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Background
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Chromogenic paranitroanilide-peptide substrate for caspase-3 (Km = 9.7 μM). Ac-DEVD-pNA is based on amino acids 213-216 in poly (ADP-ribose) polymerase (PARP), an endogenous substrate for caspase-3. This substrate is also cleaved by caspases-6, -7, -8, and -10. Release of free pNA is monitored by absorbance at 405 nm ( = 9,160 M - 1 cm -1 ). Caspase-3/CPP32 is a member of the cysteine proteases family involved in apoptosis induction. All apoptotic pathways studied to date involve proteolytic activation of Caspase-3/CPP32 as a central event in the progression of cell death. Although the death-inducing consequences of Caspase-3/CPP32 activation have not been conclusively established, several crucial substrates for the protease have been identified in vitro, including DNA-dependent protein kinase, Poly (ADP-ribose) Polymerase (PARP), Replication factor C, and Gelsolin. These substrates are involved in the later stages of apoptosis, strongly suggesting that Caspase-3/CPP32 has a key role in promoting the final processes leading to cell death.
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