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An interleukin‐1β‐converting enzyme‐like protease is a common mediator of apoptosis in thymocytes
Author(s) -
Fearnhead Howard O.,
Dinsdale David,
Cohen Gerald M.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01228-7
Subject(s) - apoptosis , poly adp ribose polymerase , biology , protease , microbiology and biotechnology , proteolysis , chromatin , programmed cell death , flow cytometry , enzyme , dna , polymerase , biochemistry
Apoptosis was induced in thymocytes using diverse stimuli in order to identify events within a common apoptotic pathway. Benzyloxycarbonyl‐valinyl‐alaninyl‐aspartyl fluoromethyl ketone (Z‐VAD.FMK), an interleukin‐1β‐converting enzyme (ICE)‐like protease inhibitor, inhibited apoptosis assessed by flow cytometry, proteolysis of poly (ADP)‐ribose polymerase (PARP), an early biochemical marker of apoptosis, and cleavage of DNA to both large kilobase pair fragments.(30–50 and 200–300 kbp) and to nucleosomal fragments. Z‐VAD.FMK also blocked all the classical ultrastructural features of apoptosis including chromatin condensation to one pole of the nucleus, nucleolar disintegration and cytoplasmic vacuolation. These results suggest the involvement of an ICE‐like protease as a common mediator of apoptosis in thymocytes.