Source:http://linkedlifedata.com/resource/pubmed/id/15936983
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-6-20
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pubmed:abstractText |
Peroxisome proliferator-activator receptors (PPAR) are involved in cholesterol homeostasis through the regulation of bile acids synthesis, composition, and reclamation. As ileal bile acid-binding protein (I-BABP) is thought to play a crucial role in the enterohepatic circulation of bile acids, we investigated whether I-BABP gene expression could also be affected by PPAR. Indeed, treatment with the PPARalpha-PPARbeta/delta agonist bezafibrate led to the up-regulation of I-BABP mRNA levels in the human intestine-derived Caco-2 cells. Cotransfections of the reporter-linked human I-BABP promoter (hI-BABP-2769/+44) together with PPAR and RXR expression vectors demonstrated that the fibrate-mediated induction of the I-BABP gene is dependent on PPARalpha or PPARbeta/delta. Using progressive 5' deletions of the hI-BABP promoter and sequence analysis, we identified a putative PPAR-binding site located at the position -198 and -186 upstream of the transcription initiation site. Electrophoretic mobility shift assays showed that the PPAR/RXR heterodimer can specifically bind to this PPRE-like motif. The deletion of the PPRE within the hI-BABP promoter abolished the PPAR-mediated transactivation in transient transfection assays. The regulation of the I-BABP promoter by PPAR appears species-specific, as the mouse I-BABP promoter, which lacks a conserved PPRE, was not responsive to exogenous PPAR expression in the presence of bezafibrate. Our findings show that the I-BABP gene may be a novel target for PPAR in humans and further emphasize the role for PPAR in the control of bile acid homeostasis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bezafibrate,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxisome Proliferator-Activated...,
http://linkedlifedata.com/resource/pubmed/chemical/bile acid binding proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
1735
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15936983-Animals,
pubmed-meshheading:15936983-Base Sequence,
pubmed-meshheading:15936983-Bezafibrate,
pubmed-meshheading:15936983-Binding Sites,
pubmed-meshheading:15936983-Caco-2 Cells,
pubmed-meshheading:15936983-Carrier Proteins,
pubmed-meshheading:15936983-Gene Expression Regulation,
pubmed-meshheading:15936983-Humans,
pubmed-meshheading:15936983-Ileum,
pubmed-meshheading:15936983-Membrane Glycoproteins,
pubmed-meshheading:15936983-Mice,
pubmed-meshheading:15936983-Molecular Sequence Data,
pubmed-meshheading:15936983-Peroxisome Proliferator-Activated Receptors,
pubmed-meshheading:15936983-Promoter Regions, Genetic,
pubmed-meshheading:15936983-Response Elements,
pubmed-meshheading:15936983-Species Specificity
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pubmed:year |
2005
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pubmed:articleTitle |
The gene encoding the human ileal bile acid-binding protein (I-BABP) is regulated by peroxisome proliferator-activated receptors.
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pubmed:affiliation |
Physiologie de la Nutrition, Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation, UMR 5170 CESG CNRS/INRA/Université de Bourgogne, 1 Esplanade Erasme F-21000, Dijon, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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