| pubmed-article:12900420 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12900420 | lifeskim:mentions | umls-concept:C0682538 | lld:lifeskim |
| pubmed-article:12900420 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:12900420 | lifeskim:mentions | umls-concept:C0007610 | lld:lifeskim |
| pubmed-article:12900420 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12900420 | lifeskim:mentions | umls-concept:C0017932 | lld:lifeskim |
| pubmed-article:12900420 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
| pubmed-article:12900420 | lifeskim:mentions | umls-concept:C0181586 | lld:lifeskim |
| pubmed-article:12900420 | lifeskim:mentions | umls-concept:C0301625 | lld:lifeskim |
| pubmed-article:12900420 | pubmed:issue | 42 | lld:pubmed |
| pubmed-article:12900420 | pubmed:dateCreated | 2003-10-13 | lld:pubmed |
| pubmed-article:12900420 | pubmed:abstractText | Glycogen synthase kinase-3beta (GSK-3beta) activity is suppressed when it becomes phosphorylated on serine 9 by protein kinase B (Akt). To determine how GSK-3beta activity opposes Akt function we used various methods to alleviate GSK-3beta suppression in prostate carcinoma cells. In some experiments, LY294002, a specific inhibitor of phosphatidylinositol 3-kinase (a kinase involved in activating Akt) and tumor necrosis factor-alpha (TNF-alpha) were used to activate GSK-3beta. In other experiments mutant forms of GSK-3beta, GSK-3betadelta9 (a constitutively active deletion mutant of GSK-3beta) and GSK-3betaY216F (an inactive point mutant of GSK-3beta) were used to alter GSK-3beta activity. LY294002, TNF-alpha, and overexpression of wild-type GSK-3beta or of GSK-3betadelta9, but not GSK-3betaY216F, alleviated the suppression of GSK-3beta activity in prostate carcinoma cells and enhanced the turnover of beta-catenin. Forced expression of wild-type GSK-3beta or of GSK-3betadelta9, but not GSK-3betaY216F, suppressed cell growth and showed that the phosphorylation status of GSK-3beta can affect its intracellular distribution. When transcription factors activator protein-1 and cyclic AMP-response element (CRE)-binding protein were analyzed as targets of GSK-3beta activity, overexpression of wild-type GSK-3beta suppressed AP1-mediated transcription and activated CRE-mediated transcription. Overexpression of GSK-3betadelta9 caused an (80-fold) increase in CRE-mediated transcription, which was further amplified (up to 130-fold) by combining GSK-3betadelta9 overexpression with the suppression of Jun activity. This study also demonstrated for the first time that expression of constitutively active GSK-3betadelta9 results in the phosphorylation of CRE-binding protein on serine 129 and enhancement of CRE-mediated transcription in intact cell nuclei. | lld:pubmed |
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| pubmed-article:12900420 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12900420 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12900420 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12900420 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12900420 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12900420 | pubmed:author | pubmed-author:DavisRoger... | lld:pubmed |
| pubmed-article:12900420 | pubmed:author | pubmed-author:KikuchiAkiraA | lld:pubmed |
| pubmed-article:12900420 | pubmed:author | pubmed-author:CliffordJohn... | lld:pubmed |
| pubmed-article:12900420 | pubmed:author | pubmed-author:LippmanScott... | lld:pubmed |
| pubmed-article:12900420 | pubmed:author | pubmed-author:MenterDavid... | lld:pubmed |
| pubmed-article:12900420 | pubmed:author | pubmed-author:SalasThomas... | lld:pubmed |
| pubmed-article:12900420 | pubmed:author | pubmed-author:ReddyShrikant... | lld:pubmed |
| pubmed-article:12900420 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12900420 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:12900420 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12900420 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12900420 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12900420 | pubmed:pagination | 41338-46 | lld:pubmed |
| pubmed-article:12900420 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:12900420 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12900420 | pubmed:articleTitle | Alleviating the suppression of glycogen synthase kinase-3beta by Akt leads to the phosphorylation of cAMP-response element-binding protein and its transactivation in intact cell nuclei. | lld:pubmed |
| pubmed-article:12900420 | pubmed:affiliation | Departments of Clinical Cancer Prevention and Gastrointestinal Medical Oncology, The University of Texas M D Anderson Cancer Center, Houston, Texas 77030, USA. | lld:pubmed |
| pubmed-article:12900420 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12900420 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12900420 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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