PLA2G2E Protein, Mouse (HEK293, His)

PLA2G2E, a secretory calcium-dependent phospholipase A2, predominantly targets extracellular phospholipids and exhibits phospholipase A2 activity by hydrolyzing the ester bond of the fatty acyl group at the sn-2 position of phospholipids. This enzymatic action results in the release of various unsaturated fatty acids, including oleoate, linoleoate, arachidonate, docosahexaenoate, and lysophosphatidylethanolamines, with a preference for lysophosphatidylethanolamines over lysophosphatidylcholines. In response to a high-fat diet, PLA2G2E hydrolyzes minor lipoprotein phospholipids, such as phosphatidylserines, phosphatidylinositols, and phosphatidylglycerols, thereby influencing lipoprotein composition and fat storage in adipose tissue and liver. Operating in an autocrine and paracrine manner, PLA2G2E contributes to lipid remodeling in cellular membranes and the generation of lipid mediators vital for pathogen clearance. Additionally, it acts as a hair follicle phospholipase A2, selectively releasing lysophosphatidylethanolamines and various unsaturated fatty acids in the skin to regulate hair follicle homeostasis. Furthermore, PLA2G2E may play a role in regulating the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes. Upon allergen exposure, it potentially participates in the allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells.