Caspase 3, Caspase 8, Caspase 9 (CASP3, CASP8, CASP9)

Caspase 3, Caspase 8, and Caspase 9 are essential cysteine-aspartic proteases that serve as central regulators of the apoptotic cell death program [1, 5]. Caspase 8 and Caspase 9 function as initiator caspases, triggered by the extrinsic (death receptor) and intrinsic (mitochondrial) pathways, respectively [1, 4]. These initiators then proteolytically activate Caspase 3, the primary executioner caspase responsible for the systematic dismantling of the cell by cleaving key structural and regulatory proteins [4, 6]. Beyond their roles in apoptosis, these enzymes are involved in non-apoptotic processes such as inflammation, cell differentiation, and tissue regeneration [7, 12]. Dysregulation of these caspases is implicated in a wide range of pathologies; for instance, their evasion is a hallmark of cancer, while their overactivation contributes to neuronal loss in neurodegenerative diseases and acute injuries like stroke or traumatic brain injury [3, 10, 13]. Therapeutic strategies target these molecules either to induce apoptosis in malignant cells or to inhibit pathological cell death in degenerative conditions [1, 2, 4].

Other names

Cysteine-aspartic acid protease 3/8/9CASP3/8/9Apoptotic caspasesCPP32 (Caspase 3)SCA-1 (Caspase 3)Apopain (Caspase 3)Yama (Caspase 3)FLICE (Caspase 8)MACH (Caspase 8)MCH5 (Caspase 8)ICE-LAP6 (Caspase 9)MCH6 (Caspase 9)

Caspase inhibition to prevent pathological cell death or Caspase activation to induce apoptosis in cancer cells