Search results for "Retinoid X Receptors"

showing 10 items of 13 documents

9-cis-Retinoic acid enhances fatty acid-induced expression of the liver fatty acid-binding protein gene

1997

The role of retinoic acids (RA) on liver fatty acid- binding protein (L-FABP) expression was investigated in the well differentiated FAO rat hepatoma cell line. 9-cis-Retinoic acid (9-ci's-RA) specifically enhanced L-FABP mRNA levels in a time- and dose-dependent manner. The higher induction was found 6 h after addition of 10 -6 M 9-CK-RA in the medium. RA also enhanced further both L-FABP mRNA levels and cytosolic L-FABP protein content induced by oleic acid. The retinoid X receptor (RXR) and the peroxisome proliferator-activated receptor (PPAR), which are known to be activated, respectively, by 9-c/s-RA and long chain fatty acid (LCFA), co-operated to bind specifically the peroxisome prol…

9-cw-Retinoic acidReceptors Retinoic Acid[SDV]Life Sciences [q-bio]Receptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorMyelin P2 ProteinMicrobodiesBiochemistry0302 clinical medicineStructural BiologyTumor Cells CulturedAlitretinoinchemistry.chemical_classification0303 health sciencesChemistryFatty AcidsDrug SynergismPeroxisomeNeoplasm Proteins9-cis-Retinoic acidLiverBiochemistryFree fatty acid receptorlipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaLong chain fatty acidFatty Acid-Binding Protein 7DimerizationPeroxisome proliferator-activated receptor gammaCarcinoma HepatocellularBiophysicsNerve Tissue ProteinsTretinoinRetinoid X receptorFatty Acid-Binding ProteinsLiver fatty acid-binding protein03 medical and health sciencesGeneticsAnimalsRNA MessengerMolecular Biology030304 developmental biologyFAO hepatoma cellFatty acidCell BiologyFatty acidRatsRetinoid X ReceptorsGene Expression RegulationNuclear receptorGene expressionCarrier Proteins[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryTranscription FactorsFEBS Letters
researchProduct

Nuclear receptors modulate the interaction of Sp1 and GC-rich DNA via ternary complex formation

2000

Binding sites for transcription factor Sp1have been implicated in the transcriptional regulation of several genes by hormones or vitamins, and here we show that a GC-rich element contributes to the retinoic acid response of the interleukin 1β promoter. To explain such observations, it has been proposed that nuclear receptors can interact with Sp1 bound to GC-rich DNA. However, evidence supporting this model has remained indirect. So far, nuclear receptors have not been detected in a complex with Sp1 and GC-rich DNA, and the expected ternary complexes in non-denaturing gels were not seen. In search for these missing links we found that nuclear receptors [retinoic acid receptor (RAR), thyroid…

Cell ExtractsTranscriptional ActivationReceptors Retinoic AcidSp1 Transcription FactorRecombinant Fusion ProteinsReceptors Cytoplasmic and NuclearTretinoinRetinoic acid receptor betaBiologyRetinoid X receptorLigandsResponse ElementsTransfectionModels BiologicalBiochemistryAntibodiesCell LineSubstrate SpecificityAnimalsPromoter Regions GeneticMolecular BiologyNuclear receptor co-repressor 1Nuclear receptor co-repressor 2Binding SitesReceptors Thyroid HormoneDNACell BiologyRetinoic acid receptor gammaRetinoid X receptor gammaGC Rich SequenceProtein Structure TertiaryNuclear receptor coactivator 1Retinoic acid receptorDrosophila melanogasterEcdysteroneRetinoid X ReceptorsOligodeoxyribonucleotidesBiochemistryReceptors CalcitriolThermodynamicsResearch ArticleInterleukin-1Protein BindingTranscription FactorsBiochemical Journal
researchProduct

Retinoid X receptor and retinoic acid response in the marine sponge Suberites domuncula

2003

SUMMARY To date no nuclear receptors have been identified or cloned from the phylogenetically oldest metazoan phylum, the Porifera (sponges). We show that retinoic acid causes tissue regression in intact individuals of the demosponge Suberites domuncula and in primmorphs, special three-dimensional cell aggregates. Primmorphs were cultivated on a galectin/poly-L-lysine matrix in order to induce canal formation. In the presence of 1 or 50 μmol l–1 retinoic acid these canals undergo regression, a process that is reversible. We also cloned the cDNA from S. domunculaencoding the retinoid X receptor (RXR), which displays the two motifs of nuclear hormone receptors, the ligand-binding and the DNA-…

DNA ComplementaryRetinoid X receptor; Suberites domuncula; marine spongesCroatiaReceptors Retinoic AcidPhysiologyMolecular Sequence DataRetinoic acidGene ExpressionApoptosisEnzyme-Linked Immunosorbent AssayTretinoinRetinoic acid receptor betaAquatic ScienceRetinoic acid-inducible orphan G protein-coupled receptorchemistry.chemical_compoundAnimalsCluster AnalysisAmino Acid SequenceMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsbiologySequence Analysis DNARetinoic acid receptor gammaBlotting Northernbiology.organism_classificationRetinoid X receptor gammaPoriferaCell biologySuberites domunculaRetinoic acid receptorRetinoid X ReceptorschemistryBiochemistryRetinoic acid receptor alphaInsect ScienceAnimal Science and ZoologySequence AlignmentTranscription FactorsJournal of Experimental Biology
researchProduct

Function of RAR? and RAR?2 at the initiation of retinoid signaling is essential for avian embryo survival and for distinct events in cardiac morphoge…

2003

Avian embryogenesis requires retinoid receptor activation by the vitamin A active form, retinoic acid (RA), during neurulation. We conducted loss-of-function analysis in quail embryos by nutritional deprivation of RA and by blocking generation of retinoid receptors. Here we identify a distinct role for RARα2 in cardiac inflow tract morphogenesis and for RARγ in cardiac left/right orientation and looping morphogenesis. Blocking normal embryos with antisense oligonucleotides to RARα2 or RXRα diminishes GATA-4 transcripts, while blocking RARγ or RXRα diminishes nodal and Pitx2 transcripts; the expression of these genes in the heart forming region resembles that of the vitamin A-deficient embry…

Embryo NonmammalianTime Factorsanimal structuresCell SurvivalReceptors Retinoic Acidmedicine.drug_classMorphogenesisRetinoic acidRetinoid receptorCoturnixBiologyRetinoidschemistry.chemical_compoundmedicineAnimalsRNA MessengerRetinoidIn Situ HybridizationHomeodomain ProteinsGeneticsRetinoid X receptor alphaPITX2MyocardiumRetinoic Acid Receptor alphaGene Expression Regulation DevelopmentalOligonucleotides AntisenseGATA4 Transcription FactorCell biologyDNA-Binding ProteinsPhenotypeRetinoid X ReceptorschemistrySignal transductionNODALSignal TransductionTranscription FactorsDevelopmental BiologyDevelopmental Dynamics
researchProduct

Induction of the fatty acid transport protein 1 and acyl-CoA synthase genes by dimer-selective rexinoids suggests that the peroxisome proliferator-ac…

2000

The intracellular fatty acid content of insulin-sensitive target tissues determines in part their insulin sensitivity. Uptake of fatty acids into cells is a controlled process determined in part by a regulated import/export system that is controlled at least by two key groups of proteins, i.e. the fatty acid transport protein (FATP) and acyl-CoA synthetase (ACS), which facilitate, respectively, the transport of fatty acids across the cell membrane and catalyze their esterification to prevent their efflux. Previously it was shown that the expression of the FATP-1 and ACS genes was controlled by insulin and by peroxisome proliferator-activated receptor (PPAR) agonists in liver or in adipose t…

MalePeroxisome proliferator-activated receptor gammaTime FactorsReceptors Retinoic AcidRetinoic acidReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorTretinoinRetinoid X receptorBiologyFatty Acid-Binding ProteinsBiochemistryMicechemistry.chemical_compoundCoenzyme A LigasesTumor Cells CulturedAnimalsHumansTissue DistributionMolecular BiologyNucleic Acid Synthesis InhibitorsCell Nucleuschemistry.chemical_classificationDose-Response Relationship DrugFatty AcidsMembrane ProteinsFatty acidMembrane Transport ProteinsSerum Albumin Bovine3T3 CellsCell BiologyFatty Acid Transport ProteinsRatsRats ZuckerRetinoic acid receptorRetinoid X ReceptorschemistryBiochemistryDactinomycinFree fatty acid receptorRNAPeroxisome proliferator-activated receptor alphaCaco-2 CellsCarrier ProteinsTranscription Factors
researchProduct

Thyroid hormone induction of the adrenoleukodystrophy-related gene (ABCD2).

2003

X-linked adrenoleukodystrophy (X-ALD) is a demyelinating disorder associated with impaired very-long-chain fatty-acid (VLCFA) beta-oxidation caused by mutations in the ABCD1 (ALD) gene that encodes a peroxisomal membrane ABC transporter. ABCD2 (ALDR) displays partial functional redundancy because when overexpressed, it is able to correct the X-ALD biochemical phenotype. The ABCD2 promoter contains a putative thyroid hormone-response element conserved in rodents and humans. In this report, we demonstrate that the element is capable of binding retinoid X receptor and 3,5,3'-tri-iodothyronine (T3) receptor (TRbeta) as a heterodimer and mediating T3 responsiveness of ABCD2 in its promoter conte…

MaleThyroid HormonesReceptors Retinoic AcidGene ExpressionATP-binding cassette transporterRetinoid X receptorRats Sprague-DawleyMiceABCD3Gene expressionABCD2medicineAnimalsHumansReceptorAdrenoleukodystrophyPromoter Regions GeneticGeneCells CulturedRepetitive Sequences Nucleic AcidPharmacologyChemokine CCL22Mice KnockoutReceptors Thyroid Hormonebiologymedicine.diseaseCell biologyRatsUp-RegulationOligodendrogliaRetinoid X ReceptorsLiverAstrocytesChemokines CCbiology.proteinCancer researchMolecular MedicineTriiodothyronineAdrenoleukodystrophyChemokine CCL17Transcription FactorsMolecular pharmacology
researchProduct

Glucocorticoids as modulators of expression and activity of Antithrombin (At): potential clinical relevance.

2014

Abstract Introduction An inverse relationship has been reported between decreased postoperative Antithrombin (AT) plasmatic levels and the incidence of complications. We hypothesized that Nuclear Hormone Receptors could modulate the expression of SERPINC1 , encoding AT, through a Hormone Regulatory Element present in its promoter, and thus hormone analogs could be a pharmacological complement in surgical procedures to activate endogenous AT synthesis. Materials and Methods The expression of SERPINC1 was analyzed in HepG2 cells by quantitative RT-PCR and Western Blot. Two studies were conducted with (a) patients submitted to cardiac surgery with cardiopulmonary bypass receiving (n =17) or no…

Malemedicine.medical_specialtyMolecular Sequence DataReceptors Cytoplasmic and NuclearRetinoid X receptorLigandsAntithrombinsCohort StudiesRetinoidsInternal medicinemedicineHumansGlucocorticoidsDexamethasoneAgedCardiopulmonary BypassBase Sequencebusiness.industryAntithrombinRNA-Binding ProteinsHematologyHep G2 CellsIsoxazolesMiddle AgedEndocrinologyRetinoid X ReceptorsTreatment OutcomeMethylprednisoloneNuclear receptorHemostasisFemaleCortisonebusinessHormonemedicine.drugThrombosis research
researchProduct

Up‐regulation of the α‐secretase ADAM10 by retinoic acid receptors and acitretin

2009

Late-onset Alzheimer's disease is often connected with nutritional misbalance, such as enhanced cholesterol intake, deficiency in polyunsaturated fatty acids, or hypovitaminosis. The alpha-secretase ADAM10 has been found to be regulated by retinoic acid, the bioreactive metabolite of vitamin A. Here we show that retinoids induce gene expression of ADAM10 and alpha-secretase activity by nonpermissive retinoid acid receptor/retinoid X receptor (RAR/RXR) heterodimers, whereby alpha- and beta-isotypes of RAR play a major role. However, ligands of other RXR binding partners, such as the vitamin D receptor, do not stimulate alpha-secretase activity. On the basis of these findings, we examined the…

Malemedicine.medical_specialtyReceptors Retinoic AcidReceptors Cytoplasmic and NuclearMice TransgenicTretinoinRetinoic acid receptor betaRetinoid X receptorBiologyBiochemistryCell LineAcitretinADAM10 ProteinAmyloid beta-Protein PrecursorMiceKeratolytic AgentsAlzheimer DiseaseInternal medicineGeneticsmedicineAnimalsHumansPromoter Regions GeneticMolecular BiologyLiver X ReceptorsReceptors Thyroid HormoneMolecular StructureRetinoid X receptor alphaMembrane ProteinsOrphan Nuclear ReceptorsRetinoid X receptor gammaAcitretinUp-RegulationDNA-Binding ProteinsPPAR gammaADAM ProteinsRetinoic acid receptorRetinoid X ReceptorsEndocrinologyGene Expression RegulationRetinoic acid receptor alphaReceptors CalcitriolAmyloid Precursor Protein SecretasesRetinoid X receptor betaBiotechnologymedicine.drugThe FASEB Journal
researchProduct

The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two re…

1995

AbstractPeroxisome proliferators (PPs) are non-genotoxic carcinogens in rodents. They can induce the expression of numerous genes via the heterodimerization of two members of the steroid hormone receptor superfamily, called the peroxisome proliferator-activated receptor (PPAR) and the 9-cis retinoic acid receptor (RXR). Many of the PP responsive genes possess a peroxisome proliferator response element (PPRE) formed by two TGACCT-related motifs. The bifunctional enzyme (HD) PPRE contains 3 such motifs, creating DR1 and DR2 sequences. PPAR and RXR regulate transcription via the DR1 element while DR2 modulates the expression of the gene via auxiliary factors in HepG2 cells.

Peroxisome proliferator-activated receptor gammaReceptors Retinoic AcidSteroid hormone receptorMolecular Sequence DataResponse elementBiophysicsReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorchemical and pharmacologic phenomenaIn Vitro TechniquesRegulatory Sequences Nucleic AcidRetinoid X receptorBiologyPeroxisomal Bifunctional EnzymeTransfectionMicrobodiesBiochemistryGene Expression Regulation EnzymologicTranscriptional activationPeroxisomal Bifunctional EnzymeMultienzyme ComplexesStructural BiologyPeroxisome proliferator response element9-cis Retinoic acid receptor alphaTumor Cells CulturedGeneticsHumansRNA MessengerIsomerasesEnoyl-CoA HydrataseMolecular Biologychemistry.chemical_classificationBinding SitesBase Sequence3-Hydroxyacyl CoA DehydrogenasesPeroxisome proliferator-activated receptorCell BiologyDNA-Binding ProteinsRetinoic acid receptorRetinoid X ReceptorsLiverOligodeoxyribonucleotidesBiochemistrychemistryRat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseEnzyme InductionPeroxisome proliferator-activated receptor alphaTranscription FactorsFEBS Letters
researchProduct

Co-regulator recruitment and the mechanism of retinoic acid receptor synergy.

2002

Crystal structure and co-regulator interaction studies have led to a general mechanistic view of the initial steps of nuclear receptor (NR) action. Agonist-induced transconformation of the ligand-binding domain (holo-LBD) leads to the formation of co-activator complexes, and destabilizes the co-repressor complexes bound to the ligand-free (apo) LBD. However, the molecular basis of retinoid-X receptor (RXR) 'subordination' in heterodimers, an essential mechanism to avoid signalling pathway promiscuity, has remained elusive. RXR, in contrast to its heterodimer partner, cannot autonomously induce transcription on binding of cognate agonists. Here we show that RXR can bind ligand and recruit co…

Protein ConformationReceptors Retinoic AcidPlasma protein bindingRetinoid X receptorLigandsNuclear Receptor Coactivator 2Structure-Activity RelationshipmedicineNuclear Receptor Co-Repressor 2Binding siteNuclear receptor co-repressor 2PhysicsMultidisciplinaryCell biologyDNA-Binding ProteinsRepressor ProteinsRetinoic acid receptorRetinoid X ReceptorsMechanism of actionBiochemistryNuclear receptorModels Chemicalembryonic structuresNuclear receptor coactivator 2medicine.symptomDimerizationProtein BindingTranscription FactorsNature
researchProduct