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Caspase‐3 can be pseudo‐activated by a Ca 2+ ‐dependent proteolysis at a non‐canonical site
Author(s) -
Pelletier Maude,
Oliver Lisa,
Meflah Khaled,
Vallette François M.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.02.079
Subject(s) - proteolysis , calcium , chemistry , calpain , cleavage (geology) , caspase , cytochrome c , apoptosis , microbiology and biotechnology , cytosol , fragmentation (computing) , caspase 3 , biophysics , non canonical , programmed cell death , biochemistry , biology , enzyme , paleontology , ecology , organic chemistry , fracture (geology)
We have shown previously that calcium could trigger nuclear fragmentation, which was associated with a caspase 3 (C3)‐like activity [Juin, P., Pelletier, M., Oliver, L., Tremblais, K., Gregoire, M., Meflah, K. and Vallette, F.M. (1998) Induction of a caspase‐3‐like activity by calcium in normal cytosolic extracts triggers nuclear apoptosis in a cell‐free system. J. Biol. Chem. 273, 17559]. Here, we report that this activation is associated with a non‐canonical truncation of C3, which induces a weak DEVDase activity. The cleavage of C3 via calcium‐dependent proteolysis is independent of caspase 9; lysate exposure to calcium prevents further cleavage and activation by the cytochrome c and dATP pathway. Altogether, our data suggest that calcium could favour a necrotic mechanism by inducing the generation of a form of C3 insensitive to mitochondrial activation.