Lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress response (  , ). At the lipid-aqueous interface, hydrolyzes the ester bond of fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (, ). Specifically targets phospholipids with a short-chain fatty acyl group at sn-2 position . Can hydrolyze phospholipids with long fatty acyl chains, only if they carry oxidized functional groups (, ). Hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), a potent pro-inflammatory signaling lipid that acts through PTAFR on various innate immune cells (    ). Hydrolyzes oxidatively truncated phospholipids carrying an aldehyde group at omega position, preventing their accumulation in low-density lipoprotein (LDL) particles and uncontrolled pro-inflammatory effects (, ). As part of high-density lipoprotein (HDL) particles, can hydrolyze phospholipids having long-chain fatty acyl hydroperoxides at sn-2 position and protect against potential accumulation of these oxylipins in the vascular wall . Catalyzes the release from membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular oxidative damage .
Subcellular locations: Secreted, Extracellular space
Associates with both LDL and HDL particles in plasma ( , ). Mainly associates with pro-inflammatory electronegative LDL particles .
Plasma (, ). Secreted by macrophages (at protein level) .