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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.R800033-JLR200 on November 14, 2008

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Journal of Lipid Research, Vol. 50, S237-S242, April 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Signaling

Phospholipase A2 structure/function, mechanism, and signaling1

John E. Burke and Edward A. Dennis2

Departments of Chemistry and Biochemistry, and Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA 92093-0601

1 Guest editor for this article was Martha K. Cathcart, Lerner Research Institute, the Cleveland Clinic.

This work was supported by National Institutes of Health Grant GM20501 (E.A.D).

Published, JLR Papers in Press, November 14, 2008.

2 To whom correspondence should be addressed. e-mail: edennis{at}ucsd.edu


ABSTRACT

Tremendous advances in understanding the structure and function of the superfamily of phospholipase A2 (PLA2) enzymes has occurred in the twenty-first century. The superfamily includes 15 groups comprising four main types including the secreted sPLA2, cytosolic cPLA2, calcium-independent iPLA2, and platelet activating factor (PAF) acetyl hydrolase/oxidized lipid lipoprotein associated (Lp)PLA2. We review herein our current understanding of the structure and interaction with substrate phospholipids, which resides in membranes for a representative of each of these main types of PLA2. We will also briefly review the development of inhibitors of these enzymes and their roles in lipid signaling.

Supplementary key words lipid signaling • phospholipids • arachidonic acid


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JLR 50th Anniversary Collections
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