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J Cell Biol. 2000 Aug 21;150(4):887-94.

Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis.

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  • 1Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

Abstract

Calpains and caspases are two cysteine protease families that play important roles in regulating pathological cell death. Here, we report that m-calpain may be responsible for cleaving procaspase-12, a caspase localized in the ER, to generate active caspase-12. In addition, calpain may be responsible for cleaving the loop region in Bcl-xL and, therefore, turning an antiapoptotic molecule into a proapoptotic molecule. We propose that disturbance to intracellular calcium storage as a result of ischemic injury or amyloid beta peptide cytotoxicity may induce apoptosis through calpain- mediated caspase-12 activation and Bcl-xL inactivation. These data suggest a novel apoptotic pathway involving calcium-mediated calpain activation and cross-talks between calpain and caspase families.

PMID:
10953012
[PubMed - indexed for MEDLINE]
PMCID:
PMC2175271
Free PMC Article

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