|
||
Report |
Correspondence to: Junying Yuan, Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115. Tel:(617) 432-4170 Fax:(617) 432-4177 E-mail: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 ß 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
This article has been cited by other articles:
|
|