Caspase-3 and Caspase-8 (CASP3/8)

Caspase-3 and Caspase-8 are essential members of the caspase family of cysteine-aspartic proteases that regulate programmed cell death. Caspase-8 acts as an initiator caspase in the extrinsic apoptotic pathway, where it is recruited to death-inducing signaling complexes (DISC) upon ligand binding to death receptors like Fas or TRAIL [2, 8]. Once activated, Caspase-8 triggers the downstream executioner phase by cleaving and activating Caspase-3 [3, 6]. Caspase-3 then orchestrates the systematic dismantling of the cell by cleaving key structural and functional proteins, such as PARP1 and lamins [3, 15]. Beyond apoptosis, these enzymes play complex roles in regulating other forms of cell death, including necroptosis and pyroptosis, as well as inflammatory signaling [5, 13]. In therapeutic contexts, Caspase-3 and Caspase-8 are targeted for activation in oncology to overcome apoptosis resistance, while their inhibition is explored as a neuroprotective strategy in conditions like stroke and Alzheimer's disease [16, 22].

Other names

Caspase-3/8CASP3 and CASP8Apopain and FLICECPP32 and MACHYama and MCH5

Inhibition of proteolytic activity by binding to the active site cysteine residue, or activation of the caspase cascade through upstream signaling pathways such as death receptor ligation or mitochondrial outer membrane permeabilization.