Cysteine-aspartic acid protease 3 and Cysteine-aspartic acid protease 7 (Caspase-3 and Caspase-7) (CASP3/7)

Caspase-3 and Caspase-7 are cysteine-aspartic acid proteases that function as the primary executioner caspases in the apoptotic signaling pathway (UniProt P42574, P55210). They are synthesized as inactive zymogens (procaspases) and are activated through proteolytic cleavage by initiator caspases, such as Caspase-8 or Caspase-9, in response to extrinsic or intrinsic death signals (StatPearls, Caspase Cascade). Once activated, these enzymes coordinate the systematic demolition of the cell by cleaving a wide array of cellular substrates, including poly(ADP-ribose) polymerase (PARP) and inhibitor of caspase-activated DNase (ICAD), leading to DNA fragmentation and chromatin condensation (PubMed: 10648661). In oncology, therapeutic strategies often aim to reactivate these caspases to induce death in resistant tumor cells, using compounds like PAC-1 (PubMed: 24991950). Conversely, in neurodegenerative and cardiovascular diseases, inhibitors such as Emricasan are explored to prevent excessive cell loss and tissue damage (PubMed: 28841100). Because of their central role in cell death, targeting Caspase-3/7 requires precise control to avoid systemic toxicity or the survival of damaged cells that could lead to secondary malignancies.

Other names

Cysteine-aspartic acid protease 3Cysteine-aspartic acid protease 7Executioner caspasesCPP32MCH3ApopainSCA-1SREBP cleavage-activating protease

Proteolytic cleavage of downstream cellular substrates to execute programmed cell death.