The caspase-3 precursor (31kDa) is first cleaved at Asp175-Ser176 to produce the p12 subunit and the p19 protein. Subsequently, the p19 protein is cleaved at Asp28-Ser29 to generate the mature p17 subunit. The active caspase-3 enzyme is a heterodimer composed of two p17 and two p12 subunits.
At the onset of apoptosis, caspase-3 proteolytically cleaves PARP at an Asp216-Gly217 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 normal steroldependent activation. Caspase-3 cleaves and activates SREBPs between the basic helixloop-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 cells of the immune system.
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