Cross-Talk between Two Cysteine Protease Families

Journal of Cell Biology - Tập 150 Số 4 - Trang 887-894 - 2000
Toshiyuki Nakagawa1, Junying Yuan2
1Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
2aDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115

Tóm tắt

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 β 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.

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