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J Biol Chem, Vol. 275, Issue 5, 3179-3191, February 4, 2000

Exogenously Added Human Group X Secreted Phospholipase A2 but Not the Group IB, IIA, and V Enzymes Efficiently Release Arachidonic Acid from Adherent Mammalian Cells*

Sofiane Bezzineabc, Rao S. Koduriabc, Emmanuel Valentincde, Makoto Murakamifg, Ichiro Kudofg, Farideh Ghomashchiab, Martin Sadileka, Gérard Lambeaudh, and Michael H. Gelbabi

From the Departments of a Chemistry and b Biochemistry, University of Washington, Seattle, Washington 98195, the d Institut de Pharmacologie Moleculaire et Cellulaire, CNRS, UPR 411, 660 Route des Lucioles, Sophia Antipolis, 06560 Valbonne, France, and f Department of Health Chemistry, School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142, Japan

Mammalian secreted phospholipases A2 (sPLA2s) comprise a group of at least eight enzymes, including the recently identified group X sPLA2. A bacterial expression system was developed to produce human group X sPLA2 (hGX). Inhibition studies show that the sPLA2 inhibitor LY311727 binds modestly more tightly to human group IIA sPLA2 than to hGX and that a pyrazole-based inhibitor of group IIA sPLA2 is much less active against hGX. The phospholipid head group preference of vesicle-bound hGX was determined. hGX binds tightly to phosphatidylcholine vesicles, which is thought to be required to act efficiently on cells. Tryptophan 67 hGX makes a significant contribution to interfacial binding to zwitterionic vesicles. As little as 10 ng/ml hGX releases arachidonic acid for cyclooxygenase-2- dependent prostaglandin E2 generation when added exogenously to adherent mammalian cells. In contrast, human group IIA, rat group V, and mouse group IB sPLA2s are virtually inactive at releasing arachidonate when added exogenously to adherent cells. Dislodging cells from the growth surface enhances the ability of all the sPLA2s to release fatty acids. Studies with CHO-K1 cell mutants show that binding of sPLA2s to glycosaminoglycans is not the basis for poor plasma membrane hydrolysis by group IB, IIA, and V sPLA2s.

* This work was supported in part by Grant HL36235 from the National Institutes of Health (to M. H. G.) and Grant CHE 9807748 from the National Science Foundation Chemistry Instrumentation (to U. W.).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.

c These three authors contributed equally to this study.

e Recipient of a grant from the region Provence Alpes Côte d'Azur-CNRS program.

g Supported by Grants-in-aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, the Human Science Foundation, and Special Coordination Funds for Promoting Science and Technology from the Science and Technology Agency.

h Supported by the CNRS, ARC, and the Ministère de la Defense Nationale Grant DGA-DRET 96/096.

i To whom correspondence should be addressed: Depts. of Chemistry and Biochemistry, University of Washington, Box 351700, Seattle, WA 98195. Tel.: 206-543-7142; Fax: 206-685-8665; E-mail: gelb@chem. washington.edu.

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