Description
Lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress response (PubMed: 7700381, PubMed: 8624782, PubMed: 2040620, PubMed: 16371369, PubMed: 17090529, PubMed: 10066756). At the lipid-aqueous interface, hydrolyzes the ester bond of fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed: 2040620, PubMed: 10504265). Specifically targets phospholipids with a short-chain fatty acyl group at sn-2 position (PubMed: 2040620). Can hydrolyze phospholipids with long fatty acyl chains, only if they carry oxidized functional groups (PubMed: 2040620, PubMed: 8624782). Hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), a potent proinflammatory signaling lipid that acts through PTAFR on various innate immune cells (PubMed: 10504265, PubMed: 10066756, PubMed: 7592717, PubMed: 11590221, PubMed: 7700381, PubMed: 18434304, PubMed: 16371369, PubMed: 8675689, PubMed: 8624782). Hydrolyzes oxidatively truncated phospholipids carrying an aldehyde group at omega position, preventing their accumulation in low-density lipoprotein (LDL) particles and uncontrolled proinflammatory effects (PubMed: 2040620, PubMed: 7700381). 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 (PubMed: 17090529). Catalyzes the release from membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular oxidative damage (PubMed: 16371369)