Contribution of individual phospholipase A₂ enzymes to the cleavage of oxidized phospholipids in human blood plasma.

ABSTRACT: Phospholipids containing oxidized esterified PUFA residues (OxPLs) are increasingly recognized for multiple biological activities and causative involvement in disease pathogenesis. Pharmacokinetics of these compounds in blood plasma is essentially not studied. Human plasma contains both genuine phospholipases A₂ [platelet activating factor acetyl hydrolase (PAF-AH) (also called Lp-PLA₂) and secretory phospholipase A2] and multifunctional enzymes capable of removing sn-2 residues in native and oxidized PLs (lecithin-cholesterol acyltransferase, peroxiredoxin-6). The goal of this study was to compare relative activities of different PLA₂ enzymes by analyzing cleavage of oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-phosphatidylcholine (OxPAPC) and oxidized 1

SUBMITTER: Jokesch P 

PROVIDER: S-EPMC11841071 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature