DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, CH | ko |
dc.contributor.author | Lee, CS | ko |
dc.contributor.author | Chang, MY | ko |
dc.contributor.author | Jang, IH | ko |
dc.contributor.author | Kim, SJ | ko |
dc.contributor.author | Hwang, IW | ko |
dc.contributor.author | Ryu, SH | ko |
dc.contributor.author | Lee, CO | ko |
dc.contributor.author | Koh, Gou Young | ko |
dc.date.accessioned | 2013-03-06T02:50:03Z | - |
dc.date.available | 2013-03-06T02:50:03Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2004-05 | - |
dc.identifier.citation | AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY, v.286, no.5, pp.H1881 - H1888 | - |
dc.identifier.issn | 0363-6135 | - |
dc.identifier.uri | http://hdl.handle.net/10203/85596 | - |
dc.description.abstract | To clarify the role of caveolae in VEGF/VEGF receptor-2 (VEGFR-2)-mediated signaling cascades, primary cultured human umbilical vein endothelial cells (HUVECs) were fractionated to isolate caveolae-enriched cell membranes. Interestingly, VEGFR-2, phospholipase D-2 (PLD2), and Ras were enriched in caveolae-enriched fractions. Moreover, VEGF increased PLD activity in a time- and dose-dependent manner in HUVECs, whereas a ligand specific for VEGFR-1 placental growth factor did not change PLD activity. A PLD inhibitor, 1-butanol, almost completely suppressed VEGF-induced ERK phosphorylation and cellular proliferation, whereas the negative control for 1-butanol, 3-butanol, did not produce significant changes. Addition of phosphatidic acid negated the 1-butanol-induced suppression. Pharmacological analyses using several inhibitors indicated that PKC-delta regulates the VEGF-induced activation of PLD/ERK. Thus PLD2 could be involved in MEK/ERK signaling cascades that are induced by the VEGF/VEGFR-2/PKC-delta pathway in endothelial cells. Pretreatment with the cholesterol depletion agent methyl-beta-cyclodextrin (MbetaCD) almost completely disassembled caveolar structures, whereas the addition of cholesterol to MbetaCD-treated cells restored caveolar structures. Pretreatment with MbetaCD largely abolished phosphorylation of MEK/ERK by VEGF, whereas the addition of cholesterol restored VEGF-induced MEK/ERK phosphorylations. These results indicate that intact caveolae are required for the VEGF/VEGFR-2-mediated MEK/ERK signaling cascade. | - |
dc.language | English | - |
dc.publisher | AMER PHYSIOLOGICAL SOC | - |
dc.subject | PROTEIN-KINASE-C | - |
dc.subject | SIGNAL-TRANSDUCTION PATHWAY | - |
dc.subject | CELL GROWTH-FACTOR | - |
dc.subject | PHOSPHOLIPASE-D | - |
dc.subject | PLASMA-MEMBRANE | - |
dc.subject | DNA-SYNTHESIS | - |
dc.subject | LIPID RAFTS | - |
dc.subject | ACTIVATION | - |
dc.subject | CHOLESTEROL | - |
dc.subject | TRANSPORT | - |
dc.title | Localization of VEGFR-2 and PLD2 in endothelial caveolae is involved in VEGF-induced phosphorylation of MEK and ERK | - |
dc.type | Article | - |
dc.identifier.wosid | 000220736500035 | - |
dc.identifier.scopusid | 2-s2.0-1942469316 | - |
dc.type.rims | ART | - |
dc.citation.volume | 286 | - |
dc.citation.issue | 5 | - |
dc.citation.beginningpage | H1881 | - |
dc.citation.endingpage | H1888 | - |
dc.citation.publicationname | AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY | - |
dc.identifier.doi | 10.1152/ajpheart.00786.2003 | - |
dc.contributor.localauthor | Koh, Gou Young | - |
dc.contributor.nonIdAuthor | Cho, CH | - |
dc.contributor.nonIdAuthor | Lee, CS | - |
dc.contributor.nonIdAuthor | Chang, MY | - |
dc.contributor.nonIdAuthor | Jang, IH | - |
dc.contributor.nonIdAuthor | Kim, SJ | - |
dc.contributor.nonIdAuthor | Hwang, IW | - |
dc.contributor.nonIdAuthor | Ryu, SH | - |
dc.contributor.nonIdAuthor | Lee, CO | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | caveolin-1 | - |
dc.subject.keywordAuthor | protein kinase C-delta | - |
dc.subject.keywordAuthor | signaling | - |
dc.subject.keywordAuthor | vascular endothelial growth factor | - |
dc.subject.keywordAuthor | phospholipase D | - |
dc.subject.keywordPlus | PROTEIN-KINASE-C | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION PATHWAY | - |
dc.subject.keywordPlus | CELL GROWTH-FACTOR | - |
dc.subject.keywordPlus | PHOSPHOLIPASE-D | - |
dc.subject.keywordPlus | PLASMA-MEMBRANE | - |
dc.subject.keywordPlus | DNA-SYNTHESIS | - |
dc.subject.keywordPlus | LIPID RAFTS | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | CHOLESTEROL | - |
dc.subject.keywordPlus | TRANSPORT | - |
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