Caspase-3 along with caspase 7 and 6 form the group of effector caspases that are responsible for the cleavage of multiple substrates including the cytokeratins, PARP, alpha fodrin, NuMA and others. Caspase-7 occurs in three varient forms. Caspase-3-like activities are required for Fas-mediated apoptosis. However, the role of caspase-1 and caspase-3 in mediating Fas-induced cell death is not clear. Although wild-type, caspase-1(-/-), and caspase-3(-/-) hepatocytes were killed at a similar rate when cocultured with FasL expressing NIH 3T3 cells, caspase-3(-/-) hepatocytes displayed drastically different morphological changes as well as significantly delayed DNA fragmentation. For both wild-type and caspase-1 (-/-) apoptotic hepatocytes, typical apoptotic features such as cytoplasmic blebbing and nuclear fragmentation are seen within 6 hr, but neither event was observed for caspase-3(-/-) hepatocytes. In thymocytes apoptotic caspase-3 (-/-) thymocytes exhibit similar abnormal morphological changes and delayed DNA fragmentation observed in hepatocytes. Cleavage of various caspase substrates implicates apoptotic events, including gelsolin, fodrin, laminB, and DFF45/ICAD are delayed or absent. The altered cleavage of these key substrates is likely responsible for the aberrant apoptosis observed in both hepatocytes and thymocytes deficient in caspase-3.
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