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J Biol Chem, Vol. 273, Issue 26, 16415-16420, June 26, 1998
From the p38, a subfamily of the mitogen-activated protein
kinase, regulates gene expression in response to various extracellular
stimuli. The pyridinyl imidazoles like SB202190 are specific inhibitors of p38
Induction of Apoptosis by SB202190 through Inhibition of p38
Mitogen-activated Protein Kinase
,
Department of Pathology and the
§ Gene Therapy Program, University of Alabama at Birmingham,
Birmingham, Alabama 35294 and the ¶ Department of Immunology, The
Scripps Research Institute, La Jolla, California 92037
and p38
and have been widely used in investigation of the
biological functions of p38. Here we show that SB202190 by itself was
sufficient to induce cell death, with typical apoptotic features
such as nucleus condensation and intranucleosomal DNA fragmentation.
SB202190 stimulated the activity of CPP32-like caspases, and its
apoptotic effect was completely blocked by the protease inhibitor
benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone and expression of
bcl-2. In addition, SB202190 was able to potentiate
apoptosis induced by Fas(APO-1) ligation or UV irradiation. Expression
of p38 attenuated the apoptotic effect of SB202190 and the cell
death induced by Fas ligation and UV irradiation. In contrast,
expression of p38 induced cell death mildly. These results indicate
that SB202190 induces apoptosis through activation of CPP32-like
caspases and suggest that distinct members of the p38 subfamily of
mitogen-activated protein kinase have different functions in
apoptosis.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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T.-L. Yu |
