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A cleavage-site-directed inhibitor of interleukin-1<i>β</i>-converting enzyme-like proteases inhibits apoptosis in primary cultures of rat hepatocytes

Biochemical JournalPublished 15 February 1996Open access
Kelvin Cain, Salmaan H. Inayat‐Hussain, Carole Couet, Gerald M. Cohen
Citations76
SJR quartileQ1
SJR score2.06
SNIP0.98
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TL;DR

These effects were abolished by benzyloxycarbonyl-valinylalanylas partylfluoromethyl ketone, a cleavage-site-directed inhibitor of interleukin-1beta-converting enzyme-like proteases, and this finding suggests that these enzymes are involved in liver apoptosis.

Abstract

Apoptosis induced in primary hepatocytes by transforming growth factor beta1 and staurosporine produced chromatin condensation, DNA cleavage is detected by in situ end-labelling, field inversion and conventional gel electrophoresis, and cell detachment. These effects were abolished by benzyloxycarbonyl-valinylalanylaspartylfluoromethyl ketone, a cleavage-site-directed inhibitor of interleukin-1beta-converting enzyme-like proteases, and this finding suggests that these enzymes are involved in liver apoptosis.

Keywords

MedicineBiochemistry, Genetics and Molecular Biology