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Originally published In Press as doi:10.1074/jbc.M907390199 on March 16, 2000

J. Biol. Chem., Vol. 275, Issue 21, 15758-15764, May 26, 2000
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Soluble E-selectin Acts in Synergy with Platelet-activating Factor to Activate Neutrophil beta 2-Integrins
ROLE OF TYROSINE KINASES AND Ca2+ MOBILIZATION*

Marie-Hélène Ruchaud-SparaganoDagger , Trevor R. Walker, Adriano G. Rossi, Christopher Haslett, and Ian Dransfield

From the Rayne Laboratory, Respiratory Medicine Unit, University of Edinburgh Medical School, Edinburgh EH8 9AG, United Kingdom

Selectins play a critical role in neutrophil recruitment to sites of inflammation, in tethering and rolling of neutrophils on vascular endothelium, as well as triggering beta 2-integrin-mediated adhesion. We have previously demonstrated potential pro-inflammatory effects of soluble E-selectin upon neutrophil effector functions, using a soluble recombinant molecule (E-zz), which increased beta 2-integrin-mediated adhesion, decreased beta 2-integrin-dependent migration, and triggered reactive oxygen species generation and release. In this study, we have examined the intracellular signals following neutrophil activation by soluble E-selectin. We show that exposure of neutrophils to E-selectin and platelet-activating factor (PAF) in combination induced a synergistic effect upon beta 2-integrin-mediated adhesion. Although soluble E-selectin did not induce Ca2+ mobilization in neutrophils by itself, elevation of intracellular Ca2+ was specifically prolonged in response to PAF but not leukotriene B4 or N-formyl-Met-Leu-Phe. The prolonged Ca2+ mobilization observed in the presence of E-selectin was dependent on Ca2+ influx from intracellular stores rather than influx of extracellular Ca2+ through SKF 96365-sensitive channels. The specific alteration of Ca2+ mobilization reported here appears not to have a role in the synergistic effects of E-selectin and PAF upon neutrophil O&cjs1138;2 release but may be involved in augmentation of beta 2-integrin-mediated adhesion.

* This work was supported by the Scottish Hospital Endowment Research Trust and by Arthritis Research Campaign Grant D0570.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 To whom correspondence should be addressed: Rayne Lab., Respiratory Medicine Unit, University of Edinburgh Medical School, Teviot Place, Edinburgh EH8 9AG, UK. Tel.: 44-131-650-6948; Fax: 44-131-650-4384; E-mail: mhs@srv1.med.ed.ac.uk.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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