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J. Biol. Chem., Vol. 275, Issue 28, 21416-21421, July 14, 2000
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,§,
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From the The mechanisms of UVB-induced apoptosis and the
role of p38 mitogen-activated protein kinase (MAPK) were investigated
in HaCaT cells. UVB doses that induced apoptosis also produced a
sustained activation of p38 MAPK and mitochondrial cytochrome
c release, leading to pro-caspase-3 activation. Late into
the apoptotic process, UVB also induced a caspase-mediated cleavage
of Bid. Caspase inhibitors benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone and
benzyloxycarbonyl-Asp-Glu-Val-Asp-fluoromethylketone substantially
blocked the UVB-induced apoptosis without preventing the release
of mitochondrial cytochrome c and the p38 MAPK activation. The inhibition of p38 MAPK counteracted both apoptosis and cytochrome c release as well as the DEVD-amino-4-methylcoumarin
cleavage activity without affecting the processing of pro-caspase-8.
These results indicate that UVB induces multiple and independent
apoptotic pathways, which culminate in pro-caspase-3 activation, and
that the initial cytochrome c release is independent of
caspase activity. Importantly, we show that a sustained p38 MAPK
activation contributes to the UVB-induced apoptosis by mediating the
release of mitochondrial cytochrome c into the cytosol.
Division of Biochemistry and
¶ Laboratory of Dermatology, Faculty of Medicine, Katholieke
Universiteit Leuven, Herestraat 49, B-3000 Leuven, Belgium and the
Department of Molecular Biology, Flanders Interuniversity
Institute for Biotechnology, University of Gent, Ledeganckstraat 35, B-9000 Gent, Belgium
Research director with the FWO-Vlaanderen.
§§
To whom correspondence should be addressed. Tel.: 32-16-345-715;
Fax: 32-16-345-995; E-mail:
patricia.agostinis@med.kuleuven.ac.be.
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