A unique family of Cysteine proteases has been described that differs in sequence, structure and substrate specificity from any previously described protease family. This family, Ced-3/caspase-1, is comprised of caspase-1, caspase-2, caspase-3, caspase-4, caspase-6, caspase-7 (also designated Mch3, ICE-LAP3 or CMH-1), caspase-9 and caspase-10. Ced-3/caspase-1 family members function as key components of the apoptotic machinery and act to destroy specific target proteins which are critical to cellular longevity. Poly (ADP-ribose) polymerase plays an integral role in surveying for DNA mutations and double strand breaks. Caspase-3, caspase-7 and caspase-9, but not caspase-1, have been shown to cleave the nuclear protein PARP into an apoptotic fragment. Caspase-6, but not caspase-3, has been shown to cleave the nuclear lamins which are critical to maintaining the integrity of the nuclear envelope and cellular morphology. Caspase-10 has been shown to activate caspase-3 and caspase-7 in response to apoptotic stimuli.