Regulation of glycogen synthase kinase-3 by thymosin beta-4 is associated with gastric cancer cell migration

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dc.contributor.authorY K Ryu-
dc.contributor.authorY S Lee-
dc.contributor.authorG H Lee-
dc.contributor.authorK S Song-
dc.contributor.authorYong Sung Kim-
dc.contributor.authorE Y Moon-
dc.date.accessioned2017-04-19T09:33:28Z-
dc.date.available2017-04-19T09:33:28Z-
dc.date.issued2012-
dc.identifier.issn00207136-
dc.identifier.uri10.1002/ijc.27490ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10908-
dc.description.abstractThymosin beta-4 (Tβ4), actin-sequestering protein, plays important roles in many cellular functions including cancer cell migrations. Glycogen synthase kinase (GSK) in Wnt signaling pathway is a key molecule to control intercellular interaction. Here, we investigated whether GSK-3 activity is regulated by Tβ4 and it is associated with Tβ4-mediated migration in gastric cancer cells. Various expression level of Tβ4 was observed in human gastric tumor tissues. Migration in gastric cancer cells, SNU638 and SNU668, was dependent on a relative expression level of Tβ4. Cell migration was higher in SNU668 with a higher expression level of Tβ4 than that in SNU638 with a lower Tβ4. Although the level of phosphorylated(p)-GSK-3α (inactive), β-catenin, E-cadherin and E-cadherin:β-catenin complex was relatively higher, p-GSK-3β (inactive) was lower in SNU638 compared to those in SNU668 cells. LiCl, GSK-3α/β inhibitor, reduced lung metastasis of B16F10 mouse melanoma cells and SNU668 cell migration. Small interference (si)RNA of GSK-3α increased SNU638 cell migration in accordance with the reduction of E-cadherin:β-catenin complex formation through a decrease in β-catenin and E-cadherin. Expression level of GSK-3α/β, β-catenin and E-cadherin in SNU668 and SNU638 was reversed by Tβ4-siRNA and by the treatment with acetylated-serine-aspartic acid-lysine-proline (SDKP) tetrapeptide of Tβ4, respectively. E-cadherin expression in SNU638 cells was decreased by β-catenin-siRNA. PD98059, MEK inhibitor, or U0126, ERK inhibitor, reduced SNU668 cell migration accompanying an increase in p-GSK-3α, β-catenin and E-cadherin. Taken together, data indicated that the expression of GSK-3α, β-catenin and E-cadherin could be negatively regulated by Tβ4-induced ERK phosphorylation. It suggests that Tβ4 could be a novel regulator to control Wnt signaling pathways.-
dc.publisherWiley-
dc.titleRegulation of glycogen synthase kinase-3 by thymosin beta-4 is associated with gastric cancer cell migration-
dc.title.alternativeRegulation of glycogen synthase kinase-3 by thymosin beta-4 is associated with gastric cancer cell migration-
dc.typeArticle-
dc.citation.titleInternational Journal of Cancer-
dc.citation.number9-
dc.citation.endPage2077-
dc.citation.startPage2067-
dc.citation.volume131-
dc.contributor.affiliatedAuthorYong Sung Kim-
dc.contributor.alternativeName류연경-
dc.contributor.alternativeName이유선-
dc.contributor.alternativeName이근희-
dc.contributor.alternativeName송규상-
dc.contributor.alternativeName김용성-
dc.contributor.alternativeName문은이-
dc.identifier.bibliographicCitationInternational Journal of Cancer, vol. 131, no. 9, pp. 2067-2077-
dc.identifier.doi10.1002/ijc.27490-
dc.subject.keywordβ-catenin-
dc.subject.keywordcell migration-
dc.subject.keywordE-cadherin-
dc.subject.keywordERK-
dc.subject.keywordgastric cancer cell-
dc.subject.keywordGSK-3-
dc.subject.keywordSNU638-
dc.subject.keywordSNU668-
dc.subject.keywordthymosin beta-4-
dc.subject.keywordWnt-
dc.subject.localβ-catenin-
dc.subject.localcell migration-
dc.subject.localCell migration-
dc.subject.localE-cadherin-
dc.subject.localERK-
dc.subject.localgastric cancer cell-
dc.subject.localGSK-3-
dc.subject.localSNU638-
dc.subject.localSNU668-
dc.subject.localthymosin beta-4-
dc.subject.localThymosin β4-
dc.subject.localWnt-
dc.subject.localWNT-
dc.description.journalClassY-
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Division of Biomedical Research > Genome Editing Research Center > 1. Journal Articles
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