Secreted phospholipase A2 (sPLA2)

Secreted phospholipase A2 (sPLA2) refers to a family of low-molecular-weight, Ca2+-dependent enzymes that catalyze the hydrolysis of the sn-2 fatty acyl bond of membrane phospholipids, releasing free fatty acids (such as arachidonic acid) and lysophospholipids. These molecules act as precursors for numerous bioactive lipid mediators, including eicosanoids, which are key regulators of inflammation and immunity. sPLA2s are widely distributed in mammalian tissues and fluids as well as in venoms (snake, bee), and exhibit substrate specificity based on fatty acid and headgroup structure. They play major roles in physiological membrane remodeling, host antibacterial defense, and the pathogenesis of inflammatory, cardiovascular, and neurodegenerative diseases through lipid signaling cascades. Variants and isoforms exist across species and tissues. Owing to their central involvement in generating inflammatory signals, sPLA2 enzymes represent promising but challenging pharmacological targets for anti-inflammatory and cardio-protective drug development. Caveats: "Secreted phospholipase A2" refers to a broad enzyme family, with several isoforms (e.g., Group II, V, X) that may have distinct tissue expression and disease relevance. Precise disease and drug associations may be isoform-specific.

Other names

sPLA2Secretory phospholipase A2Group II phospholipase A2PLA2G (with group-specific gene symbols, e.g., PLA2G2A, PLA2G5, PLA2G10)

Inhibition of sPLA2 blocks hydrolysis of phospholipids, reducing arachidonic acid and lysophospholipid formation, and limits downstream production of pro-inflammatory lipid mediators (prostaglandins, leukotrienes, thromboxanes). Reduces inflammatory and atherogenic processes in tissues.