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© The Rockefeller University Press,
0021-9525/2000//887 $5.00
The Journal of Cell Biology, Volume 150, Number 4,
, 2000 887-894
Report |
Cross-Talk between Two Cysteine Protease Families
: Activation of Caspase-12 by Calpain in Apoptosis
Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115.(617) 432-4177(617) 432-4170
jyuan{at}hms.harvard.edu
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.
Key Words: calcium • Alzheimer's disease • Bcl-xL • endoplasmic reticulum • ER stress
© 2000 The Rockefeller University Press
Abbreviations used in this paper: Aβ, amyloid β; IP3R, inositol 1,4,5-trisphosphate receptor; OD, oxygen deprivation; OGD, oxygen and glucose deprivation; t-caspase-12, T159-N419 caspase-12.
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