Linked Life Data

9756906

Source:http://linkedlifedata.com/resource/pubmed/id/9756906

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1998-11-2
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26652-61
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9756906-Base Sequence, pubmed-meshheading:9756906-Binding Sites, pubmed-meshheading:9756906-Cell Line, pubmed-meshheading:9756906-Cell Nucleus, pubmed-meshheading:9756906-Chloramphenicol O-Acetyltransferase, pubmed-meshheading:9756906-DNA Primers, pubmed-meshheading:9756906-Gene Expression Regulation, pubmed-meshheading:9756906-HeLa Cells, pubmed-meshheading:9756906-Humans, pubmed-meshheading:9756906-Nuclear Proteins, pubmed-meshheading:9756906-Pituitary Gland, pubmed-meshheading:9756906-Prolactin, pubmed-meshheading:9756906-Promoter Regions, Genetic, pubmed-meshheading:9756906-Protein Binding, pubmed-meshheading:9756906-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:9756906-Receptors, Estrogen, pubmed-meshheading:9756906-Receptors, Retinoic Acid, pubmed-meshheading:9756906-Retinoid X Receptors, pubmed-meshheading:9756906-Trans-Activators, pubmed-meshheading:9756906-Transcription Factors
pubmed:year
1998
pubmed:articleTitle
Activation of the prolactin gene by peroxisome proliferator-activated receptor-alpha appears to be DNA binding-independent.
pubmed:affiliation
Instituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas, 28029 Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't