The CED-3/ICE-like Protease Mch2 Is Activated during Apoptosis and Cleaves the Death Substrate Lamin A

作者：Kim Orth, Arul M. Chinnaiyan, Manish Garg, Christopher J. Froelich, Vishva M. Dixit · 发表于：Journal of Biological Chemistry · 年份：1996 · DOI：10.1074/jbc.271.28.16443 · 被引用次数：461 · 研究领域：Cell death mechanisms and regulation、Phagocytosis and Immune Regulation、Nuclear Structure and Function

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-xL, 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.