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Prostaglandin E synthase, a terminal enzyme for prostaglandin E2 biosynthesis Kudo I; Murakami MJ Biochem Mol Biol 2005[Nov]; 38 (6): 633-8Biosynthesis of prostanoids is regulated by three sequential enzymatic steps, namely phospholipase A2 enzymes, cyclooxygenase (COX) enzymes, and various lineagespecific terminal prostanoid synthases. Prostaglandin E synthase (PGES), which isomerizes COX-derived PGH2 specifically to PGE2, occurs in multiple forms with distinct enzymatic properties, expressions, localizations and functions. Two of them are membrane-bound enzymes and have been designated as mPGES-1 and mPGES-2. mPGES-1 is a perinuclear protein that is markedly induced by proinflammatory stimuli, is down-regulated by antiinflammatory glucocorticoids, and is functionally coupled with COX-2 in marked preference to COX-1. Recent gene targeting studies of mPGES-1 have revealed that this enzyme represents a novel target for anti-inflammatory and anti-cancer drugs. mPGES-2 is synthesized as a Golgi membrane-associated protein, and the proteolytic removal of the N-terminal hydrophobic domain leads to the formation of a mature cytosolic enzyme. This enzyme is rather constitutively expressed in various cells and tissues and is functionally coupled with both COX-1 and COX-2. Cytosolic PGES (cPGES) is constitutively expressed in a wide variety of cells and is functionally linked to COX-1 to promote immediate PGE2 production. This review highlights the latest understanding of the expression, regulation and functions of these three PGES enzymes.|*Gene Expression Regulation, Enzymologic[MESH]|Animals[MESH]|Anti-Inflammatory Agents, Non-Steroidal/pharmacology[MESH]|Anti-Inflammatory Agents/pharmacology[MESH]|Cytosol/metabolism[MESH]|Dinoprostone/*biosynthesis/metabolism[MESH]|Glucocorticoids/metabolism[MESH]|Golgi Apparatus/metabolism[MESH]|Humans[MESH]|Inflammation[MESH]|Intramolecular Oxidoreductases/*physiology[MESH]|Mice[MESH]|Models, Biological[MESH]|Prostaglandin-E Synthases[MESH]|Protein Structure, Tertiary[MESH] |
