Calcium signalling and the regulation of apoptosis
Abstract
Apoptotic cell death is characterized by cell shrinkage, chromatin condensation and fragmentation, formation of apoptotic bodies and phagocytosis (Kerr et al., 1972). At the molecular level, activation of a family of cysteine proteases, caspases, related to interleukin-1beta-converting enzyme is believed to be a crucial event in apoptosis. This is associated with the proteolysis of nuclear and cytoskeletal proteins, cell shrinkage, glutathione efflux, exposure of phosphatidylserine on the cell surface, membrane blebbing, etc. In CD95- or TNF-mediated apoptosis, the proteolytic cascade is believed to be triggered directly by caspase binding to the activated plasma membrane receptor complex. In other forms of apoptosis, the mechanisms of activation of the proteolytic cascade are less well established but may involve imported proteases, such as granzyme B, or factors released from the mitochondria and, possibly, other organelles. Recently, the possibility that cytochrome c released from the mitochondria may serve to activate dormant caspases in the cytosol, and thereby to propagate the apoptotic process, has attracted considerable attention. A perturbation of intracellular Ca(2+) homeostasis has been found to trigger apoptosis in ...Continue Reading
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