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Platelet-activating factor acetylhydrolase 2, 40kDa

platelet-activating factor acetylhydrolase II, HSD-PLA2
This gene encodes platelet-activating factor acetylhydrolase isoform 2, a single-subunit intracellular enzyme that catalyzes the removal of the acetyl group at the SN-2 position of platelet-activating factor (identified as 1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine). However, this lipase exhibits a broader substrate specificity than simply platelet activating factor. Two other isoforms of intracellular platelet-activating factor acetylhydrolase exist, and both are multi-subunit enzymes. Additionally, there is a single-subunit serum isoform of this enzyme. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PAF, ACID, 1-Alkyl-2-acetylglycerophosphocholine Esterase, Inactive, fibrillin-1
Papers on platelet-activating factor acetylhydrolase II
Lipoprotein-associated phospholipase A2 concentrations in plasma are associated with the extent of coronary artery disease and correlate to adipose tissue levels of marine n-3 fatty acids.
Christensen et al., Aalborg, Denmark. In Atherosclerosis, 2008
Lp-PLA2 was higher in those with more extensive Coronary artery disease
Neuroprotective role of transgenic PAF-acetylhydrolase II in mouse models of focal cerebral ischemia.
Hiraga et al., Toyama, Japan. In Stroke, 2007
PAF-AH II exerts strong neuroprotective effects against ischemic injury: the neurological deficit scores, cerebral edema index, and relative infarction volume are all significantly lower in PAFAH2 transgenic mice than in wild-type mice.
Identification of platelet-activating factor acetylhydrolase II in human skin.
Travers et al., Indianapolis, United States. In J Invest Dermatol, 2002
presence of platelet-activating factor acetylhydrolase II in a restricted pattern in human skin; it is involved in protecting this organ against oxidative stress through the degradation of oxidatively modified bioactive phospholipids.
Platelet-activating factor acetylhydrolases: broad substrate specificity and lipoprotein binding does not modulate the catalytic properties of the plasma enzyme.
Gelb et al., Seattle, United States. In Biochemistry, 2001
examines substrate specificity for intracellular and plasma PAF-AHs
Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor.
Tew et al., Harlow, United Kingdom. In Biochem J, 1998
Using expressed sequence tag (EST) homology screening, a new human serine dependent phospholipase A2 (HSD-PLA2) was identified that has 40% amino acid identity with human low density lipoprotein-associated phospholipase A2 (LDL-PLA2).
Purification and characterization of platelet-activating factor acetylhydrolase II from bovine liver cytosol.
Inoue et al., Tokyo, Japan. In J Biol Chem, 1995
Platelet-activating factor (PAF) acetylhydrolase, which inactivates PAF by removing the acetyl group at the sn-2 position, is distributed widely in plasma and tissues.
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