title: Phospholipase A2 structure/function, mechanism, and signaling.
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.
authors.affiliation: Department of Chemistry, School of Medicine, University of California, San Diego, La Jolla, CA 92093-0601, USA.
authors.forename: John E
authors.initials: JE
authors.lastname: Burke
authors.forename: Edward A
authors.initials: EA
authors.lastname: Dennis
mesh_terms: D043203:1-Alkyl-2-acetylglycerophosphocholine Esterase / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology; D006801:Humans; D050356:Lipid Metabolism; D054467:Phospholipases A2 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D054467:Phospholipases A2; D043203:1-Alkyl-2-acetylglycerophosphocholine Esterase; D002118:Calcium