Cysteinyl aspartic acid-protease 8, Cysteinyl aspartic acid-protease 9, Apoptosis regulator BAX (Caspase-8 (CASP8, FLICE), Caspase-9 (CASP9), BAX)

Caspase-8, Caspase-9, and Bcl2-associated X protein (BAX) are key molecules in the regulation and execution of apoptosis. Caspase-8 primarily initiates the extrinsic pathway of apoptosis downstream of death receptors, while Caspase-9 is activated in the intrinsic (mitochondrial-mediated) pathway following cytochrome c release and ApoF-1 binding[4][5]. Both activate downstream effector caspases such as caspase-3. Bcl2-associated X protein (BAX) is a pro-apoptotic member of the Bcl-2 family, responsible for promoting mitochondrial outer membrane permeabilization (MOMP), cytochrome c release, and facilitating intrinsic apoptosis; its activity is opposed by anti-apoptotic Bcl-2 family proteins[1][2][7]. Modulation of these proteins is a major area in cancer therapy, aiming to restore cell death in resistant tumors or prevent inappropriate cell loss in neurodegeneration and immune disorders.

Other names

FLICEFADD-like IceMach-1Mch5ICE-LAP6APAF-3BAXbcl-2-like protein 4apoptosis regulator BAX

Inhibition of anti-apoptotic Bcl-2 family proteins to promote apoptosis (Venetoclax, Navitoclax) Direct inhibition of caspase enzyme activity (Emricasan, Z-VAD-FMK) Activation or restoration of pro-apoptotic signaling (encouraging BAX translocation, caspase activation cascade)