| pubmed-article:11108261 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11108261 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:11108261 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
| pubmed-article:11108261 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:11108261 | lifeskim:mentions | umls-concept:C0021665 | lld:lifeskim |
| pubmed-article:11108261 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:11108261 | lifeskim:mentions | umls-concept:C0720298 | lld:lifeskim |
| pubmed-article:11108261 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:11108261 | pubmed:dateCreated | 2000-12-6 | lld:pubmed |
| pubmed-article:11108261 | pubmed:abstractText | This study examines whether the serine/threonine protein kinase, Akt, is involved in the cross-talk between epidermal growth factor (EGF) and insulin-related growth factor I (IGF-I) receptors and ER-alpha. Treatment of MCF-7 cells with either EGF or IGF-I resulted in a rapid phosphorylation of Akt and a 14- to 16-fold increase in Akt activity, respectively. Akt activation was blocked by inhibitors of phosphatidylinositol 3-kinase, but not by an inhibitor of the ribosomal protein kinase p70S6K. Stable transfection of cells with a dominant negative Akt mutant blocked the effects of EGF and IGF-I on ER-alpha expression and activity, whereas stable transfection of cells with a constitutively active Akt mutant mimicked the effects of EGF and IGF-I. In the latter cells, there was a decrease in the amount of ER-alpha protein and messenger RNA (70-80%) and an increase in the amount of progesterone receptor protein, messenger RNA (4- to 9- and by 3.5- to 7-fold, respectively) and pS2 (3- to 5-fold). Coexpression of wild-type ER-alpha and the dominant negative Akt mutant in COS-1 cells also blocked the growth factor-stimulated activation of ER-alpha, but coexpression of the wild-type receptor with the constitutively active Akt mutant increased ER-alpha activity. Receptor activation was blocked by an antiestrogen. Studies using mutants of ER-alpha demonstrated that Akt increased estrogen receptor activity through the amino-terminal activation function-1 (AF-1). Serines S104 S106, S118, and S167 appear to play a role in the activation of ER-alpha by Akt. | lld:pubmed |
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| pubmed-article:11108261 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11108261 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:11108261 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11108261 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11108261 | pubmed:issn | 0013-7227 | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:ChambonPP | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:Katzenellenbo... | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:StoicaAA | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:FrankeT FTF | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:MartinM BMB | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:StoicaB ABA | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:StoicaG EGE | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:McLemoreM SMS | lld:pubmed |
| pubmed-article:11108261 | pubmed:author | pubmed-author:OlivoS ESE | lld:pubmed |
| pubmed-article:11108261 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11108261 | pubmed:volume | 141 | lld:pubmed |
| pubmed-article:11108261 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11108261 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11108261 | pubmed:pagination | 4503-11 | lld:pubmed |
| pubmed-article:11108261 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:11108261 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11108261 | pubmed:articleTitle | A role for Akt in mediating the estrogenic functions of epidermal growth factor and insulin-like growth factor I. | lld:pubmed |
| pubmed-article:11108261 | pubmed:affiliation | Department of Oncology, Lombardi Cancer Center, Georgetown University, Washington, DC 20007, USA. | lld:pubmed |
| pubmed-article:11108261 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11108261 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11108261 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11108261 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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