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Caspase 3, also known as appoint,SCA-1, Yama and CPP32,IS AN ASPARTATESPECIFIC CYSTEINE protease that belongs to the ICE subfamily of caspases.
Caspase-3 is expressed in cells as an inactive precursor from which the p17 and p11 subunits of the mature caspase-3 are proteolytically generated during apoptosis.The caspase-3 precursor is first cleaved at Asp 175-Ser 176 to produce the p11 subunit and the p20 peptide.Subsequently,the p20 peptide is cleaved at Asp 28-Ser 29 to generate the mature p17 subunit. The active caspasw-3 enzyme is a heterodimer composed of two p17 and two p11 subunits. At the onset of apoptosis, caspase-3 proteoluytically cleaves PARP at a Asp 216-Gly 217 bond.During the execution of the apoptotic cascade, activated caspase-3 releases SREBP from the membrane of the ER in a proteolytic reaction that is distinct from their normalsterol-dependent activation. Caspase-3 cleaves and activates SREBPs between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Caspase-3 also cleaves and activates caspase-6,-7 and -9. The human caspase-3 gene encodes a cytoplasmic protein that is highly expressed in lung,spleen,heart,liver,kidney and kells of the immune system.