Platelet-activating factor acetylhydrolase 2 (PAFAH2)

Platelet-activating factor acetylhydrolase 2 (PAFAH2) is a single-subunit intracellular enzyme classified within the phospholipase A2 (PLA2) family that hydrolyzes the sn-2 acetyl group of platelet-activating factor (PAF) and oxidatively modified phospholipids, inactivating these potent pro-inflammatory mediators. Unlike most PLA2s, PAFAH2 does not require calcium for activity and demonstrates broad substrate specificity, targeting a variety of short-chain sn-2 acyl groups. PAFAH2 is particularly important under oxidative stress, where it translocates from the cytosol to membranes to degrade oxidized phospholipids, thereby protecting cells, including neurons and keratinocytes, from lipid peroxidation and apoptosis. Variants of this enzyme—including serum and other cytoplasmic isoforms—are implicated in diverse pathological processes, including cardiovascular and neurodegenerative diseases[1][3][5][7].

Other names

Platelet-activating factor acetylhydrolase 2, cytoplasmicPlatelet-activating factor acetylhydrolase 2, 40kDaPAFAH-IIHSD-PLA2PAF:lysophospholipid transacetylasePAF:sphingosine transacetylasePlatelet-activating factor acetyltransferase PAFAH2Serine-dependent phospholipase A2

Inhibition or modulation of PAFAH2 reduces inactivation of platelet-activating factor and other pro-inflammatory lipids, potentially altering inflammatory and oxidative stress responses.