PAFAH2 Human

The discovery of PAFAH2 is closely linked to the identification of PAF in the early 1970s. PAF was initially recognized as a phospholipid capable of inducing anaphylactic shock and activating platelets . Subsequent research revealed that PAF’s biological activity is highly dependent on the acetyl group at the sn-2 position, which is rapidly hydrolyzed by PAFAH2 . This hydrolysis results in the formation of lyso-PAF and acetate, effectively inactivating PAF and mitigating its proinflammatory effects .

PAFAH2 is a calcium-independent enzyme with a molecular weight of approximately 45 kDa . It circulates in plasma in an active form and is associated with lipoproteins . The enzyme’s activity is upregulated in response to inflammatory stimuli, suggesting its role as a physiological response to inflammation . PAFAH2’s ability to hydrolyze oxidized phospholipids further underscores its importance in managing oxidative stress and inflammation .

The clinical significance of PAFAH2 is evident in its association with various inflammatory conditions. Increased expression of PAFAH2 has been observed in atherosclerosis, where it is believed to play a protective role by reducing the levels of proinflammatory lipids . Conversely, genetic deficiencies in PAFAH2 have been linked to increased severity of atherosclerosis and other inflammatory syndromes . Recombinant forms of PAFAH2 have shown promise in experimental models for attenuating inflammation, highlighting its potential therapeutic applications .

Research on PAFAH2 continues to evolve, with ongoing studies exploring its structural features, regulatory mechanisms, and interactions with other biomolecules . Advances in understanding the interplay between PAFAH2, oxidized phospholipids, and lipoproteins could provide new insights into the enzyme’s role in inflammation and cardiovascular diseases .