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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2009-9-29
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pubmed:abstractText |
In situ estrogen production by aromatase conversion from androgens plays an important role in breast tumor promotion. Here, we show that 17beta-estradiol (E2) can rapidly enhance aromatase enzymatic activity through an increase of aromatase protein phosphorylation in breast cancer cell lines. In vivo labeling experiments and site-directed mutagenesis studies demonstrated that phosphorylation of the 361-tyrosine residue is crucial in the up-regulation of aromatase activity under E2 exposure. Our results demonstrated a direct involvement of nonreceptor tyrosine-kinase c-Src in E2-stimulated aromatase activity because inhibition of its signaling abrogated the up-regulatory effects induced by E2 on aromatase activity as well as phosphorylation of aromatase protein. In addition, from our data it emerges that aromatase is a target of cross talk between growth factor receptors and estrogen receptor alpha signaling. These findings show, for the first time, that tyrosine phosphorylation processes play a key role in the rapid changes induced by E2 in aromatase enzymatic activity, revealing the existence of a short nongenomic autocrine loop between E2 and aromatase in breast cancer cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aromatase,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogen Receptor alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/estrogen receptor alpha, human,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1944-9917
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1634-45
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pubmed:dateRevised |
2011-4-21
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pubmed:meshHeading |
pubmed-meshheading:19556341-Amino Acid Sequence,
pubmed-meshheading:19556341-Aromatase,
pubmed-meshheading:19556341-Breast Neoplasms,
pubmed-meshheading:19556341-Cell Line, Tumor,
pubmed-meshheading:19556341-Enzyme Activation,
pubmed-meshheading:19556341-Estradiol,
pubmed-meshheading:19556341-Estrogen Receptor alpha,
pubmed-meshheading:19556341-Female,
pubmed-meshheading:19556341-Humans,
pubmed-meshheading:19556341-Models, Biological,
pubmed-meshheading:19556341-Molecular Sequence Data,
pubmed-meshheading:19556341-Multiprotein Complexes,
pubmed-meshheading:19556341-Phosphorylation,
pubmed-meshheading:19556341-Phosphotyrosine,
pubmed-meshheading:19556341-Protein Binding,
pubmed-meshheading:19556341-Receptor, Epidermal Growth Factor,
pubmed-meshheading:19556341-Receptors, Growth Factor,
pubmed-meshheading:19556341-Signal Transduction,
pubmed-meshheading:19556341-src-Family Kinases
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pubmed:year |
2009
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pubmed:articleTitle |
Rapid estradiol/ERalpha signaling enhances aromatase enzymatic activity in breast cancer cells.
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pubmed:affiliation |
Department of Pharmaco-Biology, University of Calabria, Arcavacata di Rende (CS) 87030, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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