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J. Biol. Chem., Vol. 276, Issue 19, 15659-15665, May 11, 2001
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From the Department of Physiology, University of Cambridge, Downing
Street, Cambridge CB2 3EG, United Kingdom
Extracellular signal-regulated kinases
(ERKs), are common participants in a broad variety of signal
transduction pathways. Several studies have demonstrated the presence
of ERKs in human platelets and their activation by the physiological
agonist thrombin. Here we report the involvement of the ERK cascade in
store-mediated Ca2+ entry in human platelets.
Treatment of
dimethyl-bis-(o-aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid-loaded platelets with thapsigargin to deplete the
intracellular Ca2+ stores resulted in a time- and
concentration-dependent activation of ERK1 and ERK2.
Incubation with either U0126 or PD 184352, specific inhibitors of
mitogen-activated protein kinase kinase (MEK), prevented thapsigargin-induced ERK activation. Furthermore, U0126 and PD 184352 reduced Ca2+ entry stimulated by thapsigargin or thrombin,
in a concentration-dependent manner. The role of ERK in
store-mediated Ca2+ entry was found to be independent of
phosphatidylinositol 3- and 4-kinases, the tyrosine kinase pathway, and
actin polymerization but sensitive to treatment with inhibitors of Ras,
suggesting that the ERK pathway might be a downstream effector of Ras
in mediating store-mediated Ca2+ entry in human platelets.
In addition, we have found that store depletion stimulated ERK
activation does not require PKC activity. This study demonstrates for
the first time a novel mechanism for regulation of store-mediated
Ca2+ entry in human platelets involving the ERK cascade.
Role of the ERK Pathway in the Activation of Store-mediated
Calcium Entry in Human Platelets*
and
*
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.
Supported by a Grant of Junta de Extremadura-Consejería de
Educación y Juventud and Fondo Social Europeo, Spain.
§
To whom correspondence should be addressed: Dept. of Physiology,
Downing Street, University of Cambridge, Cambridge CB2 3EG, United
Kingdom. Tel.: 44-1223-333870; Fax: 44-1223-333840; E-mail: sos10@cam.ac.uk.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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