Phospholipase A2 group X (sPLA2-X) (sPLA2-X)

Phospholipase A2 group X (sPLA2-X), encoded by the PLA2G10 gene, is a highly potent calcium-dependent enzyme belonging to the secretory phospholipase A2 family [2, 5]. It catalyzes the hydrolysis of the sn-2 ester bond of glycerophospholipids, showing a strong preference for phosphatidylcholine, to produce free fatty acids and lysophospholipids [9, 11]. sPLA2-X is notable for its high catalytic efficiency and its unique ability to directly hydrolyze the plasma membranes of mammalian cells and lipoproteins without requiring prior cellular activation [11, 17]. This enzymatic activity leads to the release of arachidonic acid and the subsequent generation of pro-inflammatory eicosanoids, which are central to the pathogenesis of asthma, atherosclerosis, and various cancers [1, 13, 15]. In addition to its pro-inflammatory roles, sPLA2-X has been shown to mobilize omega-3 polyunsaturated fatty acids that can exert protective, anti-inflammatory effects in the context of colitis [3, 4]. In oncology, the enzyme is frequently overexpressed and promotes tumor cell survival, proliferation, and immune evasion [5, 17]. Therapeutic development has primarily focused on small-molecule inhibitors that target the catalytic site to treat inflammatory and malignant conditions, although achieving isoform selectivity and maintaining its protective physiological functions remain significant challenges [8, 19, 22].

Other names

PLA2G10Group 10 secretory phospholipase A2GX sPLA2GXSPLA2Phosphatidylcholine 2-acylhydrolase 10sPLA2-X

Inhibition of enzymatic activity by binding to the catalytic site, thereby preventing the hydrolysis of phospholipids and the release of pro-inflammatory precursors like arachidonic acid [7, 8, 19].