Abstract
Platelet-activating factor (PAF), a phospholipid autacoid with potent effects throughout the innate immune system, is selectively degraded by two small families of PAF acetylhydrolases (PAF-AHs). These Ca2+-independent phospholipases A2 display remarkable specificity for the length of the sn-2 residue, but this selectivity is lost as the residue gains oxygen functions. Two of the PAF-AHs therefore are specific oxidized phospholipid phospholipases that reduce inflammation, but also remove oxidatively truncated phospholipids that induce apoptosis. The roles of these enzymes are manifold, and their separate and combined functions are now being addressed in model systems and clinical studies.
Highlights
Platelet-activating factor (PAF), a phospholipid autacoid with potent effects throughout the innate immune system, is selectively degraded by two small families of PAF acetylhydrolases (PAF-AHs)
Group VII enzymes are known by their common names plasma PAF-AH (PLA2G7, referred to as lipoprotein-associated phospholipase A2, LpPLA2) and the liver type II PAF-AH (PAFAH2)
Sequence analyses of PLA2G7 and PAFAH2 reveal that these genes have a higher degree of homology to neutral lipases and esterases than to other members of the phospholipase A2 superfamily [4]
Summary
Department of Cell Biology,* Lerner Research Institute, Cleveland Clinic College of Medicine of Case Western Reserve University, Cleveland, OH 44195; Oklahoma Medical Research Foundation,† Oklahoma City, OK 73104; and Huntsman Cancer Institute and Department of Internal Medicine,§ University of Utah, Salt Lake City, UT 84112
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