Lippke J A, Gu Y, Sarnecki C, Caron P R, Su M S
Vertex Pharmaceuticals Incorporated, Cambridge, Massachusetts 02139, USA.
J Biol Chem. 1996 Jan 26;271(4):1825-8. doi: 10.1074/jbc.271.4.1825.
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.
我们已经鉴定并表征了一种名为CMH-1的新型半胱氨酸蛋白酶，它是白细胞介素1β转化酶（ICE）蛋白酶家族的新成员，对Asp-X具有底物特异性。CMH-1与CPP32（氨基酸同一性为52%）和MCH2（同一性为31%）具有最高的相似性。CMH-1共享形成ICE核心结构的保守氨基酸残基，以及参与催化和P1天冬氨酸结合的那些残基。CMH-1在COS细胞中的过表达导致CMH-1的加工和转染细胞的凋亡诱导。CMH-1与聚（ADP-核糖）聚合酶（PARP）的共表达也导致PARP的特异性切割。纯化的重组CMH-1在体外切割PARP，但不切割白细胞介素1β前体。
