Abstract
The phospholipase A2 (PLA2) superfamily comprises a group of lipolytic enzymes that hydrolyze the sn-2 position of glycerophospholipids (hereafter phospholipids) to release free fatty acids and lysophospholipids. The mammalian genome encodes more than 50 PLA2s or related enzymes, which are classified into several families on the basis of their structures, evolutionary relationships, and functions. These include secreted PLA2s (sPLA2s), cytosolic PLA2s (cPLA2s), Ca2+-independent PLA2s (iPLA2s, also called patatin-like phospholipases (PNPLAs)), platelet-activating factor acetylhydrolases (PAF-AHs), lysosomal PLA2s, PLA/acyltransferases (PLAATs), α/β hydrolases (ABHDs), and glycosylphosphatidylinositol-specific PLA2s. Recent studies using gene-manipulated (transgenic and knockout) mice for various PLA2 enzymes, in combination with comprehensive lipidomics to identify their physiological substrates and products, have revealed distinct roles of individual PLA2s in various pathophysiological events through lipid mediator-dependent and -independent mechanisms. In this review, we make an overview of the latest understanding of the in vivo functions of PLA2s, specifically focusing on cPLA2s and sPLA2s as they are linked to lipid mediator signaling in depth.
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