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Originally published In Press as doi:10.1194/jlr.R800042-JLR200 on October 23, 2008

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Journal of Lipid Research, Vol. 50, S29-S34, April 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Enzymology

Cyclooxygenases: structural and functional insights

Carol A. Rouzer and Lawrence J. Marnett1

A.B. Hancock Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, and Vanderbilt Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville, TN 37232-0146

Research on COX structure and function in the authors' laboratory is supported by grants from the National Institutes of Health (CA-89450 and GM-15431).

Published, JLR Papers in Press, October 23, 2008.

1 To whom correspondence should be addressed. e-mail: larry.marnett{at}vanderbilt.edu


ABSTRACT

Cyclooxygenase (COX; prostaglandin G/H synthase, EC 1.14.99.1) catalyzes the first two steps in the biosynthesis of prostaglandins (PGs). The two COX isoforms COX-1 and COX-2 are the targets of the widely used nonsteroidal anti-inflammatory drugs, indicating a role for these enzymes in pain, fever, inflammation, and tumorigenesis. The ubiquitous constitutive expression of COX-1 and inducible expression of COX-2 have led to the widely held belief that COX-1 produces homeostatic PGs, while PGs produced by COX-2 are primarily pathophysiological. However, recent discoveries call this paradigm into question and reveal as yet underappreciated functions for both enzymes. This review focuses on some of these new insights.

Supplementary key words prostaglandin • endocannabinoid • inflammation • nonsteroidal anti-inflammatory • coxib • hydroperoxide • arachidonic acid • essential fatty acid

Abbreviations: AA, arachidonic acid; 2-AG, 2-arachydonoylglycerol; COX, cyclooxygenase; LPS, lipopolysaccharide; NSAID, nonsteroidal anti-inflammmatory drug; PG, prostaglandin; PG-G, prostaglandin gyceryl ester


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JLR 50th Anniversary Collections
Anniversary Collection:: Enzymology



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