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Phospholipase A2 structure/function, mechanism, and signaling

Journal of Lipid Research · 2008 · Vol. 50 · pp. S237–S242
John E. BurkeEdward A. Dennis

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.

Protein Kinase Regulation and GTPase SignalingVitamin K Research StudiesPeroxisome Proliferator-Activated ReceptorsPhospholipase A2PhospholipaseSUPERFAMILYLipid signalingEnzymeCytosolFunction (biology)ChemistryBiochemistryCell biology

MeSH terms

AnimalsCalciumCytosolHumansSignal Transduction1-Alkyl-2-acetylglycerophosphocholine EsteraseLipid MetabolismPhospholipases A2

Funding

  • National Institutes of Health
Citations
893
FWCI
21.24
field-weighted impact
References
70
Percentile
100%
vs. same field & year
Citations per year
References
Ghrelin: Structure and Function
Physiological Reviews · 2005 · 2,790 citations
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