| pubmed-article:15786731 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15786731 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:15786731 | lifeskim:mentions | umls-concept:C0031686 | lld:lifeskim |
| pubmed-article:15786731 | lifeskim:mentions | umls-concept:C1704708 | lld:lifeskim |
| pubmed-article:15786731 | lifeskim:mentions | umls-concept:C0255156 | lld:lifeskim |
| pubmed-article:15786731 | lifeskim:mentions | umls-concept:C1325331 | lld:lifeskim |
| pubmed-article:15786731 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:15786731 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:15786731 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:15786731 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:15786731 | pubmed:dateCreated | 2005-3-24 | lld:pubmed |
| pubmed-article:15786731 | pubmed:abstractText | The interleukin-6 (IL-6) stimulates growth in cells such as multiple myeloma and B-cell plasmacytomas/hybridomas, while it inhibits growth in several myeloid leukemia cells. The IL-6 receptor has subunit called gp130. It was reported that Ser-782 of gp130 is phosphorylated by unidentified kinase(s) in cell extracts, and level of gp130 (S782A) transiently expressed on the cell surface of COS-7 is 6-times higher than that of the wild type. These results motivated us to analyze whether the phosphorylation of gp130 at Ser-782 is involved in its degradation or not. In this study, we demonstrated here that treatment of HepG2 cells with okadaic acid (OA), a potent inhibitor for PP2A, promotes phosphorylation of gp 130 at Ser-782 and degradation of gp 130. MG115, a proteasome inhibitor, suppressed this degradation. These effects of OA could not be replaced with tautomycetin (TC), an inhibitor for PP1. Purified PP2A dephosphorylated phospho-Ser-782 of gp130 in vitro. IL-6-induced activation of Stat3 was suppressed by preincubation of the cells with OA, suggesting that the IL-6 signaling pathway was blocked by OA through degradation of gp 130. Taken together, present results strongly suggest that degradation of gp 130 is regulated through a phosphorylation-dephosphorylation mechanism in which PP2A is crucially involved and that gp 130 is a potential therapeutic target in cancers. | lld:pubmed |
| pubmed-article:15786731 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15786731 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15786731 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15786731 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:15786731 | pubmed:issn | 0300-8177 | lld:pubmed |
| pubmed-article:15786731 | pubmed:author | pubmed-author:UbukataMakoto... | lld:pubmed |
| pubmed-article:15786731 | pubmed:author | pubmed-author:ShimaHiroshiH | lld:pubmed |
| pubmed-article:15786731 | pubmed:author | pubmed-author:KikuchiKunimi... | lld:pubmed |
| pubmed-article:15786731 | pubmed:author | pubmed-author:MitsuhashiShi... | lld:pubmed |
| pubmed-article:15786731 | pubmed:author | pubmed-author:TanumaNobuhir... | lld:pubmed |
| pubmed-article:15786731 | pubmed:author | pubmed-author:OnoeKazunoriK | lld:pubmed |
| pubmed-article:15786731 | pubmed:author | pubmed-author:SasaSumieS | lld:pubmed |
| pubmed-article:15786731 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15786731 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:15786731 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15786731 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15786731 | pubmed:pagination | 183-7 | lld:pubmed |
| pubmed-article:15786731 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:15786731 | pubmed:meshHeading | pubmed-meshheading:15786731... | lld:pubmed |
| pubmed-article:15786731 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15786731 | pubmed:articleTitle | Protein phosphatase type 2A, PP2A, is involved in degradation of gp130. | lld:pubmed |
| pubmed-article:15786731 | pubmed:affiliation | Institute for Genetic Medicine, Hokkaido University, Kita-15, Nishi-7, Kita-ku, Sapporo, Japan. | lld:pubmed |
| pubmed-article:15786731 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15786731 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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