PLA2G2A
PLA2G2A (phospholipase A2 group IIA, also known as PLA2B and PLA2L) is a secreted, calcium-dependent phospholipase A2 that hydrolyses the sn-2 fatty acyl bond of phospholipids. It contributes to host antimicrobial defence, inflammatory responses and tissue regeneration. Browse Assay Genie's current range of PLA2G2A research reagents below, or read on for the biology behind the target.
PLA2G2A is a secretory calcium-dependent phospholipase A2 that primarily acts on extracellular phospholipids. It hydrolyses the ester bond of the fatty acyl group at the sn-2 position, releasing free fatty acids and lysophospholipids, with a preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. Through this activity it contributes to lipid remodelling of cellular membranes and to the generation of lipid mediators involved in pathogen clearance. It also shows bactericidal activity against Gram-positive bacteria by directly hydrolysing phospholipids of the bacterial membrane.
During sterile inflammation, PLA2G2A targets the membrane phospholipids of extracellular mitochondria released from activated platelets. This generates unsaturated fatty acids such as arachidonate, which neighbouring leukocytes use to synthesise inflammatory eicosanoids including leukotrienes, while the loss of mitochondrial membrane integrity releases damage-associated molecular pattern molecules that activate innate immunity. In the intestinal crypt the protein acts as a stem cell regulator: inside the cell it supports Paneth cell differentiation by inhibiting Wnt signalling, whereas secreted into the lumen on inflammation it promotes prostaglandin E2 synthesis, which stimulates Wnt signalling and tissue regeneration. It may also contribute to the biosynthesis of N-acyl ethanolamines, which regulate energy metabolism and inflammation.
Independently of catalysis, PLA2G2A acts as an integrin ligand, binding and activating ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 at a site distinct from the classical ligand-binding site, and inducing integrin-dependent cell proliferation. The PLA2G2A gene belongs to the phospholipase A2 family, group II, and several alternatively spliced transcript variants with different 5' UTRs have been described. Its earlier HGNC name, phospholipase A2, group IIA (platelets, synovial fluid), reflects its original sources.
PLA2G2A hydrolyses bacterial membrane phospholipids and acts against Gram-positive bacteria, making it a focus for antimicrobial defence research.
By releasing arachidonate from phospholipids, PLA2G2A supplies substrate for leukotriene synthesis and helps trigger innate immune activation.
PLA2G2A regulates Wnt signalling, Paneth cell differentiation and prostaglandin E2 synthesis in the intestinal crypt and during tissue regeneration.
The enzyme remodels membrane lipids and may contribute to N-acyl ethanolamine biosynthesis, linking phospholipid turnover to energy metabolism.
PLA2G2A is a secreted calcium-dependent phospholipase A2 that cleaves the sn-2 fatty acyl bond of phospholipids. This supports lipid remodelling, bactericidal activity against Gram-positive bacteria, eicosanoid production in inflammation and intestinal tissue regeneration. It also binds and activates certain integrins independently of its catalytic activity.
The approved name is phospholipase A2 group IIA, and UniProt lists it as phospholipase A2, membrane associated. Aliases and previous symbols include PLA2B and PLA2L. An earlier HGNC name was phospholipase A2, group IIA (platelets, synovial fluid). Several transcript variants with different 5' UTRs have been reported.
Yes. Mouse and rat both have an ortholog named Pla2g2a. In humans the protein belongs to the phospholipase A2 family and to group II of the secreted enzymes. Check the datasheet of any product for its validated reactivity.
Other secreted and cytosolic phospholipase A2 family members and related phospholipase targets.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P14555; product specifications from Assay Genie datasheets.