Caspase-3 Precursor Protease Inhibitors

The apoptotic cysteine protease, caspase-3, is expressed in cells as an inactive 32 kD precursor from which 17 kD (p17) and 12 kD (p12) subunits of the mature caspase-3 were proteolytically generated during apoptosis. Using a cell-free caspase-3 processing assay it has been demonstrated, that the caspase-3 precursor appears to be cleaved first between Asp175 and Ser176, producing the p12 and p20 subunits. Subsequently, the p20 was cleaved between Asp28 and Ser29, generating the mature p17 subunit.

Family Literatur:
Z.Han et al., J. Biol. Chem., 272, 13432 (1997)