TY - JOUR
T1 - The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
AU - Orth, Kim
AU - Chinnaiyan, Arul M.
AU - Garg, Manish
AU - Froelich, Christopher J.
AU - Dixit, Vishva M.
PY - 1996
Y1 - 1996
N2 - Phylogenetic analysis of the CED-3/ICE family of cysteine proteases suggests the existence of a subfamily most related to the Caenorhabditis elegans death gene ced-3 and includes Yama (CPP32, apopain), LAP3 (Mch3, CMH1), and Mch2. Here, we show that Mch2 is processed from its zymogen form to a proteolytically active dimeric species during execution of the apoptotic program and by the cytotoxic T cell death protease granzyme B. Additionally, like Yama and LAP3, Mch2 functions downstream of the death inhibitors Bcl-2, Bcl-X(L), and CrmA. Importantly, Mch2, but not Yama or LAP3, is capable of cleaving lamin A to its signature apoptotic fragment, indicating that Mch2 is an apoptotic laminase.
AB - Phylogenetic analysis of the CED-3/ICE family of cysteine proteases suggests the existence of a subfamily most related to the Caenorhabditis elegans death gene ced-3 and includes Yama (CPP32, apopain), LAP3 (Mch3, CMH1), and Mch2. Here, we show that Mch2 is processed from its zymogen form to a proteolytically active dimeric species during execution of the apoptotic program and by the cytotoxic T cell death protease granzyme B. Additionally, like Yama and LAP3, Mch2 functions downstream of the death inhibitors Bcl-2, Bcl-X(L), and CrmA. Importantly, Mch2, but not Yama or LAP3, is capable of cleaving lamin A to its signature apoptotic fragment, indicating that Mch2 is an apoptotic laminase.
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U2 - 10.1074/jbc.271.28.16443
DO - 10.1074/jbc.271.28.16443
M3 - Article
C2 - 8663580
AN - SCOPUS:0029891838
SN - 0021-9258
VL - 271
SP - 16443
EP - 16446
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 28
ER -