (no) |
| ES (1) | ES2153816T3 (no) |
| FI (1) | FI114711B (no) |
| GE (1) | GEP20022681B (no) |
| HU (1) | HU218090B (no) |
| IE (1) | IE20020188A1 (no) |
| LT (1) | LT3472B (no) |
| LU (1) | LU91237I2 (no) |
| LV (1) | LV10284B (no) |
| NL (1) | NL300230I2 (no) |
| NO (2) | NO308312B1 (no) |
| RU (1) | RU2250213C2 (no) |
| SG (1) | SG46699A1 (no) |
| WO (1) | WO1990008771A1 (no) |
Families Citing this family (49)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE197800T1 (de) | 1989-01-31 | 2000-12-15 | Jeffrey S Rubin | Dns kodierend für einen für epithelzellen spezifischen wachstumsfaktor |
| GB9203533D0 (en) * | 1992-02-19 | 1992-04-08 | Erba Carlo Spa | Use of the conjugate between a fibroblast growth factor and a saporin in treating ocular pathologies |
| US5814605A (en) * | 1993-03-26 | 1998-09-29 | Amgen Inc. | Therapeutic uses of keratinocyte growth factor |
| CZ285996B6 (cs) * | 1993-03-26 | 1999-12-15 | Amgen Inc. | Způsob in vitro stimulace produkce nekeratinocytových epithelových buněk a růstový faktor keratinocytů pro léčbu chorob |
| CZ343795A3 (en) * | 1993-06-29 | 1996-07-17 | Chiron Corp | Shortened keratinocyte growth factor /kgf/ exhibiting increased biological activity |
| US7084119B2 (en) | 1993-06-29 | 2006-08-01 | Chiron Corporation | Truncated keratinocyte growth factor (KGF) having increased biological activity |
| US6268212B1 (en) | 1993-10-18 | 2001-07-31 | Amgen Inc. | Tissue specific transgene expression |
| US6008328A (en) * | 1994-10-13 | 1999-12-28 | Amgen Inc. | Method for purifying keratinocyte growth factors |
| ES2197926T3 (es) * | 1994-10-13 | 2004-01-16 | Amgen Inc. | Metodo para purificar factores de crecimiento de queratinocitos. |
| HUT78069A (hu) * | 1994-10-13 | 1999-08-30 | Amgen Inc. | Keratinocita növekedési faktor analógok |
| CN1168678A (zh) * | 1994-10-13 | 1997-12-24 | 安姆根有限公司 | 用kgf治疗糖尿病的方法 |
| US6818439B1 (en) | 1994-12-30 | 2004-11-16 | Chiron Corporation | Methods for administration of recombinant gene delivery vehicles for treatment of hemophilia and other disorders |
| US6030613A (en) | 1995-01-17 | 2000-02-29 | The Brigham And Women's Hospital, Inc. | Receptor specific transepithelial transport of therapeutics |
| US7232667B2 (en) | 1995-02-14 | 2007-06-19 | Human Genome Sciences, Inc. | Keratinocyte growth factor-2 polynucleotides |
| US6077692A (en) * | 1995-02-14 | 2000-06-20 | Human Genome Sciences, Inc. | Keratinocyte growth factor-2 |
| US6693077B1 (en) | 1995-02-14 | 2004-02-17 | Human Genome Sciences, Inc. | Keratinocyte growth factor-2 |
| DE69637332T2 (de) | 1995-10-11 | 2008-10-09 | Novartis Vaccines and Diagnostics, Inc., Emeryville | Kombinierung von PDGF, KGF, IGF und IGFBP für Wundheilung |
| US6692961B1 (en) | 1996-10-11 | 2004-02-17 | Invitrogen Corporation | Defined systems for epithelial cell culture and use thereof |
| US20030144202A1 (en) * | 1996-10-15 | 2003-07-31 | Amgen Inc. | Uses of keratinocyte growth factor-2 |
| US6743422B1 (en) | 1996-10-15 | 2004-06-01 | Amgen, Inc. | Keratinocyte growth factor-2 products |
| DE19716098A1 (de) * | 1997-04-17 | 1998-10-22 | Univ Ludwigs Albert | Fibroblasten mit einem Fremdgen enthaltende Zusammensetzung zur Behandlung von Wunden |
| US6228839B1 (en) | 1997-12-19 | 2001-05-08 | Emory University | Use of keratinocyte growth factor to improve oxidative status |
| US6869927B1 (en) | 1997-12-22 | 2005-03-22 | Human Genome Sciences, Inc. | Keratinocyte growth factor-2 formulations |
| KR20010033484A (ko) * | 1997-12-22 | 2001-04-25 | 휴먼 게놈 사이언시즈, 인크. | 각질세포 성장 인자-2 제제 |
| AU762519B2 (en) * | 1998-02-13 | 2003-06-26 | Human Genome Sciences, Inc. | Therapeutic uses of keratinocyte growth factor-2 |
| US6335317B1 (en) | 1998-04-10 | 2002-01-01 | Emory University | Use of gut-trophic growth factors to improve oxidative status |
| US7022683B1 (en) | 1998-05-13 | 2006-04-04 | Carrington Laboratories, Inc. | Pharmacological compositions comprising pectins having high molecular weights and low degrees of methoxylation |
| US6313103B1 (en) | 1998-05-13 | 2001-11-06 | Carrington Laboratories, Inc. | Pectic substance as a growth factor stabilizer |
| US5929051A (en) * | 1998-05-13 | 1999-07-27 | Carrington Laboratories, Inc. | Aloe pectins |
| US6372494B1 (en) * | 1999-05-14 | 2002-04-16 | Advanced Tissue Sciences, Inc. | Methods of making conditioned cell culture medium compositions |
| US6783546B2 (en) | 1999-09-13 | 2004-08-31 | Keraplast Technologies, Ltd. | Implantable prosthetic or tissue expanding device |
| US6371984B1 (en) | 1999-09-13 | 2002-04-16 | Keraplast Technologies, Ltd. | Implantable prosthetic or tissue expanding device |
| US6395414B1 (en) | 2000-02-11 | 2002-05-28 | General Motors Corporation | Staged venting of fuel cell system during rapid shutdown |
| US6376112B1 (en) | 2000-02-11 | 2002-04-23 | General Motors Corporation | Controlled shutdown of a fuel cell |
| US6413662B1 (en) | 2000-02-22 | 2002-07-02 | General Motors Corporation | Fuel cell system shutdown with anode pressure control |
| JP2001302691A (ja) * | 2000-04-17 | 2001-10-31 | Nichirei Corp | ヒトｋｇｆに対する抗体 |
| AU2002309473A1 (en) * | 2001-01-08 | 2002-10-08 | Human Genome Sciences, Inc. | Keratinocyte growth factor-2 |
| WO2002069232A2 (en) | 2001-02-19 | 2002-09-06 | Merck Patent Gmbh | Method for identification of t-cell epitopes and use for preparing molecules with reeduced immunogenicity |
| US7494669B2 (en) | 2001-02-28 | 2009-02-24 | Carrington Laboratories, Inc. | Delivery of physiological agents with in-situ gels comprising anionic polysaccharides |
| MXPA04001526A (es) * | 2001-08-21 | 2004-05-31 | Chiron Corp | Composiciones de polipetidos kgf. |
| US7202066B2 (en) * | 2002-01-29 | 2007-04-10 | Carrington Laboratories, Inc. | Combination of a growth factor and a protease enzyme |
| GB0206309D0 (en) * | 2002-03-16 | 2002-05-01 | Axordia Ltd | Isolated cells |
| WO2004019001A2 (en) * | 2002-08-20 | 2004-03-04 | Curagen Corporation | Methods for diagnosing and treatment of conditions that alter phosphate transport in mammals |
| US8304387B2 (en) | 2004-12-15 | 2012-11-06 | Swedish Orphan Biovitrum Ab (Publ) | Therapeutic formulations of keratinocyte growth factor |
| US20080119433A1 (en) * | 2006-07-06 | 2008-05-22 | Aaron Thomas Tabor | Compositions and Methods for Genetic Modification of Cells Having Cosmetic Function to Enhance Cosmetic Appearance |
| CN101679495B (zh) * | 2007-01-05 | 2013-07-17 | 赫里克斯生物医疗公司 | 用于细胞学和免疫学调节的短的生物活性肽 |
| BR112012000865A2 (pt) * | 2009-07-17 | 2019-09-24 | T Tabor Aaron | "composição e método para a modificação genética cosmética de células substancialmente intactas" |
| WO2013149258A2 (en) | 2012-03-30 | 2013-10-03 | Charles Drew University of Medicine and Science | Compositions and methods for treating or preventing metabolic syndrome disorders |
| KR102277147B1 (ko) * | 2017-12-13 | 2021-07-13 | 건국대학교 산학협력단 | 섬유아 성장인자 유래 펩타이드의 골 또는 연골 분화 촉진 용도 |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5096825A (en) * | 1983-01-12 | 1992-03-17 | Chiron Corporation | Gene for human epidermal growth factor and synthesis and expression thereof |
| US4444760A (en) * | 1983-06-17 | 1984-04-24 | Merck & Co., Inc. | Purification and characterization of a protein fibroblast growth factor |
| US4473679A (en) | 1983-12-12 | 1984-09-25 | Borg-Warner Chemicals, Inc. | Thermoplastic acrylic elastomers |
| US4743679A (en) * | 1986-02-24 | 1988-05-10 | Creative Biomolecules, Inc. | Process for producing human epidermal growth factor and analogs thereof |
| US4868113A (en) | 1986-03-03 | 1989-09-19 | Rorer Biotechnology, Inc. | Recombinant DNA vector encoding human endothelial cell growth factor |
| US4983679A (en) | 1986-05-29 | 1991-01-08 | E. I. Dupont De Nemours And Company | β-(keto or sulfonyl)esters from reaction of silylketene acetal and acyl or sulfonyl compound |
| AU617795B2 (en) | 1988-03-17 | 1991-12-05 | Leukotech A/S | Heparin-binding proteins, dna coding for them, processes for producing them as well as therapeutic preparations containing them |
| ATE197800T1 (de) | 1989-01-31 | 2000-12-15 | Jeffrey S Rubin | Dns kodierend für einen für epithelzellen spezifischen wachstumsfaktor |
| CZ343795A3 (en) | 1993-06-29 | 1996-07-17 | Chiron Corp | Shortened keratinocyte growth factor /kgf/ exhibiting increased biological activity |
| CN1168678A (zh) | 1994-10-13 | 1997-12-24 | 安姆根有限公司 | 用kgf治疗糖尿病的方法 |
-
1990
- 1990-01-30 AT AT90903253T patent/ATE197800T1/de active
- 1990-01-30 HU HU998/90A patent/HU218090B/hu unknown
- 1990-01-30 WO PCT/US1990/000418 patent/WO1990008771A1/en active IP Right Grant
- 1990-01-30 SG SG1996008633A patent/SG46699A1/en unknown
- 1990-01-30 RU SU5001740/13A patent/RU2250213C2/ru active
- 1990-01-30 EP EP00103140A patent/EP1016716A3/en not_active Withdrawn
- 1990-01-30 DK DK90903253T patent/DK0555205T3/da active
- 1990-01-30 ES ES90903253T patent/ES2153816T3/es not_active Expired - Lifetime
- 1990-01-30 GE GEAP1990983A patent/GEP20022681B/en unknown
- 1990-01-30 EP EP90903253A patent/EP0555205B1/en not_active Expired - Lifetime
- 1990-01-30 JP JP50341390A patent/JP3298874B2/ja not_active Expired - Lifetime
- 1990-01-30 DE DE69033668T patent/DE69033668T2/de not_active Expired - Lifetime
- 1990-01-30 AU AU50496/90A patent/AU647732B2/en not_active Expired
- 1990-01-31 IE IE20020188A patent/IE20020188A1/en not_active Application Discontinuation
- 1990-09-29 KR KR90702202A patent/KR950012805B1/ko not_active IP Right Cessation
-
1991
- 1991-03-15 CA CA002038398A patent/CA2038398C/en not_active Expired - Lifetime
- 1991-03-15 CA CA2349875A patent/CA2349875C/en not_active Expired - Lifetime
- 1991-07-30 FI FI913637A patent/FI114711B/fi active
-
1992
- 1992-12-23 LV LVP-92-410A patent/LV10284B/xx unknown
-
1993
- 1993-06-21 LT LTIP667A patent/LT3472B/lt not_active IP Right Cessation
-
1994
- 1994-06-28 AU AU65986/94A patent/AU684278B2/en not_active Expired
-
1995
- 1995-05-31 US US08/455,620 patent/US6420531B1/en not_active Expired - Lifetime
- 1995-05-31 US US08/455,655 patent/US5654405A/en not_active Expired - Lifetime
- 1995-05-31 US US08/455,641 patent/US5707805A/en not_active Expired - Lifetime
- 1995-05-31 US US08/455,975 patent/US6833132B1/en not_active Expired - Lifetime
- 1995-05-31 US US08/455,628 patent/US5665870A/en not_active Expired - Lifetime
- 1995-05-31 US US08/455,672 patent/US5741642A/en not_active Expired - Lifetime
- 1995-06-07 US US08/480,948 patent/US5731170A/en not_active Expired - Lifetime
- 1995-06-07 US US08/477,982 patent/US6709842B1/en not_active Expired - Lifetime
- 1995-12-27 JP JP7341890A patent/JP2716416B2/ja not_active Expired - Lifetime
-
1997
- 1997-05-16 NO NO972259A patent/NO308312B1/no not_active IP Right Cessation
- 1997-06-06 NO NO972617A patent/NO308310B1/no not_active IP Right Cessation
- 1997-10-22 JP JP09290175A patent/JP3088983B2/ja not_active Expired - Lifetime
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1999
- 1999-10-06 JP JP28551799A patent/JP3802292B2/ja not_active Expired - Lifetime
-
2000
- 2000-10-11 JP JP2000311208A patent/JP3802329B2/ja not_active Expired - Lifetime
-
2006
- 2006-03-06 JP JP2006060217A patent/JP2006149407A/ja not_active Withdrawn
- 2006-04-11 DE DE200612000021 patent/DE122006000021I1/de active Pending
- 2006-04-19 NL NL300230C patent/NL300230I2/nl unknown
- 2006-04-24 LU LU91237C patent/LU91237I2/fr unknown
Non-Patent Citations (5)
| Title |
|---|
| MACIAG T. ET AL.: "Heparin binds endothelial cell growth factor, the principal endothelial cell mitogen in bovine brain", PROC NATL ACAD SCI U S A., 1984, pages 932 - 935 |
| MACIAG T. ET AL.: "Heparin binds endothelial cell growth factor, the principal endothelial cell mitogen in bovine brain", SCIENCE, 1984, pages 932 - 935 |
| RAINES EW, ROSS R.: "Platelet-derived growth factor. I. High yield purification and evidence for multiple forms.", J BIOL CHEM., 1982 |
| U. K. LAEMMLI: "Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4", NATURE, 1970, pages 680 - 685, XP055108426, DOI: doi:10.1038/227680a0 |
| WRIGHT N. AND ALLISON M.: "The Biology of Epitelial Cell Populations", pages: 3 - 5 |
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