| Background |
PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, is a highly conserved nuclear enzyme implicated in DNA repair and in the apoptosis response of cells. This protein can be cleaved by many caspases in vitro and is one of the main cleavage targets of caspase-3 in vivo. The cleavage occurs between ASP214 and Gly 215, which separates PARP’s N-terminal DNA binding domain (24 kDa) from its C-terminal catalytic domain (89 kDa). It has been shown that cleavage of PARP facilitates cellular disassembly and inhibition of PARP cleavage attenuates apoptosis in vitro.
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