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Originally published In Press as doi:10.1074/jbc.M205855200 on September 30, 2002

J. Biol. Chem., Vol. 277, Issue 50, 48535-48549, December 13, 2002
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Interfacial Kinetic and Binding Properties of the Complete Set of Human and Mouse Groups I, II, V, X, and XII Secreted Phospholipases A2*

Alan G. SingerDagger , Farideh GhomashchiDagger , Catherine Le Calvez§, James BollingerDagger , Sofiane BezzineDagger , Morgane Rouault§||, Martin SadilekDagger , Eric Nguyen§, Michel Lazdunski§, Gérard Lambeau§**§§, and Michael H. GelbDagger Dagger Dagger

From the Dagger  Departments of Chemistry and Biochemistry, University of Washington, Seattle, Washington 98195 and the § Institut de Pharmacologie Moléculaire et Cellulaire, CNRS-UPR 411, 660 route des Lucioles, Sophia Antipolis, Valbonne 06560, France

Expression of the full set of human and mouse groups I, II, V, X, and XII secreted phospholipases A2 (sPLA2s) in Escherichia coli and insect cells has provided pure recombinant enzymes for detailed comparative interfacial kinetic and binding studies. The set of mammalian sPLA2s display dramatically different sensitivity to dithiothreitol. The specific activity for the hydrolysis of vesicles of differing phospholipid composition by these enzymes varies by up to 4 orders of magnitude, and yet all enzymes display similar catalytic site specificity toward phospholipids with different polar head groups. Discrimination between sn-2 polyunsaturated versus saturated fatty acyl chains is <6-fold. These enzymes display apparent dissociation constants for activation by calcium in the 1-225 µM range, depending on the phospholipid substrate. Analysis of the inhibition by a set of 12 active site-directed, competitive inhibitors reveals a large variation in the potency among the mammalian sPLA2s, with Me-Indoxam being the most generally potent sPLA2 inhibitor. A dramatic correlation exists between the ability of the sPLA2s to hydrolyze phosphatidylcholine-rich vesicles efficiently in vitro and the ability to release arachidonic acid when added exogenously to mammalian cells; the group V and X sPLA2s are uniquely efficient in this regard.

* This work was supported in part by National Science Foundation Grant 9807748 for the Esquire mass spectrometer.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.

Recipient of a postdoctoral fellowship from the Association de la Recherche contre le Cancer.

|| Recipient of a doctoral ingenior fellowship from the CNRS.

** Supported by the CNRS, the Association pour la Recherche sur le Cancer, and the Fonds de Recherche Hoechst Marion Roussel.

Dagger Dagger Supported by National Institutes of Health Grant HL36236. To whom correspondence should be addressed: Dept. 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.

§§ To whom correspondence should be addressed. Tel.: 33-4-93-95-77-31; Fax: 33-4-93-95-77-04; E-mail: lambeau@ipmc.cnrs.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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