Cytosolic phospholipase A2 and lysophospholipid acyltransferases

Abstract

Phospholipase A₂ (PLA₂) enzymes catalyze the hydrolysis of ester bonds at sn-2 positions of glycerophospholipids (PL), producing free fatty acids and lysophospholipids. In mammals, the PLA₂ superfamily comprises more than 30 known enzymes, including various structurally and biochemically different enzymes with diverse biological functions. Some of the enzymes are involved in the production of lipid mediators, including eicosanoids and lysophospholipid-related lipid mediators. Among them, cytosolic PLA₂α (cPLA₂α), a member of cPLA₂ family, is one of the most important intracellular PLA₂s. Upon cell activation, cPLA₂α is activated and involved in eicosanoid production under various physiological and pathological conditions. PLA₂s also play a role in membrane PL remodeling by coupling with re-acylation processes mediated by lysophospholipid acyltransferases (LPLATs) to generate sn-1/sn-2 fatty acid asymmetry of PLs. This review summarizes the biochemical and in vivo roles of cPLA₂ enzymes and LPLATs, including results from animal and human studies. This article is part of a Special Issue entitled Novel functions of phospholipase A₂ Guest Editors: Makoto Murakami and Gerard Lambeau.

Keywords: Eicosanoids; Lipid mediators; Lysophospholipid acyltransferase; Membrane glycerophospholipids; Phospholipase A(2); Platelet-activating factor.