PAFAH2

Official Full Name

platelet activating factor acetylhydrolase 2

Organism

Homo sapiens

GeneID

5051

Background

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]

Synonyms

HSD-PLA2;

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Detailed Information

PAF-AH2 and Oxidative Stress

Platelet-activating factor acetylhydrolase 2 (PAF-AH2) is a member of the cytosolic enzyme type II platelet-activating factor acetylhydrolase family (PAF-AH), which has a calculated molecular mass of 40 kDa and is distributed in both the cytosol and membranes of many kinds of cells. The platelet-activating factor-acetylhydrolase family consists of enzymes which catalyze the hydrolysis of acetyl ester at the sn-2 position of PAF (platelet-activating factor). Additionally, PAF-AH2 has been shown to play a role in inflammatory processes via hydrolysis of oxidized phospholipids and subsequent studies also successfully reproduced these observations. Oxidative stress has been reported as an underlying inflammatory factor in several disease pathologies (cancer, atherosclerosis, aging and various neurodegenerative disorders). Previous studies have shown that over-expression of PAF-AH2 can reduce oxidative stress-induced cell death and mediate oxidative stress-induced tissue damage repair. These evidences suggest that PAF-AH2 functions as an important, and perhaps primary, antioxidant enzyme in certain tissues.

As the member of the intracellular type II PAF-AH, the amino acid sequence of PAF-AH (II) does not show any similarity with any subunit of PAF-AH (I) but significant identity with plasma PAF-AH which exhibits a substrate specificity similar to plasma PAF-AH. In previous studies, although, there was no phenotypically indistinguishable between wild-type mice and Pafah2^-/- mice, mouse embryonic fibroblasts derived from Pafah2^-/- mice were more sensitive to tert-butylhydroperoxide treatment than those derived from wild-type mice. When Pafah2^-/- mice were injected with carbon tetrachloride (CCl₄), the mice showed a delay in hepatic injury recovery and an esterified form of 8-iso-PGF_2α (a known in vitro substrate of PAF-AH (II)). Based on these results, PAF-AH (II) is involved in the metabolism of esterified 8-isoprostaglandin F_2α and protects tissue from oxidative stress-induced injury.

Figure 1. PAF-AH2 protein (predicted Homo sapiens)

References:

Alexander Adibekian, Ku-Lung Hsu, Anna E Speers, Elizabeth S Monillas, Steven J Brown, Timothy Spicer, Virneliz Fernandez-Vega, Jill Ferguson, Brian J Bahnson, Benjamin F Cravatt, Peter Hodder and Hugh Rosen. (2013) 'Optimization and characterization of a triazole urea inhibitor for platelet-activating factor acetylhydrolase type 2 (PAFAH2)', Probe Structure & Characteristics.
Nozomu Kono, Takao Inoue, Yasukazu Yoshida, Hiroyuki Sato, Tomokazu Matsusue, Hiroyuki Itabe, Etsuo Niki, Junken Aoki and Hiroyuki Arai. (2008) 'Protection against Oxidative Stress-induced Hepatic Injury by Intracellular Type II Platelet-activating Factor Acetylhydrolase by Metabolism of Oxidized Phospholipids in Vivo', BIOLOGICAL CHEMISTRY, 283(3):1628-1636.
Calivarathan Latchoumycandane, Gopal K. Marathe, Renliang Zhang and Thomas M. McIntyre. (2012) 'Oxidatively Truncated Phospholipids Are Required Agents of Tumor Necrosis Factor α (TNFα)-induced Apoptosis', BIOLOGICAL CHEMISTRY, 287(21): 17693–17705.

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