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J. Biol. Chem., Vol. 276, Issue 19, 16484-16490, May 11, 2001
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From the The tumor necrosis factor (TNF), Fas, and
TNF-related apoptosis-inducing ligand (TRAIL) receptors (R) are
highly specific physiological mediators of apoptotic signaling.
We observed earlier that a number of FasR-insensitive cell lines
could redirect the proapoptotic signal to an anti-apoptotic ERK1/2
signal resulting in inhibition of caspase activation. Here we determine
that similar mechanisms are operational in regulating the apoptotic
signaling of other death receptors. Activation of the FasR,
TNF-R1, and TRAIL-R, respectively, rapidly induced subsequent
ERK1/2 activation, an event independent from caspase activity. Whereas
inhibition of the death receptor-mediated ERK1/2 activation was
sufficient to sensitize the cells to apoptotic signaling from
FasR and TRAIL-R, cells were still protected from apoptotic
TNF-R1 signaling. The latter seemed to be due to the strong activation
of the anti-apoptotic factor NF-
MAPK/ERK Overrides the Apoptotic Signaling from Fas, TNF, and
TRAIL Receptors*
§¶,§
,¶,**, and§§
Turku Centre for Biotechnology, POB 123, FIN-20521, the ¶ Turku Graduate School of Biomedical Science, the
§ Department of Biology, Åbo Akademi University, BioCity,
FIN-20520, and the Departments of Biology,
Laboratory of Animal Physiology, FIN-20014 and ** Medical Biochemistry
and Dermatology, FIN-20520, University of Turku, Turku, Finland
B, which remained inactive in FasR
or TRAIL-R signaling. However, when the cells were sensitized with
cycloheximide, which is sufficient to sensitize the cells also to
apoptosis by TNF-R1 stimulation, we noticed that adenovirus-mediated
expression of constitutively active MKK1 could rescue the cells from
apoptosis induced by the respective receptors by preventing caspase-8
activation. Taken together, our results show that ERK1/2 has a dominant
protecting effect over apoptotic signaling from the death receptors.
This protection, which is independent of newly synthesized
proteins, acts in all cases by suppressing activation of the caspase
effector machinery.
*
This work was supported by Grant 35718 from the Academy of
Finland, the Sigrid Jusélius Foundation, the Erna and Victor
Hasselblad Foundation, the Finnish Cancer Foundation, the Nordic
Academy for Advanced Study (NorFA), the Cell Signaling Program of Åbo Akademi University, EVO Grant 13336 from the Turku University Central
Hospital, and the Turku Graduate School of Biomedical Sciences (to
S. E. F. T., T. H. H., and M. A.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Current address: Dept. of Cell Biology, Max-Planck-Institut
for Biochemistry, D-82152, Martinsried, Germany.
§§
To whom correspondence should be addressed: Dept. of Biology,
Laboratory of Animal Physiology, Science Bldg. 1, University of Turku,
FIN-20014 Turku, Finland. Tel.: 358-2-333-8036; Fax: 358-2-333-8000;
E-mail: john.eriksson@utu.fi.
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