CASP3 encodes caspase-3, a thiol protease functioning as a major effector caspase in the execution phase of apoptosis 123. Following activation by initiator caspases (CASP8, CASP9, CASP10), caspase-3 catalyzes proteolytic cleavage of numerous substrates including poly(ADP-ribose) polymerase (PARP1), caspases-6, -7, and -9, and interleukin-18 45. Beyond canonical apoptosis, CASP3 cleaves huntingtin, desmogleins, and AKT1 in response to oxidative stress, regulates cell adhesion through RET cleavage, and mediates phosphatidylserine exposure on apoptotic cells 678. Additionally, CASP3 participates in pyroptosis via gasdermin-E activation and negatively regulates type I interferon production during viral infection by cleaving antiviral proteins CGAS, IRF3, and MAVS 910. CASP3 dysfunction is implicated in cancer development; somatic mutations occur in multiple tumor types with altered expression correlating to disease progression 11. CASP3 polymorphisms associate with Kawasaki disease susceptibility 12, and elevated CASP3 correlates with increased apoptosis in diabetic kidney disease 13. The dual role of CASP3—promoting apoptosis while suppressing inflammatory responses—makes it a critical therapeutic target across multiple pathologies.