Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32.
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.
Lippke
J A
JA
Vertex Pharmaceuticals Incorporated, Cambridge, Massachusetts 02139, USA.
Gu
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Y
Sarnecki
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Caron
P R
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Su
M S
MS
D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis; D001483:Base Sequence; D053179:Caspase 7; D020169:Caspases; D002460:Cell Line; D002522:Chlorocebus aethiops; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000235:genetics*; D017931:DNA Primers / Q000737:chemistry; D015870:Gene Expression; D006801:Humans; D007375:Interleukin-1 / Q000378:metabolism; D008969:Molecular Sequence Data; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D007375:Interleukin-1; D012333:RNA, Messenger; D011065:Poly(ADP-ribose) Polymerases; C505520:CASP7 protein, human; D053179:Caspase 7; D020169:Caspases; D003546:Cysteine Endopeptidases