Search results for "Retinoic acid receptor"

showing 10 items of 27 documents

Expression of retinoic acid nuclear receptors in the mouse embryonal carcinoma cell line PCC7-Mz1

1992

Mouse embryonal carcinoma cell line PCC7-Mz1 can serve as a model of mammalian neural development [1989, J. Cell. Biol. 109, 2481-2493]. Upon exposure to all-trans retinoic acid (RA), Mz1 cells differentiate into a stable pattern of neurons, astroglia and fibroblasts whereas variants of the parental cell line either are restricted in their patterns of derivatives or do not respond at all to RA. Using gene probes specific for the alpha 1, alpha 2 and beta 2 isoforms of the retinoic acid nuclear receptor, we have studied by Northern blot analysis the expression of these transcription factors in uninduced and induced cells of clone Mz1 and in variants with different developmental potential. al…

Gene isoformmedicine.medical_specialtyTranscription GeneticReceptors Retinoic AcidCellular differentiationBiophysicsRetinoic acidTretinoinExpressionBiologyEmbryonic carcinoma cell line PCC7-MzBiochemistryEmbryonal carcinomaMicechemistry.chemical_compoundStructural BiologyInternal medicineTumor Cells CulturedGeneticsmedicineAnimalsRNA MessengerNorthern blotMolecular BiologyCell NucleusdbcAMPTeratomaRetinoic acid receptorCell DifferentiationCell BiologyBlotting Northernmedicine.diseaseCell biologyRetinoic acid receptorEndocrinologyBucladesineNuclear receptorchemistryCell cultureRNACarrier ProteinsPoly AIsoformsFEBS Letters
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Interleukin-12 and -23 Control Plasticity of CD127(+) Group 1 and Group 3 Innate Lymphoid Cells in the Intestinal Lamina Propria.

2015

Human group 1 ILCs consist of at least three phenotypically distinct subsets, including NK cells, CD127(+) ILC1, and intraepithelial CD103(+) ILC1. In inflamed intestinal tissues from Crohn's disease patients, numbers of CD127(+) ILC1 increased at the cost of ILC3. Here we found that differentiation of ILC3 to CD127(+) ILC1 is reversible in vitro and in vivo. CD127(+) ILC1 differentiated to ILC3 in the presence of interleukin-2 (IL-2), IL-23, and IL-1β dependent on the transcription factor RORγt, and this process was enhanced in the presence of retinoic acid. Furthermore, we observed in resection specimen from Crohn's disease patients a higher proportion of CD14(+) dendritic cells (DC), whi…

Interleukin 2Receptors Retinoic AcidCellular differentiationCD14ImmunologyInterleukin-1betaRetinoic acidLipopolysaccharide Receptorschemical and pharmacologic phenomenaTretinoinMice SCIDBiologyInterleukin-12 Subunit p35Interleukin-7 Receptor alpha Subunitchemistry.chemical_compoundMiceIntestinal mucosaCrohn DiseaseMice Inbred NODmedicineImmunology and AllergyAnimalsHumansRetinoid X Receptor gammaLymphocytesIntestinal MucosaInterleukin-7 receptorCells CulturedMice KnockoutRetinoic Acid Receptor alphaInnate lymphoid cellvirus diseaseshemic and immune systemsCell DifferentiationDendritic CellsNuclear Receptor Subfamily 1 Group F Member 3Molecular biologyKiller Cells NaturalMice Inbred C57BLInfectious DiseaseschemistryLymphocyte TransfusionImmunologyInterleukin 12Interleukin-23 Subunit p19Interleukin-2medicine.drugImmunity
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Vitamin E activates CRABP-II gene expression in cultured human fibroblasts, role of protein kinase C

2004

The treatment of human fibroblasts with different tocopherols in the presence of retinol caused an increase in cytoplasmic retinoic acid binding protein II (CRABP-II) mRNA and protein. The possibility of an involvement of protein kinase C (PKC) in the response to tocopherols was supported by the results obtained with the PKC-specific inhibitors, calphostin C and bisindolylmaleimide I. The effect of alpha-tocopherol was prevented by okadaic acid, suggesting that a protein phosphatase is responsible for PKC dephosphorylation produced by the presence of tocopherols. The results shown support the hypothesis that phosphorylation/dephosphorylation of RXRalpha via PKC may be involved in the regula…

MaleBisindolylmaleimideTranscription GeneticReceptors Retinoic AcidPhosphatasealpha-TocopherolBiophysicsBiochemistryDephosphorylationchemistry.chemical_compoundStructural BiologyProtein kinase COkadaic AcidGeneticsHumansVitamin ERNA MessengerRetinoic acid bindingPhosphorylationMolecular BiologyProtein kinase CCells CulturedDNA PrimersBase SequenceReverse Transcriptase Polymerase Chain ReactionInfant NewbornRetinoid X receptor αCell BiologyMolecular biologyRetinoic acid receptorCalphostin CchemistryGene Expression RegulationProtein phosphatasePhosphorylationFibroblastCytoplasmic retinoic acid binding protein IIFEBS Letters
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Analysis of t(15;17) chromosomal breakpoint sequences in therapy-related versus de novo acute promyelocytic leukemia: Association of DNA breaks with …

2010

We compared genomic breakpoints at the PML and RARA loci in 23 patients with therapy-related acute promyelocytic leukemia (t-APL) and 25 de novo APL cases.Eighteen of 23 t-APL cases received the topoisomerase II poison mitoxantrone for their primary disorder. DNA breaks were clustered in a previously reported 8 bp "hot spot" region of PML corresponding to a preferred site of mitoxantrone-induced DNA topoisomerase II-mediated cleavage in 39% of t-APL occurring in patients exposed to this agent and in none of the cases arising de novo (P = 0.007). As to RARA breakpoints, clustering in a 3' region of intron 2 (region B) was found in 65% of t-APL and 28% of de novo APL patients, respectively. S…

MaleCancer ResearchReceptors Retinoic AcidRetinoic AcidMessengerPromyelocytic Leukemia ProteinTranslocation GeneticChromosome BreakpointsLeukemia Promyelocytic Acuteimmune system diseasesReceptorsPromyelocyticGeneticsLeukemiabiologyReverse Transcriptase Polymerase Chain ReactionRetinoic Acid Receptor alphaNuclear ProteinsDNA NeoplasmMiddle AgedFemaleHumanAdultAcute promyelocytic leukemiaChromosome BreakpointsTranslocationAntineoplastic AgentsAcuteChromosomesYoung AdultPromyelocytic leukemia proteinGeneticGeneticsmedicineConsensus sequenceHumansRNA MessengerReceptors Retinoic Acid; Male; Young Adult; Middle Aged; Chromosome Breakpoints; Female; Chromosomes Human Pair 17; Tumor Suppressor Proteins; Humans; DNA Neoplasm; Translocation Genetic; Leukemia Promyelocytic Acute; Antineoplastic Agents; Nuclear Proteins; RNA Messenger; Mitoxantrone; Reverse Transcriptase Polymerase Chain Reaction; Chromosomes Human Pair 15; Transcription Factors; Aged; AdultneoplasmsAgedChromosomes Human Pair 15Pair 17Tumor Suppressor ProteinsTopoisomeraseBreakpointPair 15DNAmedicine.diseaseRetinoic acid receptor alphabiology.proteinNeoplasmRNAHuman genomeMitoxantroneSettore MED/15 - Malattie del SangueChromosomes Human Pair 17Transcription FactorsGenes, Chromosomes and Cancer
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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
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Retinoic acid inhibits nitric oxide synthase-2 expression through the retinoic acid receptor-alpha.

2000

Retinoids are multipotent modulators of cellular functions and suppress cytokine-induced production of nitric oxide (NO) in several cell types. We have explored the mechanisms by which retinoic acid (RA) regulates NO production in rat aortic smooth muscle cells (VSMC), which express NOS2 in response to proinflammatory cytokines. RA inhibited interleukin-1beta (IL-1beta)-induced NOS2 mRNA expression and NO production. These effects were attenuated by the retinoic acid receptor (RAR) antagonist CD3106, indicating that they were mediated through retinoic acid receptors (RARs). The synthetic retinoid agonists CD336 (which specifically binds RARalpha) and CD367 (which binds all RARs) but not ago…

MaleTranscription GeneticReceptors Retinoic AcidBiophysicsRetinoic acidNitric Oxide Synthase Type IIRetinoic acid receptor betaAorta ThoracicTretinoinBiochemistryGene Expression Regulation EnzymologicMuscle Smooth VascularProinflammatory cytokineRetinoic acid-inducible orphan G protein-coupled receptorRats Sprague-Dawleychemistry.chemical_compoundparasitic diseasesAnimalsPromoter Regions GeneticMolecular BiologyCells CulturedbiologyRetinoic Acid Receptor alphaNitric oxide synthase 2Cell BiologyRetinoic acid receptor gammarespiratory systemCell biologyRatsRetinoic acid receptorKineticsBiochemistrychemistryRetinoic acid receptor alphabiology.proteinNitric Oxide SynthaseInterleukin-1Biochemical and biophysical research communications
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Correlation between the effects of retinoic acid and dexamethasone on liver tyrosine aminotransferase

1997

A single dose of 50 microg of trans-retinoic acid administered to rats significantly raised the level of hepatic tyrosine after a few hours. This effect was compared with that of dexamethasone and a possible correlation between these effectors was also investigated. An equal increase in enzyme activity level caused by retinoic acid was observed in adrenalectomized rats, leading to the suggestion that the effect of retinoic acid on liver tyrosine aminotransferase is independent of glucocorticoids. However, the study of the binding activity of the liver nuclear glucocorticoid receptors vs dexamethasone showed that this activity is favoured by retinoic acid, whereas no variation was evidenced …

Malemedicine.medical_specialtyReceptors Retinoic AcidEndocrinology Diabetes and MetabolismClinical BiochemistryTyrosine TransaminaseRetinoic acidretinoic acid receptorAntineoplastic AgentsTretinoindexamethasoneBiologyBiochemistrychemistry.chemical_compoundReceptors GlucocorticoidEndocrinologyGlucocorticoid receptorTyrosine aminotransferaseInternal medicineglucocorticoid receptorretinoic acidmedicineAnimalsRats WistarTyrosineReceptorMolecular BiologyDexamethasoneTyrosine TransaminaseBinding SitesAdrenalectomyCell BiologyRatsEndocrinologyLiverchemistryTyrosineMolecular Medicinetyrosine aminotransferaseInjections IntraperitonealGlucocorticoidmedicine.drug
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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
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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
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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
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