Cytosolic phospholipase A2 and lysophospholipid acyltransferases.

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.

• Publication year

  2019

• Venue

  Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

• Publication date

  2019-06-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.bbalip.2018.08.006PMID 30905348
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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