pubmed-article:14529564 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C1512505 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C0034804 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C0288472 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C1512474 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C0249197 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C1420626 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
pubmed-article:14529564 | lifeskim:mentions | umls-concept:C2266853 | lld:lifeskim |
pubmed-article:14529564 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:14529564 | pubmed:dateCreated | 2003-10-7 | lld:pubmed |
pubmed-article:14529564 | pubmed:abstractText | We analysed the antiproliferative activity of various histone deacetylase (HDAC) inhibitors such as trichostatin A (TSA) on human breast cancer cells. We observed a lower sensitivity to HDAC inhibition for oestrogen receptor negative (ER-) versus positive (ER+) cell lines. This differential response was associated neither with a modification of drug efflux via the multidrug resistance system nor with a global modification of histone acetyltransferase (HAT)/HDAC activities. In contrast, we demonstrated that in ER+ breast cancer cells the p21(WAF1/CIP1) gene was more sensitive to TSA regulation and was expressed at higher levels. These differences were observed both in transient transfection experiments and on the endogenous p21(WAF1/CIP1) gene. The Sp1 transcription factor, which was shown to interact in vitro with both class I and class II HDACs, is sufficient to confer the differential sensitivity to TSA and participated in the control of p21(WAF1/CIP1) basal expression. Finally, re-expression of ERalpha following adenoviral infection of ER- breast cancer cells increased both p21(WAF1/CIP1) protein accumulation and the growth inhibitory activity of TSA. Altogether, our results highlight the key role of ERalpha and p21(WAF1/CIP1) gene expression in the sensitivity of breast cancer cells to hyperacetylating agents. | lld:pubmed |
pubmed-article:14529564 | pubmed:language | eng | lld:pubmed |
pubmed-article:14529564 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14529564 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:14529564 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14529564 | pubmed:month | Oct | lld:pubmed |
pubmed-article:14529564 | pubmed:issn | 0022-0795 | lld:pubmed |
pubmed-article:14529564 | pubmed:author | pubmed-author:VignonFF | lld:pubmed |
pubmed-article:14529564 | pubmed:author | pubmed-author:CavaillèsVV | lld:pubmed |
pubmed-article:14529564 | pubmed:author | pubmed-author:LazennecGG | lld:pubmed |
pubmed-article:14529564 | pubmed:author | pubmed-author:MargueronRR | lld:pubmed |
pubmed-article:14529564 | pubmed:author | pubmed-author:LicznarAA | lld:pubmed |
pubmed-article:14529564 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14529564 | pubmed:volume | 179 | lld:pubmed |
pubmed-article:14529564 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14529564 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14529564 | pubmed:pagination | 41-53 | lld:pubmed |
pubmed-article:14529564 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:14529564 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14529564 | pubmed:articleTitle | Oestrogen receptor alpha increases p21(WAF1/CIP1) gene expression and the antiproliferative activity of histone deacetylase inhibitors in human breast cancer cells. | lld:pubmed |
pubmed-article:14529564 | pubmed:affiliation | INSERM U540, Endocrinologie Moléculaire et Cellulaire des Cancers and Université de Montpellier I, 60, rue de Navacelles, 34090 Montpellier, France. | lld:pubmed |
pubmed-article:14529564 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14529564 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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