Identification and Characterization of CPP32/Mch2 Homolog 1, a Novel Cysteine Protease Similar to CPP32

• DOI: 10.1074/jbc.271.4.1825
• Publication Date: 2002-07-26T14:57:46Z
• Authors: Judith A. Lippke; Yong Gu; Charlyn Sarnecki; Paul R. Caron; Michael S.-S. Su
• Keywords: Caspase 7; 0303 health sciences; Base Sequence; Sequence Homology, Amino Acid; Molecular Sequence Data; Gene Expression; Apoptosis; Cell Line; Cysteine Endopeptidases; 03 medical and health sciences; Caspases; Chlorocebus aethiops; Animals; Humans; Amino Acid Sequence; RNA, Messenger; Cloning, Molecular; Poly(ADP-ribose) Polymerases; Sequence Alignment; DNA Primers; Interleukin-1

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.