scholarly journals Oligomeric state regulated trafficking of human platelet-activating factor acetylhydrolase type-II

2015 ◽  
Vol 1854 (5) ◽  
pp. 469-475 ◽  
Author(s):  
Elizabeth S. Monillas ◽  
Jeffrey L. Caplan ◽  
Anastasia F. Thévenin ◽  
Brian J. Bahnson
Keyword(s):  
Human Platelet ◽  
Platelet Activating Factor ◽  
Type Ii ◽  
Oligomeric State ◽  
Platelet Activating Factor Acetylhydrolase ◽  
Regulated Trafficking

scholarly journals Trafficking of Platelet-Activating Factor Acetylhydrolase Type II in Response to Oxidative Stress

Biochemistry ◽  
2011 ◽  
Vol 50 (39) ◽  
pp. 8417-8426 ◽  
Author(s):  
Anastasia F. Thévenin ◽  
Elizabeth S. Monillas ◽  
Jason M. Winget ◽  
Kirk Czymmek ◽  
Brian J. Bahnson
Keyword(s):  
Oxidative Stress ◽  
Platelet Activating Factor ◽  
Type Ii ◽  
Platelet Activating Factor Acetylhydrolase

scholarly journals Protection against Oxidative Stress-induced Hepatic Injury by Intracellular Type II Platelet-activating Factor Acetylhydrolase by Metabolism of Oxidized Phospholipids in Vivo

2007 ◽  
Vol 283 (3) ◽  
pp. 1628-1636 ◽  
Author(s):  
Nozomu Kono ◽  
Takao Inoue ◽  
Yasukazu Yoshida ◽  
Hiroyuki Sato ◽  
Tomokazu Matsusue ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hepatic Injury ◽  
Platelet Activating Factor ◽  
Type Ii ◽  
Oxidized Phospholipids ◽  
Wild Type ◽  
Membrane Phospholipids ◽  
Platelet Activating Factor Acetylhydrolase

Membrane phospholipids are susceptible to oxidation, which is involved in various pathological processes such as inflammation, atherogenesis, neurodegeneration, and aging. One enzyme that may help to remove oxidized phospholipids from cells is intracellular type II platelet-activating factor acetylhydrolase (PAF-AH (II)), which hydrolyzes oxidatively fragmented fatty acyl chains attached to phospholipids. Overexpression of PAF-AH (II) in cells or tissues was previously shown to suppress oxidative stress-induced cell death. In this study we investigated the functions of PAF-AH (II) by generating PAF-AH (II)-deficient (Pafah2-/-) mice. PAF-AH (II) was predominantly expressed in epithelial cells such as kidney proximal and distal tubules, intestinal column epithelium, and hepatocytes. Although PAF-AH activity was almost abolished in the liver and kidney of Pafah2-/- mice, Pafah2-/- mice developed normally and were phenotypically indistinguishable from wild-type mice. However, mouse embryonic fibroblasts derived from Pafah2-/- mice were more sensitive to tert-butylhydroperoxide treatment than those derived from wild-type mice. When carbon tetrachloride (CCl4) was injected into mice, Pafah2-/- mice showed a delay in hepatic injury recovery. Moreover, after CCl4 administration, liver levels of the esterified form of 8-iso-PGF2α, a known in vitro substrate of PAF-AH (II), were higher in Pafah2-/- mice than in wild-type mice. These results indicate that PAF-AH (II) is involved in the metabolism of esterified 8-isoprostaglandin F2α and protects tissue from oxidative stress-induced injury.

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