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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

DOI

10.1042/bj3150021

Type

Journal article

Journal

The Biochemical journal

Publication Date

04/1996

Volume

315 ( Pt 1)

Pages

21 - 24

Addresses

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

Keywords

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