Caspase-3, apoptosis-related cysteine peptidase (Caspase-3)

Caspase‐3 is a key executioner enzyme within the cysteine-aspartic acid proteases (“caspases”) family that orchestrates programmed cell death (“apoptosis”). It exists as an inactive proenzyme (“procaspase‐3”) which becomes activated through proteolytic cleavage by initiator caspases such as caspases‐8, ‑9, or ‑10. Once active, it catalyzes the selective cleavage of numerous cellular substrates—including poly(ADP-ribose) polymerase (PARP), sterol regulatory element binding proteins (SREBPs), amyloid precursor protein—and activates downstream effector caspases like caspases 6 and 7. This central role makes it essential not only for normal development but also highly relevant in pathologies where apoptosis is dysregulated such as cancer resistance mechanisms or neurodegeneration due to inappropriate neuronal loss. Its activity can be measured using specific antibodies against its cleaved form—a gold-standard marker for cells undergoing apoptosis.

Other names

CASP3CPP32CPP32BSCA-1ApopainYamaCysteine protease CPP32

Drugs targeting Caspase‑3 typically act by one of the following mechanisms: - Direct inhibition of enzymatic activity via covalent or non-covalent binding to the active site cysteine residue. - Activation by promoting zymogen processing or mimicking upstream apoptotic signals. - Indirect modulation through upstream pathway regulation affecting initiator caspases.