| Lysophosphatidic acids are new substrates for the phosphatase domain of soluble epoxide hydrolase. | |
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MedLine Citation:
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PMID: 22217705 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Soluble epoxide hydrolase (sEH) is a bi-functional enzyme which has a C-terminus epoxide hydrolase domain and N-terminus phosphatase domain. The endogenous substrates of epoxide hydrolase are known to be epoxyeicosatrienoic acids, but the endogenous substrates of the phosphatase activity are not well understood. In this study, to explore the substrates of sEH, we investigated the inhibition of the phosphatase activity of sEH towards a 4-methylumbelliferyl phosphate by using lecithin and its hydrolyzed products. Although lecithin itself did not inhibit the phosphatase activity, the hydrolyzed lecithin significantly inhibited it, suggesting that lysophospholipid and fatty acid can inhibit it. Next, we investigated the inhibition of phosphatase activity by lysophosphatidyl choline, palmitoyl lysophosphatidic acid, monopalmytoyl glycerol and palmitic acid. Palmitoyl lysophosphatidic acid and fatty acid efficiently inhibited it, suggesting that lysophosphatidic acids (LPAs) are substrates for the phosphatase activity of sEH. As expected, palmitoyl, stearoyl, oleoyl, and arachidonoyl LPAs were efficiently dephosphorylated by sEH (Km, 3-7 uM; Vmax, 150-193 nmol/min/mg). These results suggest that LPAs are substrates of sEH, which may regulate physiological functions of cells via their metabolism. |
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Authors:
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Ami Oguro; Susumu Imaoka |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-1-3 |
Journal Detail:
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Title: Journal of lipid research Volume: - ISSN: 0022-2275 ISO Abbreviation: - Publication Date: 2012 Jan |
Date Detail:
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Created Date: 2012-1-5 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0376606 Medline TA: J Lipid Res Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Bioscience, School of Science and Technology, Kwansei Gakuin University, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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