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J Biol Chem, Vol. 273, Issue 17, 10792-10797, April 24, 1998
From the Laboratorio Glaxo Wellcome-Consejo Superior de
Investigaciones Científicas de Biología Molecular y
Celular, Centro de Biología Molecular "Severo Ochoa"
(Consejo Superior de Investigaciones Científicas-Universidad
Autónoma de Madrid), Universidad Autónoma, Canto
Blanco, 28049 Madrid, Spain
Considerable attention has recently been focused
on the role played by different kinase cascades in the control of
apoptosis. The triggering of stress-activated kinases concomitant with
the inhibition of the extracellular signal-regulated kinase (ERK) pathway has been observed in a number of cell systems undergoing programmed cell death. In addition, the activation of the
phosphoinositide 3-kinase (PI 3-kinase)-Akt signaling cascade has been
shown to protect from apoptosis. Here we have explored the potential
role played by the inhibition of ERK in the activation of the stress kinases as well as the possible cross-talk with the PI 3-kinase pathway
in HeLa cells. We show that the simple inhibition of ERK basal activity
is sufficient to trigger apoptosis and p38 activation with no changes
in Jun N-terminal kinase/stress-activated protein kinase. This is a
process dependent on the caspases and is completely abrogated by serum.
The incubation with wortmannin or the transfection of dominant negative
mutants of p85 or Akt block the inhibitory function of serum,
suggesting the involvement of the PI 3-kinase-Akt system. Consistent
with this, expression of active mutants of PI 3-kinase and Akt inhibits
p38 activation and apoptosis. We also show here that the inhibition of
ERK triggers the caspase system, which is abolished by serum in a
wortmannin-dependent manner. Collectively, these results
demonstrate a link between ERK and the p38 apoptotic pathway that is
modulated by the survival PI 3-kinase-Akt module, acting upstream the
caspase system.
The Activation of p38 and Apoptosis by the Inhibition of Erk Is
Antagonized by the Phosphoinositide 3-Kinase/Akt Pathway
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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