Caspase-3 and Caspase-7 (CASP3, CASP7)

Caspase-3 and Caspase-7 are cysteine proteases central to the execution phase of apoptosis. Synthesized as inactive zymogens, they are activated by upstream initiator caspases (such as caspase-8 and caspase-9), which cleave them to reveal active sites. Once active, these enzymes cleave numerous cellular substrates at specific aspartic acid residues, leading to the orderly dismantling of cell components, DNA fragmentation, and formation of apoptotic bodies. Both play overlapping but non-identical roles in apoptosis and possess similar substrate specificity (Asp-Glu-Val-Asp; DEVD). Dysregulation of caspase-3/7 activity is linked to various diseases, including cancer, neurodegeneration, heart disease, and inflammatory responses[2][3][4][6][7]. Caspase-3/7 activity is exploited for drug screening, apoptosis imaging, and as a clinical biomarker for cell death[4][5]. Therapeutic targeting is challenging due to their central role in normal physiology, and inhibition or overactivation may disrupt tissue homeostasis or immune functions[2][3].

Other names

CASP3CASP7Apoptotic cysteine proteaseEffector caspasesExecutioner caspases

Inhibitors block caspase-3/7 catalytic site, preventing substrate cleavage and thus apoptosis. Activators increase caspase activity, promoting apoptotic cell death. Imaging substrates (DEVD, KGDEVD) are cleaved by active caspase-3/7, allowing detection of apoptosis.