Enhancement of lysophosphatidic acid-induced ERK phosphorylation by phospholipase D1 via the formation of phosphatidic acid

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dc.contributor.authorJang Hee Hong-
dc.contributor.authorSeo Ok Oh-
dc.contributor.authorMichael Lee-
dc.contributor.authorYoung Rok Kim-
dc.contributor.authorDong Uk Kim-
dc.contributor.authorGang Min Hur-
dc.contributor.authorJae Heun Lee-
dc.contributor.authorKyu Lim-
dc.contributor.authorByung Doo Hwang-
dc.contributor.authorSeung Kiel Park-
dc.date.accessioned2017-04-19T08:58:01Z-
dc.date.available2017-04-19T08:58:01Z-
dc.date.issued2001-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1006/bbrc.2001.4517ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5495-
dc.description.abstractWe made stable cell lines overexpressing PLD1 (GP-PLD1) from GP+envAm12 cell, a derivative of NIH 3T3 cell. PLD1 activity and extracellular signal-regulated kinase (ERK) phosphorylation were enhanced in GP-PLD1 cells by the treatment of lysophosphatidic acid (LPA). In contrast, these LPA-induced effects were attenuated with the pretreatment of pertussis toxin (PTX) or protein kinase C (PKC) inhibitor. Moreover, accumulation of phosphatidic acid (PA), a product of PLD action, potentiated the LPA-induced ERK activation in GP-PLD1 cells while blocking of PA production with the treatment of 1-butanol attenuated LPA-induced ERK phosphorylation. From these results, we suggest that LPA activate PLD1 through pertussis toxin-sensitive G protein and PKC-dependent pathways, then PA produced from PLD1 activation facilitate ERK phosphorylation.-
dc.publisherElsevier-
dc.titleEnhancement of lysophosphatidic acid-induced ERK phosphorylation by phospholipase D1 via the formation of phosphatidic acid-
dc.title.alternativeEnhancement of lysophosphatidic acid-induced ERK phosphorylation by phospholipase D1 via the formation of phosphatidic acid-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number5-
dc.citation.endPage1342-
dc.citation.startPage1337-
dc.citation.volume281-
dc.contributor.affiliatedAuthorMichael Lee-
dc.contributor.affiliatedAuthorDong Uk Kim-
dc.contributor.alternativeName홍장희-
dc.contributor.alternativeName오세옥-
dc.contributor.alternativeName이미가엘-
dc.contributor.alternativeName김영래-
dc.contributor.alternativeName김동욱-
dc.contributor.alternativeName허강민-
dc.contributor.alternativeName이재흔-
dc.contributor.alternativeName임규-
dc.contributor.alternativeName황병두-
dc.contributor.alternativeName박승길-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 281, no. 5, pp. 1337-1342-
dc.identifier.doi10.1006/bbrc.2001.4517-
dc.subject.keywordphospholipase D-
dc.subject.keywordmitogen activated protein kinase-
dc.subject.keywordphosphatidic acid-
dc.subject.keywordprotein kinase C-
dc.subject.keywordlysophosphatidic acid-
dc.subject.keywordGi protein-
dc.subject.localPhospholipase D-
dc.subject.localphospholipase D-
dc.subject.localmitogen activated protein kinase-
dc.subject.localmitogen-activated protein kinase-
dc.subject.localmitogen-activated protein kinases-
dc.subject.localMitogen activated protein kinase-
dc.subject.localMitogen-acti-vated protein kinase-
dc.subject.localMitogen-activated protein kinase-
dc.subject.localMitogen-activated protein kinase (MAPK)-
dc.subject.localMitogen-activated protein kinases-
dc.subject.localMitogen-activated protein kinases (MAPKs)-
dc.subject.localMitogen-activated protein (MAP) kinase-
dc.subject.localMitogenactivated protein kinase-
dc.subject.localphosphatidic acid-
dc.subject.localProtein kinase C-
dc.subject.localprotein kinase C-
dc.subject.localprotein kinase c-
dc.subject.locallysophosphatidic acid-
dc.subject.localLysophophatidic acid-
dc.subject.localLysophosphatidic acid-
dc.subject.localGi protein-
dc.description.journalClassY-
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Division of Biomedical Research > Rare Disease Research Center > 1. Journal Articles
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