Xenopus peroxisome proliferator activated receptors: Genomic organization, response element recognition, heterodimer formation with retinoid X receptor and activation by fatty acids

 Xenopus peroxisome proliferator activated receptors: Genomic organization, response element recognition, heterodimer formation with retinoid X receptor and activation by fatty acids},
  author={Grigorios D. Krey and Hansj{\"o}rg Keller and Abderrahim Mahfoudi and Jeffrey A. Medin and Keiko Ozato and Christine Dreyer and Walter Wahli},
  journal={The Journal of Steroid Biochemistry and Molecular Biology},
  • G. Krey, H. Keller, +4 authors W. Wahli
  • Published 1993
  • Medicine, Biology
  • The Journal of Steroid Biochemistry and Molecular Biology
Peroxisome proliferator activated receptors are ligand activated transcription factors belonging to the nuclear hormone receptor superfamily. Three cDNAs encoding such receptors have been isolated from Xenopus laevis (xPPAR alpha, beta, and gamma). Furthermore, the gene coding for xPPAR beta has been cloned, thus being the first member of this subfamily whose genomic organization has been solved. Functionally, xPPAR alpha as well as its mouse and rat homologs are thought to play an important… Expand
Peroxisome Proliferator-activated Receptor Mediates Cross-talk with Thyroid Hormone Receptor by Competition for Retinoid X Receptor
It is demonstrated that PPAR selectively inhibits the transcriptional activity of TRs by competition for RXR and possibly non-RXR TR-auxiliary proteins, independent of the formation of PPAR:TR heterodimers or competition for DNA binding. Expand
Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression.
It is suggested that PPARs are key messengers responsible for the translation of nutritional and pharmacological stimuli into changes in gene expression and differentiation pathways. Expand
Polarity and Specific Sequence Requirements of Peroxisome Proliferator-activated Receptor (PPAR)/Retinoid X Receptor Heterodimer Binding to DNA
It is demonstrated that only MEp and not MEd is able to bind PPAR/retinoid X receptor (RXR) heterodimers and mediate peroxisome proliferator signaling. Expand
Peroxisome proliferator-activated receptors: insight into multiple cellular functions.
The different structural domains of PPARs are presented in terms of activation mechanisms, namely ligand binding, phosphorylation, and cofactor interaction, and the specificity of ligands is described for each of the three PPAR isotypes. Expand
International Union of Pharmacology. LXI. Peroxisome Proliferator-Activated Receptors
The three peroxisome proliferator-activated receptors (PPARs) are ligand-activated transcription factors of the nuclear hormone receptor superfamily. They share a high degree of structural homologyExpand
DNA Binding Properties of Peroxisome Proliferator-activated Receptor Subtypes on Various Natural Peroxisome Proliferator Response Elements
The three subtypes of the peroxisome proliferator-activated receptors (PPARα, β/δ, and γ) form heterodimers with the 9-cis-retinoic acid receptor (RXR) and bind to a common consensus responseExpand
The Insulin-like Growth Factor-binding Protein 1 Gene Is a Primary Target of Peroxisome Proliferator-activated Receptors*
It is demonstrated, in human hepatocellular carcinoma cells and in normal mouse liver, that IGFBP-1 mRNA expression is under the primary control of PPAR ligands. Expand
Fibrates increase human REV-ERBalpha expression in liver via a novel peroxisome proliferator-activated receptor response element.
It is demonstrated that fibrates induce the expression of the nuclear receptor Rev-erbalpha, a negative regulator of gene transcription, and a subset of DR2 sites are identified as novel PPARalpha response elements. Expand
Structural requirements and cell-type specificity for ligand activation of peroxisome proliferator-activated receptors
Findings identify certain structural features in PPAR-activating agents that modulate PPAR activation, and suggest that as with other nuclear receptors, activation is cell-type specific. Expand
A natural polymorphism in peroxisome proliferator-activated receptor-alpha hinge region attenuates transcription due to defective release of nuclear receptor corepressor from chromatin.
The data suggest that the PPARalpha/NCoR interaction is physiologically relevant and can produce a discernable phenotype when the magnitude of the interaction is altered by a naturally occurring variation. Expand


Positive regulation of the peroxisomal β‐oxidation pathway by fatty acids through activation of peroxisome proliferator‐activated receptors (PPAR)
The data suggest that PPARs have an important role in lipid metabolism, and that 5,8,11,14‐eicosatetraynoic acid, which is the alkyne homolog of arachidonic acid, is the most potent activator of xPPARα described to date. Expand
Interaction of the peroxisome-proliferator-activated receptor and retinoid X receptor.
The results raise the possibility of convergence of the PPAR and retinoid-dependent signaling pathways on promoters containing PPRE-like responsive elements. Expand
The mouse peroxisome proliferator activated receptor recognizes a response element in the 5′ flanking sequence of the rat acyl CoA oxidase gene.
An element located 570 bp upstream of the ACO gene that confers responsiveness to the hypolipidaemic peroxisome proliferator Wy‐14,643 contains a direct repeat of the sequence motifs TGACCT and TGTCCT and binds PPAR, indicating an important role of PPAR in mediating the action of peroxISome proliferators including the induction of ACO. Expand
Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors
Three novel members of the Xenopus nuclear hormone receptor superfamily have been cloned and their multiplicity suggests the existence of hitherto unknown cellular signaling pathways for xenobiotics and putative endogenous ligands. Expand
The peroxisome proliferator-activated receptor mediates the induction of CYP4A6, a cytochrome P450 fatty acid omega-hydroxylase, by clofibric acid.
Gene transfer experiments indicate that induction by the peroxisome proliferators, clofibric acid and WY-14,643, of luciferase expression driven by the promoter and 5'-flanking sequences of theExpand
Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors
The coupling of the peroxisome proliferator and retinoid signalling pathways is demonstrated and evidence for a physiological role for 9-cis retinoic acid in modulating lipid metabolism is provided. Expand
Identification of a peroxisome proliferator-responsive element upstream of the gene encoding rat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase.
  • B. Zhang, S. Marcus, +5 authors J. Capone
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1992
Gel retardation analysis with nuclear extracts demonstrated that ciprofibrate-treated or untreated H4IIEC3 cells, but not HeLa cells or monkey kidney cells, contained sequence-specific DNA binding factors that interact with the PPRE, which has implications for understanding the mechanisms of coordinated transcriptional induction of genes encoding peroxisomal proteins by hypolipidemic agents and otherPeroxisome proliferators. Expand
Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acids.
A novel member of the steroid hormone receptor superfamily is identified by cDNA cloning from a human osteosarcoma SAOS-2/B10 cell library and Amino acid sequence alignment and transcriptional activation experiments revealed that the new protein is closely related to the mouse peroxisome proliferator activated receptor. Expand
Genomic organization of the retinoic acid receptor gamma gene.
In comparison with the steroid receptor subfamily, various splice sites of RAR gamma occur at altered positions, suggesting that the RAR subfamily has diverged early during evolution. Expand
Two cis-acting regulatory sequences in the peroxisome proliferator-responsive enhancer region of rat acyl-CoA oxidase gene.
The mechanism of transcriptional induction of the rat liver acyl-CoA oxidase gene by hypolipidemic agents is clarified, and it is found that the sequence between -639 and -472 acts as a peroxisome proliferator-responsive, tissue-specific enhancer. Expand