Members of the ICE/CED-3 cysteine protease family have key roles in inflammation and mammalian apoptosis
The ICE family member Caspase-3 (also known as CPP32, Yama, apopain) is activated early in apoptosis and appears to be involved in the proteolysis of several important molecules, including poly (ADP ribose) polymerase (PARP)
Activated Caspase-3 cleaves PARP from its 116 kDa to an 85 kDa residual fragment
The cleavage site in PARP is C-terminal to Asp-216
The upstream sequence of the cleavage site, DEVD (Asp-Glu-Val-Asp), is utilized as a basis for the highly specific Caspase-3 substrate, Ac (N-acetyl)-DEVD-AMC (7-amino-4-methylcoumarin)