KR987000085A - 헤지호그-유래의 신규한 폴리펩티드(Novel Hedgehog-Derived Polypeptides) - Google Patents
헤지호그-유래의 신규한 폴리펩티드(Novel Hedgehog-Derived Polypeptides) Download PDFInfo
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- KR987000085A KR987000085A KR1019970703752A KR19970703752A KR987000085A KR 987000085 A KR987000085 A KR 987000085A KR 1019970703752 A KR1019970703752 A KR 1019970703752A KR 19970703752 A KR19970703752 A KR 19970703752A KR 987000085 A KR987000085 A KR 987000085A
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- polypeptide
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- amino acid
- hedgehog
- acid sequence
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- 229920001184 polypeptide Polymers 0.000 title claims abstract 31
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract 31
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract 31
- 238000000034 method Methods 0.000 claims abstract 15
- 239000012634 fragment Substances 0.000 claims abstract 6
- 102000040430 polynucleotide Human genes 0.000 claims 9
- 108091033319 polynucleotide Proteins 0.000 claims 9
- 239000002157 polynucleotide Substances 0.000 claims 9
- 125000003275 alpha amino acid group Chemical group 0.000 claims 8
- 210000002569 neuron Anatomy 0.000 claims 7
- 241000289669 Erinaceus europaeus Species 0.000 claims 5
- 230000002797 proteolythic effect Effects 0.000 claims 5
- 210000004027 cell Anatomy 0.000 claims 4
- 238000003776 cleavage reaction Methods 0.000 claims 4
- 239000013604 expression vector Substances 0.000 claims 4
- 230000007017 scission Effects 0.000 claims 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims 3
- 108020001507 fusion proteins Proteins 0.000 claims 3
- 102000037865 fusion proteins Human genes 0.000 claims 3
- 102000003693 Hedgehog Proteins Human genes 0.000 claims 2
- 108090000031 Hedgehog Proteins Proteins 0.000 claims 2
- 102000004887 Transforming Growth Factor beta Human genes 0.000 claims 2
- 108090001012 Transforming Growth Factor beta Proteins 0.000 claims 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 claims 2
- 230000004069 differentiation Effects 0.000 claims 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims 2
- 230000035755 proliferation Effects 0.000 claims 2
- 238000003259 recombinant expression Methods 0.000 claims 2
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 claims 2
- 102000005606 Activins Human genes 0.000 claims 1
- 108010059616 Activins Proteins 0.000 claims 1
- 102000016970 Follistatin Human genes 0.000 claims 1
- 108010014612 Follistatin Proteins 0.000 claims 1
- 239000000488 activin Substances 0.000 claims 1
- 230000033228 biological regulation Effects 0.000 claims 1
- 210000004899 c-terminal region Anatomy 0.000 claims 1
- 239000003795 chemical substances by application Substances 0.000 claims 1
- 239000000411 inducer Substances 0.000 claims 1
- 230000006698 induction Effects 0.000 claims 1
- 210000002161 motor neuron Anatomy 0.000 claims 1
- 210000005036 nerve Anatomy 0.000 claims 1
- 241000289659 Erinaceidae Species 0.000 abstract 1
- 230000000468 autoproteolytic effect Effects 0.000 abstract 1
- 210000004900 c-terminal fragment Anatomy 0.000 abstract 1
- 230000015556 catabolic process Effects 0.000 abstract 1
- 238000006731 degradation reaction Methods 0.000 abstract 1
- 210000004898 n-terminal fragment Anatomy 0.000 abstract 1
- 102000004169 proteins and genes Human genes 0.000 abstract 1
- 108090000623 proteins and genes Proteins 0.000 abstract 1
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Abstract
본 발명은 각각 헤지호그의 N 및 C 단편 또는 N-말단 및 C-말단 단편이라 칭하는 신규한 두 개의 폴리펩티드를 제공하는 것에 관한 것이다. 상기 두 개의 신규한 폴리펩티드는 천연 단백질내의 자가 단백질 분해 영역에 의해 인식되는 G↓CF 위치에서의 특이성 분해후에 유도된다. 또한, 본 발명은 상기 N 및 C 단편의 사용방법을 제공한다.
Description
본 내용은 요부공개 건이므로 전문내용을 수록하지 않았음
Claims (31)
- 헤지호그 단백질의 아미노 말단 아미노산으로부터 유래한 아미노산 서열을 보유하고, 카르복시 말단에 천연 헤지호그 폴리펩티드의 카르복시 말단 단편의 단백질 분해 활성에 의해 특이적으로 인식되는 G↓CF 절단 위치를 보유하는 것을 특징으로 하는 거의 순수한 폴리펩티드.
- 제 1 항의 아미노산 서열을 보유하는 폴리펩티드를 암호화하는 분리된 폴리뉴클레오티드 서열.
- 제 2 항에 있어서, 제 1 항의 폴리펩티드의 아미노산 서열을 보유하는 폴리펩티드를 암호화하고, 제 1 항의 폴리펩디드와 면역반응하는 항체에 대한 하나 이상의 에피토프를 보유하는 분리된 폴리뉴클레오티드 서열.
- 제 2 항의 폴리뉴클레오티드를 함유하는 재조합 발현 벡터.
- 제 4 항의 발현 백터를 함유하는 숙주 세포.
- 제 1 항의 폴리펩티드에 결합하고, 제 1 항의 폴리펩티드의 면역반응성 단편에 결합하는 항체.
- 제 6 항에 있어서, 상기 항체가 다중클론 항체인 항체.
- 제 6 항에 있어서, 상기 항체가 단일클론 항체인 항체.
- 헤지호그 단백질의 카르복시 말단 아미노산으로부터 유래한 아미노산 서열을 보유하고, 아미노 말단에 천연 헤지호그 폴리펩티드의 카르복시 말단 단편의 단백질 분해 활성에 의해 특이적으로 인식되는 G↓CF 절단 위치를 보유하는 것을 특징으로 하는 거의 순수한 폴리펩티드.
- 제 9 항의 아미노산 서열을 보유하는 폴리펩티드를 암호화하는 분리된 폴리뉴클레오티드 서열.
- 제 10 항에 있어서, 제 9 항의 폴리펩티드의 아미노산 서열을 보유하는 폴리펩티드를 암호화하고, 제 9 항의 폴리펩디드와 면역반응하는 항체에 대한 하나 이상의 에피토프를 보유하는 분리된 폴리뉴클레오티드 서열.
- 제 10 항의 폴리뉴클레오티드를 함유하는 재조합 발현 벡터.
- 제 12 항의 발현 백터를 함유하는 숙주 세포.
- 제 9 항의 폴리펩티드에 결합하고, 제 9 항의 폴리펩티드의 면역반응성 단편에 결합하는 항체.
- 제 14 항에 있어서, 상기 항체가 다중클론 항체인 항체.
- 제 14 항에 있어서, 상기 항체가 단일클론 항체인 항체.
- 신경 세포와 헤지호그 폴리펩티드를 접촉시키는 단계를 포함하는, 신경 세포의 증식 또는 분화를 조절하는 방법.
- 제 17 항에 있어서, 상기 헤지호그 폴리펩티드가 제 1 항의 폴리펩티드인 방법.
- 제 17 항에 있어서, 상기 헤지호그 폴리펩티드가 제 9 항의 폴리펩티드인 방법.
- 제 17 항에 있어서, 상기 조절이 증식 또는 분화의 유도인 방법.
- 제 17 항에 있어서, 상기 신경 세포가 거의 바닥판 신경 세포로부터 유래하는 방법.
- 제 21 항에 있어서, 상기 신경 세포가 운동 신경인 방법.
- 제 17 항에 있어서, 상기 신경 세포가 척추동물 신경세포인 방법.
- 제 23 항에 있어서, 상기 척추동물이 인간인 방법.
- 제 17 항에 있어서, 상기 세포와 TGF-β류를 접촉시키는 단계를 추가로 포함하는 방법.
- 제 25 항에 있어서, 상기 TGF-β가 액티빈인 방법.
- 제 17 항에 있어서, 상기 세포와 신경 유도제를 접촉시키는 단계를 추가로 포함하는 방법.
- 제 27 항에 있어서, 상기 신경 유도제가 노긴, 폴리스타틴 및 뉴로트로핀으로 구성되는 군으로부터 선택되는 방법.
- 제 9 항의 폴리펩티드의 단백질 분해 영역을 포함하는 제 1 폴리펩티드, 상기 제 1 폴리펩티드에 의해 인식되는 절단 위치 및 제 2 폴리펩티드를 포함하는 자가 단백질 분해성 융합 단백질.
- 제 29 항의 융합 단백질을 암호화하는 폴리뉴클레오티드.
- 제 9 항의 폴리펩티드의 단백질 분해 영역 및 상기 단백질 분해 영역에 의해 인식되는 절단 위치를 포함하는 제 1 폴리펩티드를 암호화하는 제 1 폴리뉴클레오티드와 제 2 폴리펩티드를 암호화하는 제 2 폴리뉴클레오티드를 작동가능하게 연결시키는 단계를 포함하는, 자가 단백질 분해성 융합 단백질의 제조 방법.※ 참고사항 : 최초출원 내용에 의하여 공개하는 것임.
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US08/349498 | 1994-12-02 | ||
US8/349498 | 1994-12-02 | ||
US08/349,498 US6281332B1 (en) | 1994-12-02 | 1994-12-02 | Hedgehog-derived polypeptides |
PCT/US1995/015923 WO1996016668A1 (en) | 1994-12-02 | 1995-12-04 | Novel hedgehog-derived polypeptides |
Related Child Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
KR10-2004-7006632A Division KR20040064700A (ko) | 1994-12-02 | 1995-12-04 | 헤지호그-유래의 신규한 폴리펩티드 |
Publications (2)
Publication Number | Publication Date |
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KR987000085A true KR987000085A (ko) | 1998-03-30 |
KR100453096B1 KR100453096B1 (ko) | 2005-04-06 |
Family
ID=23372653
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
KR1019970703752A KR100453096B1 (ko) | 1994-12-02 | 1995-12-04 | 헤지호그-유래의신규한폴리펩티드 |
KR10-2004-7006632A KR20040064700A (ko) | 1994-12-02 | 1995-12-04 | 헤지호그-유래의 신규한 폴리펩티드 |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
KR10-2004-7006632A KR20040064700A (ko) | 1994-12-02 | 1995-12-04 | 헤지호그-유래의 신규한 폴리펩티드 |
Country Status (9)
Country | Link |
---|---|
US (2) | US6281332B1 (ko) |
EP (1) | EP0793502A4 (ko) |
JP (2) | JPH11500605A (ko) |
KR (2) | KR100453096B1 (ko) |
AU (2) | AU712346B2 (ko) |
CA (1) | CA2206509C (ko) |
FI (1) | FI121366B (ko) |
NO (1) | NO323079B1 (ko) |
WO (2) | WO1996017924A2 (ko) |
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-
1994
- 1994-12-02 US US08/349,498 patent/US6281332B1/en not_active Expired - Lifetime
-
1995
- 1995-12-04 KR KR1019970703752A patent/KR100453096B1/ko not_active IP Right Cessation
- 1995-12-04 CA CA2206509A patent/CA2206509C/en not_active Expired - Lifetime
- 1995-12-04 JP JP8519152A patent/JPH11500605A/ja active Pending
- 1995-12-04 AU AU44183/96A patent/AU712346B2/en not_active Expired
- 1995-12-04 WO PCT/US1995/015463 patent/WO1996017924A2/en active Application Filing
- 1995-12-04 WO PCT/US1995/015923 patent/WO1996016668A1/en not_active Application Discontinuation
- 1995-12-04 EP EP95943029A patent/EP0793502A4/en not_active Ceased
- 1995-12-04 AU AU43705/96A patent/AU4370596A/en not_active Abandoned
- 1995-12-04 US US08/567,357 patent/US6132728A/en not_active Expired - Lifetime
- 1995-12-04 KR KR10-2004-7006632A patent/KR20040064700A/ko not_active Application Discontinuation
-
1997
- 1997-05-30 FI FI972312A patent/FI121366B/fi not_active IP Right Cessation
- 1997-05-30 NO NO19972494A patent/NO323079B1/no not_active IP Right Cessation
-
2006
- 2006-01-04 JP JP2006000290A patent/JP2006151989A/ja active Pending
Also Published As
Publication number | Publication date |
---|---|
AU712346B2 (en) | 1999-11-04 |
NO323079B1 (no) | 2006-12-27 |
EP0793502A4 (en) | 1999-10-13 |
NO972494L (no) | 1997-07-30 |
FI121366B (fi) | 2010-10-29 |
JP2006151989A (ja) | 2006-06-15 |
NO972494D0 (no) | 1997-05-30 |
US6132728A (en) | 2000-10-17 |
CA2206509A1 (en) | 1996-06-06 |
JPH11500605A (ja) | 1999-01-19 |
KR20040064700A (ko) | 2004-07-19 |
US6281332B1 (en) | 2001-08-28 |
FI972312A0 (fi) | 1997-05-30 |
KR100453096B1 (ko) | 2005-04-06 |
WO1996016668A1 (en) | 1996-06-06 |
FI972312A (fi) | 1997-12-30 |
AU4418396A (en) | 1996-06-19 |
EP0793502A1 (en) | 1997-09-10 |
CA2206509C (en) | 2011-05-03 |
WO1996017924A2 (en) | 1996-06-13 |
AU4370596A (en) | 1996-06-26 |
WO1996017924A3 (en) | 1996-09-26 |
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