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Interleukin-1 beta converting enzyme (ICE)-like proteases, which are synthesized as inactive precursors, play a key role in the induction of apoptosis. We now demonstrate that benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK), an ICE-like protease inhibitor, inhibits apoptosis by preventing the processing of CPP32 to its active form. These results suggest that novel inhibitors of apoptosis can be developed which prevent processing of proforms of ICE-like proteases.

Original publication




Journal article


The Biochemical journal

Publication Date



315 ( Pt 1)


21 - 24


MRC Toxicology Unit, University of Leicester, Lancaster Road, Leicester, U.K.


Tumor Cells, Cultured, Humans, Leukemia, Monocytic, Acute, Leukemia, T-Cell, Cysteine Endopeptidases, Caspases, Poly(ADP-ribose) Polymerases, Amino Acid Chloromethyl Ketones, Oligopeptides, Protease Inhibitors, Cysteine Proteinase Inhibitors, Apoptosis, Enzyme Activation, Amino Acid Sequence, Molecular Sequence Data, Caspase 3, Poly(ADP-ribose) Polymerase Inhibitors