CASP3 is part of the cysteine-aspartic acid protease（caspase) family. Sequential activation of caspase-3 enzyme results in the execution-phase of cell apoptosis/programmed cell death. Caspase 3 has been called the "henchman that goes around and executes the cell." Caspase3 exists as an inactive proenzyme which undergoes proteolytic processing at conserved aspartic residues to produce 2 subunits， large and small， that dimerize to form the active enzyme. CASP3 cleaves and activates caspases 6， 7 and 9， and be processed by caspases 8， 9 and 10. Caspase-3 is involved in the cleavage of amyloid-beta 4A precursor protein， which is associated with neuronal death in Alzheimer’s & Huntington disease.
High levels of Caspase-3 are found in lymphocytes， indicating that it is an important mediator of apoptosis in the immune system.
CSN-mediated deneddylation is regulated by active CASP3.
CASP-3 cleavage of RAD51 results in a functional decrease in RAD51 strand exchange activity and inhibition of caspase 3 activity increases RAD51 protein levels.
Mice overexpressing human caspase 3 have increased susceptibility to degenerative insults. Single nucleotide polymorphisms in Caspase-3 gene is associated with lung cancer.
Caspase3 is activated by elaidic acid and palmitic acid.
CASP3 activity is enhanced by safrole oxidase in lung cancer cells.
Expression of CASP3 in peripheral blood mononuclear cells is significantly increased in SLE patients.
