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Article: Ginsenoside-Rg1 induces vascular endothelial growth factor expression through the glucocorticoid receptor-related phosphatidylinositol 3-kinase/Akt and β-catenin/T-cell factor-dependent pathway in human endothelial cells

TitleGinsenoside-Rg1 induces vascular endothelial growth factor expression through the glucocorticoid receptor-related phosphatidylinositol 3-kinase/Akt and β-catenin/T-cell factor-dependent pathway in human endothelial cells
Authors
Issue Date2006
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2006, v. 281 n. 47, p. 36280-36288 How to Cite?
AbstractGinsenoside-Rg1, the most prevalent active constituent of ginseng, is a potent proangiogenic factor of vascular endothelial cells. This suggests that Rg1 may be a new modality for angiotherapy. Rg1 can activate the glucocorticoid receptor (GR). However, the regulatory steps downstream from GR that promote Rg1-induced angiogenesis have not been elucidated. Here we showed for the first time that Rg1 was a potent stimulator of vascular endothelial growth factor (VEGF) expression in human umbilical vein endothelial cells, and importantly this induction was mediated through a phosphatidylinositol 3-kinase (PI3K)/ Akt and β-catenin/T-cell factor-dependent pathway via the GR. Rg1 stimulation resulted in an increase in the level of β-catenin, culminating its nuclear accumulation, and subsequent activation of VEGF expression. Transfection of a stable form of β-catenin (S37A) or the use of a glycogen synthase kinase 3β inhibitor to stabilize β-catenin induced VEGF synthesis, whereas small interfering RNA-mediated down-regulation of β-catenin did not, confirming that the effect was β-catenin-specific. Using a luciferase reporter gene assay, we observed that Rg1 increased T-cell factor/lymphoid enhancer factor transcriptional activity. These events were mediated via a PI3K-dependent phosphorylation of the inhibitory Ser9 residue of glycogen synthase kinase 3β. In addition, the GR antagonist RU486 was able to inhibit Rg1-induced PI3K/Akt and β-catenin activation. These findings provide new insights into the mechanism responsible for Rg1 functions. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in the U.S.A.
Persistent Identifierhttp://hdl.handle.net/10722/178976
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKar, WLen_US
dc.contributor.authorYuen, LPen_US
dc.contributor.authorWong, RNSen_US
dc.contributor.authorWong, ASTen_US
dc.date.accessioned2012-12-19T09:51:12Z-
dc.date.available2012-12-19T09:51:12Z-
dc.date.issued2006en_US
dc.identifier.citationJournal Of Biological Chemistry, 2006, v. 281 n. 47, p. 36280-36288en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/178976-
dc.description.abstractGinsenoside-Rg1, the most prevalent active constituent of ginseng, is a potent proangiogenic factor of vascular endothelial cells. This suggests that Rg1 may be a new modality for angiotherapy. Rg1 can activate the glucocorticoid receptor (GR). However, the regulatory steps downstream from GR that promote Rg1-induced angiogenesis have not been elucidated. Here we showed for the first time that Rg1 was a potent stimulator of vascular endothelial growth factor (VEGF) expression in human umbilical vein endothelial cells, and importantly this induction was mediated through a phosphatidylinositol 3-kinase (PI3K)/ Akt and β-catenin/T-cell factor-dependent pathway via the GR. Rg1 stimulation resulted in an increase in the level of β-catenin, culminating its nuclear accumulation, and subsequent activation of VEGF expression. Transfection of a stable form of β-catenin (S37A) or the use of a glycogen synthase kinase 3β inhibitor to stabilize β-catenin induced VEGF synthesis, whereas small interfering RNA-mediated down-regulation of β-catenin did not, confirming that the effect was β-catenin-specific. Using a luciferase reporter gene assay, we observed that Rg1 increased T-cell factor/lymphoid enhancer factor transcriptional activity. These events were mediated via a PI3K-dependent phosphorylation of the inhibitory Ser9 residue of glycogen synthase kinase 3β. In addition, the GR antagonist RU486 was able to inhibit Rg1-induced PI3K/Akt and β-catenin activation. These findings provide new insights into the mechanism responsible for Rg1 functions. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in the U.S.A.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.-
dc.subject.meshAnimalsen_US
dc.subject.meshCentral Nervous System Agents - Pharmacologyen_US
dc.subject.meshEndothelial Cells - Cytology - Metabolismen_US
dc.subject.meshEndothelium, Vascular - Cytologyen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshGinsenosides - Pharmacologyen_US
dc.subject.meshHumansen_US
dc.subject.meshPhosphatidylinositol 3-Kinases - Metabolismen_US
dc.subject.meshRna, Small Interfering - Metabolismen_US
dc.subject.meshReceptors, Glucocorticoid - Metabolismen_US
dc.subject.meshSignal Transductionen_US
dc.subject.meshSubcellular Fractions - Metabolismen_US
dc.subject.meshTcf Transcription Factors - Metabolismen_US
dc.subject.meshVascular Endothelial Growth Factor A - Biosynthesis - Metabolismen_US
dc.subject.meshBeta Catenin - Metabolismen_US
dc.titleGinsenoside-Rg1 induces vascular endothelial growth factor expression through the glucocorticoid receptor-related phosphatidylinositol 3-kinase/Akt and β-catenin/T-cell factor-dependent pathway in human endothelial cellsen_US
dc.typeArticleen_US
dc.identifier.emailWong, AST: awong1@hkucc.hku.hken_US
dc.identifier.authorityWong, AST=rp00805en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.M606698200en_US
dc.identifier.pmid17008323-
dc.identifier.scopuseid_2-s2.0-33846013596en_US
dc.identifier.hkuros124971-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33846013596&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume281en_US
dc.identifier.issue47en_US
dc.identifier.spage36280en_US
dc.identifier.epage36288en_US
dc.identifier.isiWOS:000242100500080-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridKar, WL=15757444900en_US
dc.identifier.scopusauthoridYuen, LP=15081685200en_US
dc.identifier.scopusauthoridWong, RNS=7402126957en_US
dc.identifier.scopusauthoridWong, AST=23987963300en_US

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