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Originally published In Press as doi:10.1074/jbc.M009217200 on January 26, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15666-15675, May 11, 2001
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Cyclic Nucleotides Modulate Store-mediated Calcium Entry through the Activation of Protein-tyrosine Phosphatases and Altered Actin Polymerization in Human Platelets*

Juan A. RosadoDagger , Tanya Porras§, Manuel Conde, and Stewart O. Sage||

From the Department of Physiology, University of Cambridge, Downing Street, Cambridge CB2 3EG, United Kingdom

Agonists elevate the cytosolic calcium concentration in human platelets via a receptor-operated mechanism, involving both Ca2+ release from intracellular stores and subsequent Ca2+ entry, which can be inhibited by platelet inhibitors, such as prostaglandin E1 and nitroprusside which elevate cAMP and cGMP, respectively. In the present study we investigated the mechanisms by which cAMP and cGMP modulate store-mediated Ca2+ entry. Both prostaglandin E1 and sodium nitroprusside inhibited thapsigargin-evoked store-mediated Ca2+ entry and actin polymerization. However, addition of these agents after induction of store-mediated Ca2+ entry did not affect either Ca2+ entry or actin polymerization. Furthermore, prostaglandin E1 and sodium nitroprusside dramatically inhibited the tyrosine phosphorylation induced by depletion of the internal Ca2+ stores or agonist stimulation without affecting the activation of Ras or the Ras-activated phosphatidylinositol 3-kinase or extracellular signal-related kinase (ERK) pathways. Inhibition of cyclic nucleotide-dependent protein kinases prevented inhibition of agonist-evoked Ca2+ release but it did not have any effect on the inhibition of Ca2+ entry or actin polymerization. Phenylarsine oxide and vanadate, inhibitors of protein-tyrosine phosphatases prevented the inhibitory effects of the cGMP and cAMP elevating agents on Ca2+ entry and actin polymerization. These results suggest that Ca2+ entry in human platelets is directly down-regulated by cGMP and cAMP by a mechanism involving the inhibition of cytoskeletal reorganization via the activation of protein tyrosine phosphatases.

* 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.

Dagger Supported by a Grant of Junta de Extremadura-Consejería de Educación y Juventud and Fondo Social Europeo, Spain.

§ Supported by a National Institutes of Health Minority Access to Research Careers Undergraduate Fellowship and the Minority International Research Training Program.

Supported by fellowship from Ministerio de Educación y Cultura/Dirección General de Investigación Científica y Tecnológica, Universidad del Pais Vasco Grants PB94-1357 and UPV 042.310-G11/98, and the Medical Foundation Jesús de Gangoiti-Barrera.

|| 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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