DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, S | ko |
dc.contributor.author | Jung, Y | ko |
dc.contributor.author | Kim, D | ko |
dc.contributor.author | Koh, H | ko |
dc.contributor.author | Chung, Jongkyeong | ko |
dc.date.accessioned | 2013-02-28T02:01:23Z | - |
dc.date.available | 2013-02-28T02:01:23Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000-08 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.275, no.34, pp.25979 - 25984 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/72182 | - |
dc.description.abstract | We have studied a possible role of extracellular zinc ion in the activation of p70S6k, which plays an important role in the progression of cells from the G(1) to S phase of the cell cycle, Treatment of Swiss 3T3 cells with zinc sulfate led to the activation and phosphorylation of p70S6k in a dose-dependent manner, The activation of p70S6k by zinc treatment was biphasic, the early phase being at 30 min followed by the late phase at 120 min. The zinc-induced activation of p70S6k was partially inhibited by down-regulation of phorbol 12-myristate 13-acetate-responsive protein kinase C (PKC) by chronic treatment with phorbol 12-myristate 13-acetate, but this was not significant. Moreover, Go6976, a specific calcium-dependent PKC inhibitor, did not significantly inhibit the activation of p70S6k by zinc. These results demonstrate that the zinc-induced activation of p70S6k is not related to PKC, Also, extracellular calcium was not involved in the activation of p70S6k by zinc. Further characterization of the zinc-induced activation of p70S6k using specific inhibitors of the p70S6k signaling pathway, namely rapamycin, wortmannin, and LY294002, showed that zinc acted upstream of mTOR/FRAP/RAFT and phosphatidylinositol 3-kinase (PI3K), because these inhibitors caused the inhibition of zinc-induced p70S6k activity, In addition, Akt, the upstream component of p70S6k, was activated by zinc in a biphasic manner, as was p70S6k, Moreover, dominant interfering alleles of Akt and PDK1 blocked the zinc-induced activation of p70S6k, whereas the lipid kinase activity of PI3K was potently activated by zinc, Taken together, our data suggest that zinc activates p70S6k through the PI3K signaling pathway. | - |
dc.language | English | - |
dc.publisher | Amer Soc Biochemistry Molecular Biology Inc | - |
dc.subject | PROTEIN-KINASE | - |
dc.subject | MAMMALIAN PROTEIN | - |
dc.subject | EPITHELIAL-CELLS | - |
dc.subject | P70(S6K) | - |
dc.subject | INSULIN | - |
dc.subject | AKT | - |
dc.subject | MECHANISM | - |
dc.subject | STRESS | - |
dc.subject | TARGET | - |
dc.subject | PHOSPHORYLATION | - |
dc.title | Extracellular zinc activates p70 S6 kinase through the phosphatidylinositol 3-kinase signaling pathway | - |
dc.type | Article | - |
dc.identifier.wosid | 000088999700015 | - |
dc.identifier.scopusid | 2-s2.0-0034714258 | - |
dc.type.rims | ART | - |
dc.citation.volume | 275 | - |
dc.citation.issue | 34 | - |
dc.citation.beginningpage | 25979 | - |
dc.citation.endingpage | 25984 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.contributor.localauthor | Chung, Jongkyeong | - |
dc.contributor.nonIdAuthor | Kim, S | - |
dc.contributor.nonIdAuthor | Jung, Y | - |
dc.contributor.nonIdAuthor | Kim, D | - |
dc.contributor.nonIdAuthor | Koh, H | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | PROTEIN-KINASE | - |
dc.subject.keywordPlus | MAMMALIAN PROTEIN | - |
dc.subject.keywordPlus | EPITHELIAL-CELLS | - |
dc.subject.keywordPlus | P70(S6K) | - |
dc.subject.keywordPlus | INSULIN | - |
dc.subject.keywordPlus | AKT | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | STRESS | - |
dc.subject.keywordPlus | TARGET | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
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