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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Involvement of phospholipase D in sphingosine 1-phosphate-induced activation of phosphatidylinositol 3-kinase and Akt in Chinese hamster ovary cells overexpressing EDG3

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dc.contributor.author Banno, Y ko
dc.contributor.author Takuwa, Y ko
dc.contributor.author Akao, Y ko
dc.contributor.author Okamoto, H ko
dc.contributor.author Osawa, Y ko
dc.contributor.author Naganawa, T ko
dc.contributor.author Nakashima, S ko
dc.contributor.author Suh, Pann-Ghill ko
dc.contributor.author Nozawa, Y ko
dc.date.available 2014-09-04T00:41:22Z -
dc.date.created 2014-09-02 ko
dc.date.issued 2001-09 ko
dc.identifier.citation JOURNAL OF BIOLOGICAL CHEMISTRY, v.276, no.38, pp.35622 - 35628 ko
dc.identifier.issn 0021-9258 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/5692 -
dc.description.abstract Phospholipase D (PLD), phosphatidylinositol 3-kinase (PI3K), and Akt are known to be involved in cellular signaling related to proliferation and cell survival. In this report, we provide evidence that PLD links sphingosine 1-phosphate (S1P)-induced activation of the G protein-coupled EDG3 receptor to stimulation of PI3K and its downstream effector Akt in Chinese hamster ovary (CHO) cells. S1P stimulation of EDG3-overexpressing CHO cells but not vector-transfected cells induced activation of PLD, PI3K, and Akt in a time- and dose-dependent manner. Akt phosphorylation was prevented by the PI3K inhibitors wortmannin and LY294002 (2-(4-monrpholinyl)-8-phenyl-4H-1-benzopyran-4-one), indicating that Akt activation was dependent on PI3K. S1P-induced activation of PI3K and Akt was abrogated by 1-butanol, which inhibited S1P-induced accumulation of phosphatidic acid by serving as a phosphatidyl group acceptor in the transphosphatidylation reaction catalyzed by PLD, whereas both PI3K and Akt activation were not inhibited by 2-butanol without such reaction. Co-expression of wild-type PLD2 with myc-Akt resulted in increased Akt activation in response to S1P. In contrast, co-expression of a catalytically inactive mutant of PLD2 eliminated the S1P-induced Akt activation. The treatment of EDG3-expressing CHO cells with exogenous Streptomyces chromofuscus PLD, which caused an accumulation of phosphatidic acid, resulted in increases in PI3K activity and the phosphorylation of Akt, the latter of which was completely abolished by LY294002. Furthermore, S1P-induced membrane ruffling, which was dependent on PI3K and Rac, was inhibited by 1-butanol, but not by 2-butanol. These results demonstrate that PLD participates in the activation of PI3K and Akt stimulation of EDG3 receptor. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC ko
dc.title Involvement of phospholipase D in sphingosine 1-phosphate-induced activation of phosphatidylinositol 3-kinase and Akt in Chinese hamster ovary cells overexpressing EDG3 ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-0035929583 ko
dc.identifier.wosid 000171109300056 ko
dc.type.rims ART ko
dc.description.wostc 55 *
dc.description.scopustc 60 *
dc.date.tcdate 2015-05-06 *
dc.date.scptcdate 2014-09-02 *
dc.identifier.doi 10.1074/jbc.M105673200 ko
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035929583 ko
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