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Papers In Press, published online ahead of print June 1, 2009
J. Lipid Res., doi:10.1194/jlr.R900004-JLR200

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Journal of Lipid Research, Vol. 50, 1015-1038, June 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Thematic Review

Thematic Review Series: Proteomics. An integrated omics analysis of eicosanoid biology^1,

Matthew W. Buczynski, Darren S. Dumlao and Edward A. Dennis²

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

¹ Guest editor for this article was Jay W. Heinecke, JLR Associate Editor, University of Washington.

The online version of this article (available at http://www.jlr.org) contains supplementary data in the form of seven tables.

This work was supported by the National Institutes of Health LIPID MAPS Large Scale Collaborative Grant GM069338 and R01 GM64611 and GM20501. M.W.B. was supported by Gastroenterology Pre-doctoral Training Grant 2T32DK007202-32 from the National Institutes of Health.

Published, JLR Papers in Press, February 24, 2009.

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

Eicosanoids have been implicated in a vast number of devastating inflammatory conditions, including arthritis, atherosclerosis, pain, and cancer. Currently, over a hundred different eicosanoids have been identified, with many having potent bioactive signaling capacity. These lipid metabolites are synthesized de novo by at least 50 unique enzymes, many of which have been cloned and characterized. Due to the extensive characterization of eicosanoid biosynthetic pathways, this field provides a unique framework for integrating genomics, proteomics, and metabolomics toward the investigation of disease pathology. To facilitate a concerted systems biology approach, this review outlines the proteins implicated in eicosanoid biosynthesis and signaling in human, mouse, and rat. Applications of the extensive genomic and lipidomic research to date illustrate the questions in eicosanoid signaling that could be uniquely addressed by a thorough analysis of the entire eicosanoid proteome.

Supplementary key words genomics • proteomics • lipidomics • cyclooxygenase • lipoxygenase • cytochrome P450 • prostaglandin • leukotriene • eicosanoid

Abbreviations: AKR, aldo-keto reductase; ALX, lipoxin A₄ receptor; COX, cyclooxygenase; CRTH2, chemoattractant receptor-homologous, molecule expressed on Th2 cells; CYP, cytochrome P450; cysLT, cysteinyl leukotrienes; DHET, dihydroxyeicosatrienoic acid; EET, epoxyeicosatrienoic acid; EX, eoxin; FLAP, 5-lipoxygenase activating protein; GGL, -glutamyl leukotrienase; GGT, -glutamyl transpeptidase; GPCR, G protein-coupled receptor; HETE, hydroxyeicosatetraenoic acid; HpETE, hydroperoxy-eicosatetraenoic acid; HX, hepoxilin; 9K-PGR, 9-keto prostaglandin reductase; LT, leukotriene; LTAH, leukotriene A₄ hydrolase; LTB₄DH, leukotriene B₄ 12-hydroxydehydrogenase; LTCS, leukotriene C₄ synthase; LIPID MAPS, Lipid Metabolites and Pathways Strategies; LOX, lipoxygenase; LX, lipoxin; MAPEG, membrane-associated protein in eicosanoid and glutathione; MBD, membrane-bound dipeptidase; mGST, microsomal glutathione S-transferase; PG, prostaglandin; PGDH, prostaglandin dehydrogenase; PGDS, prostaglandin D synthase; PGES, PGE synthase; PGFS, prostaglandin F synthase; PGR, prostaglandin reductase; PLA₂, phospholipase A₂; PPAR, peroxisome proliferator-activated receptor; sEH, soluble epoxide hydrolase; TRPV4, vanilloid type 4 receptor; TXA₂, thromboxane A₂; 11-TXDH, 11-dehydroxythromboxane B₂ dehydrogenase

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