Caspases are a family of cytosolic aspartate specific cysteine proteases involved in apoptosis and inflammation. Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a key protease that is activated during the early stages of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins during apoptosis, such as ply (APD-ribose) polymerase (PARP). The processed form of Caspase 3 consists of large (17kDa) and small (12kDa) subunits which is derived from the 32 kDa proenzyme and associate to form an active enzyme. Caspase 3 is cleaved at Asp28 Ser29 and Asp175 Ser176. The active Caspase 3 proteolytically cleaves and activates other caspases (e.g. Caspases 6, 7 and 9).
References:
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Caraballo JM et al. High p27 protein levels in chronic lymphocytic leukemia are associated to low Myc and Skp2 expression, confer resistance to apoptosis and antagonize Myc effects on cell cycle. Oncotarget. 2014 Jul; 5(13): 4694–4708.
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CASP3, CPP32
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836
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17 kDa.
