Early caspase‐3 activation independent of apoptosis is required for cellular function

Publisher Website
Google Scholar
Abstract
A number of pro‐apoptotic stimuli induce the activation of caspase‐9, an initiator protease that activates executioner caspases, such as caspase‐3, leading to the development of programmed cell death. Here we demonstrate that cell (platelets and pancreatic acinar cells) stimulation with agonists induces a bimodal activation of caspase‐3. The early caspase‐3 activation occurs within 1 min of stimulation and is independent on caspase‐9 or mitochondrial cytochrome c release suggesting that is a non‐apoptotic event. The ability of agonists to induce early activation of caspase‐3 is similar to that observed for other physiological processes. Activation of caspase‐3 by physiological concentrations of cellular agonists, including thrombin or CCK‐8, is independent of rises in cytosolic calcium concentration but requires PKC activation, and is necessary for agonist‐induced activation of the tyrosine kinases Btk and pp60src and for several cellular functions, including store‐operated calcium entry, platelet aggregation, or pancreatic secretion. Thus, early activation of caspase‐3 seems to be a non‐apoptotic event required for cellular function. J. Cell. Physiol. 209: 142–152, 2006.

This publication has 50 references indexed in Scilit: