| pubmed-article:9756906 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9756906 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:9756906 | lifeskim:mentions | umls-concept:C1418938 | lld:lifeskim |
| pubmed-article:9756906 | lifeskim:mentions | umls-concept:C1418776 | lld:lifeskim |
| pubmed-article:9756906 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9756906 | pubmed:issue | 41 | lld:pubmed |
| pubmed-article:9756906 | pubmed:dateCreated | 1998-11-2 | lld:pubmed |
| pubmed-article:9756906 | pubmed:abstractText | Although the effects of the peroxisome proliferator-activated receptors (PPARs) have been studied primarily in adipocytes and liver, the wide distribution of these receptors suggests that they might also play a role in other cell types. We present evidence that PPAR activators stimulate the expression of the prolactin gene in pituitary GH4C1 cells. Transfection assays in non-pituitary HeLa cells showed that stimulation of the prolactin promoter by PPARalpha requires the presence of the transcription factor GHF-1 (or Pit-1). Proximal promoter sequences confer responsiveness to PPARalpha, and activation by this receptor is lost concomitantly with the response to GHF-1. Surprisingly, expression of the retinoid X receptor (RXR) abolishes stimulation by PPARalpha. Furthermore, the promoter region that confers PPARalpha responsiveness does not contain a PPAR response element. This suggests that the transcriptional effect of PPARalpha might be mediated by protein-protein interactions rather than by binding of PPAR/RXR to the promoter. A direct interaction between PPARalpha and GHF-1 was confirmed by in vitro binding studies. Expression of the coactivators SRC-1 and CREB-binding protein, which bind to PPAR, also enhanced the responsiveness of the prolactin promoter to PPARalpha. Furthermore, CREB-binding protein also significantly increased activation by GHF-1, and both proteins associated in vitro. Thus, PPARalpha, a receptor that normally acts as a ligand-dependent transcription factor by binding to specific DNA sequences in one context, can also stimulate the prolactin promoter by association with GHF-1 and coactivator proteins. | lld:pubmed |
| pubmed-article:9756906 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9756906 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9756906 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9756906 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9756906 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9756906 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9756906 | pubmed:author | pubmed-author:ArandaAA | lld:pubmed |
| pubmed-article:9756906 | pubmed:author | pubmed-author:TolónR MRM | lld:pubmed |
| pubmed-article:9756906 | pubmed:author | pubmed-author:CastilloA IAI | lld:pubmed |
| pubmed-article:9756906 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9756906 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:9756906 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9756906 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9756906 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9756906 | pubmed:pagination | 26652-61 | lld:pubmed |
| pubmed-article:9756906 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:9756906 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9756906 | pubmed:articleTitle | Activation of the prolactin gene by peroxisome proliferator-activated receptor-alpha appears to be DNA binding-independent. | lld:pubmed |
| pubmed-article:9756906 | pubmed:affiliation | Instituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas, 28029 Madrid, Spain. | lld:pubmed |
| pubmed-article:9756906 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9756906 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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