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Originally published In Press as doi:10.1074/jbc.M203137200 on September 19, 2002

J. Biol. Chem., Vol. 277, Issue 50, 48523-48534, December 13, 2002
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On the Binding Preference of Human Groups IIA and X Phospholipases A2 for Membranes with Anionic Phospholipids*

Sofiane BezzineDagger §, James G. BollingerDagger §, Alan G. SingerDagger §, Sarah L. Veatch, Sarah L. KellerDagger , and Michael H. GelbDagger §||

From the Departments of Dagger  Chemistry, § Biochemistry, and  Physics, University of Washington, Seattle, Washington 98195

Mammals contain 9-10 secreted phospholipases A2 (sPLA2s) that display widely different affinities for membranes, depending on the phospholipid composition. The much higher enzymatic activity of human group X sPLA2 (hGX) compared with human group IIA sPLA2 (hGIIA) on phosphatidylcholine (PC)-rich vesicles is due in large part to the higher affinity of the former enzyme for such vesicles; this result also holds when vesicles contain cholesterol and sphingomyelin. The inclusion of anionic phosphatidylserine in PC vesicles dramatically enhances interfacial binding and catalysis of hGIIA but not of hGX. This is the result of the large number of lysine and arginine residues scattered over the entire surface of hGIIA, which cause the enzyme to form a supramolecular aggregate with multiple vesicles. Thus, high affinity binding of hGIIA to anionic vesicles is a complex process and cannot be attributed to a few basic residues on its interfacial binding surface, as is also evident from mutagenesis studies. The main reason hGIIA binds poorly to PC-rich vesicles is that it lacks a tryptophan residue on its interfacial binding surface, a residue that contributes to the high affinity binding of hGX to PC-rich vesicles. Results show that the lag in the onset of hydrolysis of PC vesicles by hGIIA is due in part to the poor affinity of this enzyme for these vesicles. Binding affinity of hGIIA, hGX, and their mutants to PC-rich vesicles is well correlated to the ability of these enzymes to act on the PC-rich outer plasma membrane of mammalian cells.

* This work was supported by National Institutes of Health Grant HL36236 (to M. H. G.), a National Science Foundation Career Award, the Petroleum Research Fund (American Chemical Society), the Royalty Research Fund (University of Washington) (to S. L. K.), and a University of Washington Center for Nanotechnology IGERT Graduate Fellowship (to S. L. V.).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.

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

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