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J. Biol. Chem., Vol. 283, Issue 13, 8065-8069, March 28, 2008

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Minireview

Non-redundant Functions of Cyclooxygenases: Oxygenation of Endocannabinoids^*

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

The two cyclooxygenase (COX) enzymes catalyze the oxygenation of arachidonic acid to prostaglandin endoperoxides, which are the common intermediates in the biosynthesis of the bioactive lipids prostaglandins and thromboxane. COX-1 and COX-2 are 60% identical in amino acid sequence, exhibit highly homologous three-dimensional structures, and appear functionally similar at the biochemical level. Recent work has uncovered a subtle functional difference between the two enzymes, namely the ability of COX-2 to efficiently utilize neutral derivatives (esters and amides) of arachidonic acid as substrates. Foremost among these neutral substrates are the endocannabinoids 2-arachidonoylglycerol and arachidonoylethanolamide. This raises the possibility that COX-2 oxygenation plays a role in a novel signaling pathway dependent on agonist-induced release of endocannabinoids and their selective oxygenation by COX-2. Among the products of COX-2 oxygenation of endocannabinoids are glyceryl prostaglandins, some of which (e.g. glyceryl prostaglandin E₂ and glyceryl prostaglandin I₂) exhibit interesting biological activities in inflammatory, neurological, and vascular systems. These compounds are produced in intact cells stimulated with physiological agonists and have been isolated from in vivo sources. Important concepts relevant to the hypothesis of a COX-2-selective signaling pathway are presented.

^* This minireview will be reprinted in the 2008 Minireview Compendium, which will be available in January, 2009. This work was supported by National Institutes of Health Research Grants CA89450 and GM15431.

¹ To whom correspondence should be addressed: Dept. of Biochemistry, Vanderbilt University School of Medicine, 23rd Ave. at Pierce, Nashville, TN 37232-0146. Tel.: 615-343-7327; Fax: 615-343-7534; E-mail: larry.marnett{at}vanderbilt.edu.

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				C. A. Rouzer and L. J. Marnett Cyclooxygenases: structural and functional insights J. Lipid Res., April 1, 2009; 50(Supplement): S29 - S34. [Abstract] [Full Text] [PDF]