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Phospholipase A2 (PLA2) refers to a superfamily of enzymes that hydrolyze the ester bond at the sn-2 position of phospholipids, releasing a free fatty acid and a lysophospholipid. This reaction is crucial in lipid metabolism and cell signaling, particularly in generating arachidonic acid for eicosanoid biosynthesis, which plays key roles in inflammation and other physiological processes. The PLA2 superfamily is diverse, comprising at least six major families based on structure, location, substrate specificity, and physiological role, including secreted PLA2 (sPLA2), cytosolic PLA2 (cPLA2), Ca²⁺-independent PLA2 (iPLA2), lipoprotein-associated PLA2 (LpPLA2), lysosomal PLA2 (LPLA2), and adipose-tissue-specific PLA2 (AdPLA). Elevated levels or altered activities serve as biomarkers or therapeutic targets for several conditions, and inhibitors targeting specific groups/isoforms are under investigation for anti-inflammatory therapies.
Inhibition of phospholipase A2 activity, blocking the release of arachidonic acid and subsequent production of inflammatory mediators.
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