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- W1985339713 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." @default.
- W1985339713 created "2016-06-24" @default.
- W1985339713 creator A5008180238 @default.
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- W1985339713 date "2000-08-21" @default.
- W1985339713 modified "2023-10-09" @default.
- W1985339713 title "Cross-Talk between Two Cysteine Protease Families" @default.
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- W1985339713 doi "https://doi.org/10.1083/jcb.150.4.887" @default.
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