Identification and characterization of CPP32/2Mch2 homolog 1, a novel cysteine protease similar to CPP32

被引：158

作者：

Lippke, JA ^{[1
]}

Gu, Y ^{[1
]}

Sarnecki, C ^{[1
]}

Caron, PR ^{[1
]}

Su, MSS ^{[1
]}

机构：

[1] VERTEX PHARMACEUT INC,CAMBRIDGE,MA 02139

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1996年 / 271卷 / 04期

关键词：

D O I：

10.1074/jbc.271.4.1825

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have identified and characterized a novel cysteine protease named CMH-1 that is a new member of the interleukin 1 beta converting enzyme (ICE) family of proteases with substrate specificity for Asp-X. CMH-1 has the highest similarity to CPP32 (52% amino acid identity) and MCH2 (31% identical). CMH-1 shares conserved amino acid residues that form the core structure of ICE as well as those residues involved in catalysis and in the P1 aspartate binding. Overexpression of CMH-1 in COS cells resulted in the processing of CMH-1 and the induction of apoptosis of transfected cells. Coexpression of CMH-1 with poly(ADP-ribose) polymerase (PARP) also resulted in a specific cleavage of PARP. Purified recombinant CMH-1 cleaved PARP but not interleukin 1 beta precursor in vitro.

引用

页码：1825 / 1828

页数：4

共 34 条

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