2. Academic Validation
  3. Phospholipase A2 catalysis and lipid mediator lipidomics

Phospholipase A2 catalysis and lipid mediator lipidomics

  • Biochim Biophys Acta Mol Cell Biol Lipids. 2019 Jun;1864(6):766-771. doi: 10.1016/j.bbalip.2018.08.010.
Varnavas D Mouchlis 1,  Edward A Dennis 2
Affiliations

Affiliations

  • 1 Department of Chemistry and Biochemistry, Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA 92093-0601, United States of America. Electronic address: [email protected].
  • 2 Department of Chemistry and Biochemistry, Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA 92093-0601, United States of America. Electronic address: [email protected].
PMID: 30905345 DOI: 10.1016/j.bbalip.2018.08.010
Abstract

Phospholipase A2 (PLA2) Enzymes are the upstream regulators of the eicosanoid pathway liberating free arachidonic acid from the sn-2 position of membrane Phospholipids. Free intracellular arachidonic acid serves as a substrate for the eicosanoid biosynthetic Enzymes including cyclooxygenases, lipoxygenases, and cytochrome P450s that lead to inflammation. The Group IVA cytosolic (cPLA2), Group VIA calcium-independent (iPLA2), and Group V secreted (sPLA2) are three well-characterized human Enzymes that have been implicated in eicosanoid formation. In this review, we will introduce and summarize the regulation of catalytic activity and cellular localization, structural characteristics, interfacial activation and kinetics, substrate specificity, inhibitor binding and interactions, and the downstream implications for eicosanoid biosynthesis of these three important PLA2 Enzymes.

Keywords

Catalytic mechanism; HD-XMS; LC/MS assays; Molecular dynamics; Phospholipase; Substrate specificity.

Figures