PLA2 (human, recombinant Group XV)

Phospholipase A2 (PLA2) (Group XV), also known as lysosomal phospholipase A and acetyltransferase, is a calcium-independent and acidic pH-optimum phospholipase encoded by PLA2G15 in humans. It is composed of an alpha/beta-hydrolase domain, a cap domain, and a membrane-binding domain, is ubiquitously expressed, and localizes to lysosomes. PLA2 (Group XV) hydrolyzes sn-1 and sn-2 fatty acids in phospholipids, contributing to phospholipid degradation in lysosomes. It also functions as a bis(monoacylglycerol) phosphate (BMP) hydrolase, hydrolyzing BMP lipid species independent of their saturation or chain length. Pla2g15 knockdown induces phospholipidosis and enlargement of alveolar macrophages, mimicking a foam cell phenotype, in young mice. In aged mice, Pla2g15 knockdown induces the development of glomerulonephritis, lymphoid hypertrophy, and abnormal serologies, including positive anti-nuclear antibodies, anti-dsDNA antibodies, and high circulating immunoglobulin levels, indicating an autoimmune phenotype similar to systemic lupus erythematosus (SLE). Similar to PLA2G15 knockout, pharmacologic inhibition of PLA2 (Group XV) by cationic amphiphilic drugs, such as amiodarone, induces phospholipidosis in cells, indicating that PLA2 (Group XV) may be a screening candidate for prediction of drug-induced phospholipidosis during pre-clinical drug development studies. Pla2g15 knockdown reduces Purkinje cell loss, microgliosis, astrocytosis, and CNS demyelination in a mouse model of Niemann-Pick disease type C1 (NPC1). Cayman's PLA2 (human, recombinant Group XV) can be used for enzyme activity assay and Western blot (WB) applications.