Intracellular PAF catabolism by PAF acetylhydrolase counteracts continual PAF synthesis
نویسندگان
چکیده
منابع مشابه
Intracellular PAF catabolism by PAF acetylhydrolase counteracts continual PAF synthesis.
Stimulated inflammatory cells synthesize platelet-activating factor (PAF), but lysates of these cells show little enhancement in PAF synthase activity. We show that human neutrophils contain intracellular plasma PAF acetylhydrolase (PLA2G7), an enzyme normally secreted by monocytes. The esterase inhibitors methyl arachidonoylfluorophosphonate (MAFP), its linoleoyl homolog, and Pefabloc inhibit ...
متن کاملPAF-acetylhydrolase expressed during megakaryocyte differentiation inactivates PAF-like lipids.
Platelet activating factor (PAF) and PAF-like lipids induce inflammatory responses in target cells. These lipid mediators are inactivated by PAF-acetylhydrolase (PAF-AH). The PAF signaling system affects the growth of hematopoietic CD34(+) cells, but roles for PAF-AH in this process are unknown. Here, we investigated PAF-AH function during megakaryopoiesis and found that human CD34(+) cells acc...
متن کاملDetermination of phospholipase activity of PAF acetylhydrolase.
This article presents a radiometric assay to determine the enzymatic activity of platelet-activating factor (PAF) acetylhydrolase (PAF-AH), also known as lipoprotein-associated phospholipase A2 and phospholipase A2 group 7A. The method is based on the release of radioactively labeled acetate from sn-2-labeled PAF and separation of substrate and product using reversed-phase column chromatography...
متن کاملThe emerging roles of PAF acetylhydrolase.
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 theref...
متن کاملCoupling PAF Signaling to Dynein Regulation Structure of LIS1 in Complex with PAF-Acetylhydrolase
Mutations in the LIS1 gene cause lissencephaly, a human neuronal migration disorder. LIS1 binds dynein and the dynein-associated proteins Nde1 (formerly known as NudE), Ndel1 (formerly known as NUDEL), and CLIP-170, as well as the catalytic alpha dimers of brain cytosolic platelet activating factor acetylhydrolase (PAF-AH). The mechanism coupling the two diverse regulatory pathways remains unkn...
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ژورنال
عنوان ژورنال: Journal of Lipid Research
سال: 2007
ISSN: 0022-2275
DOI: 10.1194/jlr.m700325-jlr200