PLA2G4A
PLA2G4A (phospholipase A2 group IVA, also known as cytosolic phospholipase A2, cPLA2-alpha or PLA2G4) is a calcium-dependent phospholipase that releases arachidonic acid from membrane phospholipids. This step supplies the precursor for eicosanoid biosynthesis and inflammatory lipid mediators. Browse Assay Genie's current range of PLA2G4A research reagents below, or read on for the biology behind the target.
PLA2G4A has primarily calcium-dependent phospholipase and lysophospholipase activities and plays a major role in membrane lipid remodelling and in the biosynthesis of lipid mediators of the inflammatory response. It preferentially hydrolyses the ester bond of the fatty acyl group at the sn-2 position of phospholipids, and selectively removes sn-2 arachidonoyl groups from membrane phospholipids. The released arachidonic acid is the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative route, the enzyme hydrolyses the sn-2 fatty acyl chain of eicosanoid lysophospholipids to release free bioactive eicosanoids.
The enzyme shows further activities. It has phospholipase A1 activity at the sn-1 position only when an ether linkage rather than an ester linkage is present at sn-2, and this hydrolysis is not stereospecific. In the presence of phosphoinositides it has calcium-independent phospholipase A2 and lysophospholipase activities. It also has O-acyltransferase activity, transferring fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol, which may contribute to monoacylglycerol synthesis. The hydrolysis reaction also produces lysophospholipids that are converted into platelet-activating factor.
The PLA2G4A gene encodes a member of the cytosolic phospholipase A2 group IV family, listed by HGNC among the C2 domain containing phospholipases; its previous name was phospholipase A2, group IVA (cytosolic, calcium-dependent). The enzyme is activated by increased intracellular Ca(2+) and by phosphorylation, which drives its translocation from the cytosol and nucleus to perinuclear membrane vesicles. Eicosanoids, including prostaglandins and leukotrienes, regulate haemodynamics and inflammatory responses, and PLA2G4A is important in embryo implantation and parturition through its ability to trigger prostanoid production. Alternative splicing gives multiple transcript variants. Mouse and rat orthologs are both named Pla2g4a.
PLA2G4A supplies the arachidonic acid precursor for eicosanoids, making it central to studies of inflammatory lipid mediator biosynthesis.
The enzyme feeds the cyclooxygenase pathway and can also release free eicosanoids from lysophospholipids, giving two routes to examine.
Its phospholipase, lysophospholipase and O-acyltransferase activities make it a focus for work on phospholipid turnover and monoacylglycerol synthesis.
PLA2G4A triggers prostanoid production and has an important role in embryo implantation and parturition.
PLA2G4A is a calcium-dependent phospholipase that hydrolyses the sn-2 acyl group of membrane phospholipids, preferentially releasing arachidonic acid. This is the precursor for prostaglandins and leukotrienes. It also has lysophospholipase and O-acyltransferase activities, and it is activated by raised Ca(2+) and phosphorylation.
PLA2G4A is also called cytosolic phospholipase A2, cPLA2-alpha and PLA2G4. HGNC lists its previous name as phospholipase A2, group IVA (cytosolic, calcium-dependent). Alternative splicing of the gene results in multiple transcript variants, so different transcripts may be described in the literature.
Yes. Both mouse and rat have an ortholog named Pla2g4a. Its roles in eicosanoid production, embryo implantation and parturition are described in UniProt. Check the datasheet of any product for its validated reactivity.
Other phospholipase A2 group members, related phospholipases and lipid-mediator pathway targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P47712; product specifications from Assay Genie datasheets.