Functional interactions of peroxisome proliferator-activated receptor, retinoid-X receptor, and Sp1 in the transcriptional regulation of the acyl-coenzyme-A oxidase promoter.

Détails

ID Serval
serval:BIB_3DE8F23CA361
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Functional interactions of peroxisome proliferator-activated receptor, retinoid-X receptor, and Sp1 in the transcriptional regulation of the acyl-coenzyme-A oxidase promoter.
Périodique
Molecular Endocrinology
Auteur⸱e⸱s
Krey G., Mahfoudi A., Wahli W.
ISSN
0888-8809[print], 0888-8809[linking]
Statut éditorial
Publié
Date de publication
02/1995
Volume
9
Numéro
2
Pages
219-231
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Peroxisome proliferator-activated receptor (PPARs) are members of the nuclear receptor superfamily. For transcriptional activation of their target genes, PPARs heterodimerize with the retinoid-X receptor (RXR). The convergence of the PPAR and RXR signaling pathways has been shown to have an important function in lipid metabolism. The promoter of the gene encoding the acyl-coenzyme-A oxidase (ACO), the rate-limiting enzyme in peroxisomal beta-oxidation of fatty acids, is a target site of PPAR action. In this study, we examined the role and the contribution of both cis-and trans-acting factors in the transcriptional regulation of this gene using transient transfections in insect cells. We identified several functional cis-acting elements present in the promoter of the ACO gene and established that PPAR-dependent as well as PPAR-independent mechanisms can activate the ACO promoter in these cells. We show that the PPAR/RXR heterodimer exerts its effect through two response elements within the ACO promoter, in synergy with the transcription factor Sp1 via five Sp1-binding sites. Furthermore, this functional interaction also occurs when Sp1 is co-expressed with PPAR or RXR alone, indicating that activation can occur independently of PPAR/RXR heterodimers.
Mots-clé
Acyl-CoA Oxidase, Animals, Base Sequence, Cell Line, Consensus Sequence, Drosophila, Gene Expression Regulation, Enzymologic, Genes, Reporter, Molecular Sequence Data, Mutagenesis, Site-Directed, Oxidoreductases/genetics, Oxidoreductases/metabolism, Precipitin Tests, Promoter Regions, Genetic, Receptors, Cytoplasmic and Nuclear/metabolism, Receptors, Retinoic Acid/metabolism, Regulatory Sequences, Nucleic Acid, Retinoid X Receptors, Sp1 Transcription Factor/metabolism, Transcription Factors/metabolism, Transfection
Pubmed
Web of science
Création de la notice
24/01/2008 16:04
Dernière modification de la notice
20/08/2019 13:34
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