JP2002536018A5 - - Google Patents
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- Publication number
- JP2002536018A5 JP2002536018A5 JP2000598639A JP2000598639A JP2002536018A5 JP 2002536018 A5 JP2002536018 A5 JP 2002536018A5 JP 2000598639 A JP2000598639 A JP 2000598639A JP 2000598639 A JP2000598639 A JP 2000598639A JP 2002536018 A5 JP2002536018 A5 JP 2002536018A5
- Authority
- JP
- Japan
- Prior art keywords
- glycosylated
- seq
- protein
- nucleic acid
- glycosylated leptin
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- NRYBAZVQPHGZNS-ZSOCWYAHSA-N leptin Chemical class O=C([C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CC(C)C)CCSC)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CS)C(O)=O NRYBAZVQPHGZNS-ZSOCWYAHSA-N 0.000 description 34
- 235000018102 proteins Nutrition 0.000 description 24
- 102000004169 proteins and genes Human genes 0.000 description 24
- 108090000623 proteins and genes Proteins 0.000 description 24
- 210000004027 cell Anatomy 0.000 description 21
- 150000007523 nucleic acids Chemical class 0.000 description 20
- 108020004707 nucleic acids Proteins 0.000 description 14
- 102000039446 nucleic acids Human genes 0.000 description 14
- 230000013595 glycosylation Effects 0.000 description 9
- 238000006206 glycosylation reaction Methods 0.000 description 9
- 108091028043 Nucleic acid sequence Proteins 0.000 description 8
- 108010076504 Protein Sorting Signals Proteins 0.000 description 8
- 238000000034 method Methods 0.000 description 8
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 7
- 125000003275 alpha amino acid group Chemical group 0.000 description 7
- 235000001014 amino acid Nutrition 0.000 description 6
- 101001063991 Homo sapiens Leptin Proteins 0.000 description 5
- 102000035195 Peptidases Human genes 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 5
- 150000001413 amino acids Chemical class 0.000 description 5
- 238000003776 cleavage reaction Methods 0.000 description 5
- 102000049953 human LEP Human genes 0.000 description 5
- 239000008194 pharmaceutical composition Substances 0.000 description 5
- 235000019833 protease Nutrition 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- 239000004475 Arginine Substances 0.000 description 4
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 4
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 4
- 102000035122 glycosylated proteins Human genes 0.000 description 4
- 108091005608 glycosylated proteins Proteins 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 239000013598 vector Substances 0.000 description 4
- 238000012258 culturing Methods 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- 241000282693 Cercopithecidae Species 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 208000008589 Obesity Diseases 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 235000020824 obesity Nutrition 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 125000005629 sialic acid group Chemical group 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- -1 CD11α Chemical compound 0.000 description 1
- 108010075016 Ceruloplasmin Proteins 0.000 description 1
- 102100023321 Ceruloplasmin Human genes 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 108010014612 Follistatin Proteins 0.000 description 1
- 102000016970 Follistatin Human genes 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090000467 Interferon-beta Proteins 0.000 description 1
- 102000003996 Interferon-beta Human genes 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 229940029329 intrinsic factor Drugs 0.000 description 1
- 229940039781 leptin Drugs 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 108010047303 von Willebrand Factor Proteins 0.000 description 1
- 102100036537 von Willebrand factor Human genes 0.000 description 1
- 229960001134 von willebrand factor Drugs 0.000 description 1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US24967599A | 1999-02-12 | 1999-02-12 | |
| US09/249,675 | 1999-02-12 | ||
| PCT/US2000/003652 WO2000047741A1 (en) | 1999-02-12 | 2000-02-11 | Glycosylated leptin compositions and related methods |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2002536018A JP2002536018A (ja) | 2002-10-29 |
| JP2002536018A5 true JP2002536018A5 (enExample) | 2006-11-30 |
| JP4841037B2 JP4841037B2 (ja) | 2011-12-21 |
Family
ID=22944511
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000598639A Expired - Fee Related JP4841037B2 (ja) | 1999-02-12 | 2000-02-11 | グリコシル化レプチン組成物および関連する方法 |
Country Status (11)
| Country | Link |
|---|---|
| EP (1) | EP1151102B1 (enExample) |
| JP (1) | JP4841037B2 (enExample) |
| AT (1) | ATE323766T1 (enExample) |
| AU (1) | AU781460B2 (enExample) |
| CA (1) | CA2359840C (enExample) |
| CY (1) | CY1107470T1 (enExample) |
| DE (1) | DE60027409T2 (enExample) |
| DK (1) | DK1151102T3 (enExample) |
| ES (1) | ES2257287T3 (enExample) |
| PT (1) | PT1151102E (enExample) |
| WO (1) | WO2000047741A1 (enExample) |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002079415A2 (en) * | 2001-03-30 | 2002-10-10 | Lexigen Pharmaceuticals Corp. | Reducing the immunogenicity of fusion proteins |
| WO2003020303A1 (en) * | 2001-08-29 | 2003-03-13 | The University Of Buckingham | Use of leptin for infant with low birth weight for prevention of obesity |
| PL214862B1 (pl) * | 2001-10-22 | 2013-09-30 | Amgen | Sposób in vitro do okreslania predyspozycji pacjenta ludzkiego z lipoatrofia do reagowania na leczenie bialkiem leptyny, kompozycje farmaceutyczne do zastosowania do leczenia lipoatrofii i kompozycje farmaceutyczne zawierajace bialko leptyny |
| US7094579B2 (en) * | 2002-02-13 | 2006-08-22 | Xoma Technology Ltd. | Eukaryotic signal sequences for prokaryotic expression |
| US20040248262A1 (en) | 2003-01-22 | 2004-12-09 | Koeberl Dwight D. | Constructs for expressing lysomal polypeptides |
| US20070141666A1 (en) | 2003-09-26 | 2007-06-21 | Applied Research Systems Ars Holding N.V. | Leader sequences for use in production of proteins |
| HUE026826T2 (en) | 2004-10-29 | 2016-07-28 | Ratiopharm Gmbh | Modeling and glycopegylation of fibroblast growth factor (FGF) |
| WO2008067599A1 (en) * | 2006-12-04 | 2008-06-12 | Apollo Life Sciences Limited | Isolated leptin and adiponectin molecules and chimeric molecules thereof |
| JP5876649B2 (ja) | 2007-06-12 | 2016-03-02 | ラツィオファルム ゲーエムベーハーｒａｔｉｏｐｈａｒｍ ＧｍｂＨ | ヌクレオチド糖の改良製造法 |
| JP2009126856A (ja) * | 2007-11-28 | 2009-06-11 | Fancl Corp | 血中中性脂肪上昇抑制剤 |
| JP5622720B2 (ja) | 2008-05-21 | 2014-11-12 | ニューロテスインコーポレイテッド | 神経原繊維変化に関連する進行性認知障害の治療方法 |
| US8501686B2 (en) | 2008-06-05 | 2013-08-06 | University Of Michigan | Method of treating fatty liver diseases and conditions in non-lipodystrophic subjects |
| JP2012508242A (ja) | 2008-11-04 | 2012-04-05 | ニコラオス テザプシディス | 神経原線維のもつれ及びアミロイドβの蓄積に起因する進行性認知機能障害を治療するためのレプチン組成物及び方法 |
| EA024507B1 (ru) | 2010-09-28 | 2016-09-30 | Амилин Фармасьютикалс, Ллк | Хорошо растворимые лептины |
| CN108524919A (zh) | 2012-05-17 | 2018-09-14 | 延伸生物科学股份有限公司 | 用于改进的药物递送的载体 |
| EP3434268B1 (en) | 2012-09-27 | 2022-04-20 | The Children's Medical Center Corporation | Compounds for the treatment of obesity and methods of use thereof |
| TR201901299T4 (tr) | 2013-11-26 | 2019-02-21 | Childrens Medical Ct Corp | Obezite tedavisine yönelik bileşikler ve bunların kullanım yöntemleri. |
| WO2015153933A1 (en) | 2014-04-03 | 2015-10-08 | The Children's Medical Center Corporation | Hsp90 inhibitors for the treatment of obesity and methods of use thereof |
| US9789197B2 (en) | 2014-10-22 | 2017-10-17 | Extend Biosciences, Inc. | RNAi vitamin D conjugates |
| WO2016065052A1 (en) | 2014-10-22 | 2016-04-28 | Extend Biosciences, Inc. | Insulin vitamin d conjugates |
| WO2016065042A1 (en) | 2014-10-22 | 2016-04-28 | Extend Biosciences, Inc. | Therapeutic vitamin d conjugates |
| CN110267674A (zh) * | 2016-07-08 | 2019-09-20 | 奥美药业有限公司 | 包含瘦素的融合蛋白及其生产和使用方法 |
| EP3509624B1 (en) | 2016-09-12 | 2023-08-09 | Amryt Pharmaceuticals Inc. | Methods of detecting anti-leptin neutralizing antibodies |
| JP2025534350A (ja) | 2022-09-30 | 2025-10-15 | エクステンド バイオサイエンシズ インコーポレーテッド | 長時間作用型副甲状腺ホルモン |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5326700A (en) * | 1990-11-06 | 1994-07-05 | Eli Lilly And Company | DNA sequences encoding t-PA derivatives with cleavable sites |
| ZA946122B (en) * | 1993-08-17 | 1995-03-20 | Amgen Inc | Erythropoietin analogs |
| US6309853B1 (en) * | 1994-08-17 | 2001-10-30 | The Rockfeller University | Modulators of body weight, corresponding nucleic acids and proteins, and diagnostic and therapeutic uses thereof |
| AU4766596A (en) * | 1995-01-31 | 1996-08-21 | Eli Lilly And Company | Ob gene product antibodies |
| ES2217327T3 (es) * | 1995-11-22 | 2004-11-01 | Amgen Inc., | Proteina ob para aumentar la masa de tejido magro. |
| AU1406497A (en) * | 1995-12-06 | 1997-06-27 | Schering Corporation | Mutational variants of mammalian ob gene proteins |
| JPH09176198A (ja) * | 1995-12-28 | 1997-07-08 | Kikkoman Corp | 抗肥満タンパク質モノクローナル抗体及びハイブリドーマ |
| EP0877627A1 (en) * | 1996-01-25 | 1998-11-18 | Eli Lilly And Company | Obesity protein analog compounds and formulations thereof |
| EP0827750A3 (en) * | 1996-08-23 | 2002-11-20 | Eli Lilly And Company | Obesity protein formulations |
| AU1208599A (en) * | 1997-10-31 | 1999-05-24 | Eli Lilly And Company | Glycosylated obesity protein analogs |
| PT1107793E (pt) * | 1998-08-10 | 2005-02-28 | Amgen Inc | Conjugados de dextrano-leptina, composicoes farmaceuticas e processos relacionados |
| US6420339B1 (en) * | 1998-10-14 | 2002-07-16 | Amgen Inc. | Site-directed dual pegylation of proteins for improved bioactivity and biocompatibility |
-
2000
- 2000-02-11 CA CA2359840A patent/CA2359840C/en not_active Expired - Fee Related
- 2000-02-11 AT AT00911784T patent/ATE323766T1/de active
- 2000-02-11 JP JP2000598639A patent/JP4841037B2/ja not_active Expired - Fee Related
- 2000-02-11 ES ES00911784T patent/ES2257287T3/es not_active Expired - Lifetime
- 2000-02-11 DK DK00911784T patent/DK1151102T3/da active
- 2000-02-11 DE DE60027409T patent/DE60027409T2/de not_active Expired - Lifetime
- 2000-02-11 PT PT00911784T patent/PT1151102E/pt unknown
- 2000-02-11 WO PCT/US2000/003652 patent/WO2000047741A1/en not_active Ceased
- 2000-02-11 EP EP00911784A patent/EP1151102B1/en not_active Expired - Lifetime
- 2000-02-11 AU AU33623/00A patent/AU781460B2/en not_active Ceased
-
2006
- 2006-07-07 CY CY20061100939T patent/CY1107470T1/el unknown
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