Search results for "RETINOIC ACID"

showing 10 items of 107 documents

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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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
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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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T helper type 17-related cytokine expression is increased in the bronchial mucosa of stable chronic obstructive pulmonary disease patients.

2009

Summary There are increased numbers of activated T lymphocytes in the bronchial mucosa of stable chronic obstructive pulmonary disease (COPD) patients. T helper type 17 (Th17) cells release interleukin (IL)-17 as their effector cytokine under the control of IL-22 and IL-23. Furthermore, Th17 numbers are increased in some chronic inflammatory conditions. To investigate the expression of interleukin (IL)-17A, IL-17F, IL-21, IL-22 and IL-23 and of retinoic orphan receptor RORC2, a marker of Th17 cells, in bronchial biopsies from patients with stable COPD of different severity compared with age-matched control subjects. The expression of IL-17A, IL-17F, IL-21, IL-22, IL-23 and RORC2 was measure…

MaleTranslational StudiesReceptors Retinoic Acidmedicine.medical_treatmentImmunologyautoimmunity bronchial biopsies emphysema neutrophilsInflammationBronchiInterleukin-23Polymerase Chain ReactionStatistics NonparametricPulmonary Disease Chronic ObstructiveAutoimmunity bronchial biopsies emphysema neutrophils pathologymedicineInterleukin 23Immunology and AllergyHumansRNA MessengerAgedDNA PrimersCOPDAnalysis of VarianceMucous MembraneReceptors Thyroid Hormonebusiness.industryInterleukinsRespiratory diseaseInterleukin-17SmokingInterleukinT-Lymphocytes Helper-InducerMiddle AgedNuclear Receptor Subfamily 1 Group F Member 3medicine.diseaseImmunohistochemistryrespiratory tract diseasesRespiratory Function TestsCytokineCase-Control StudiesImmunologyFemaleInterleukin 17medicine.symptombusinessCD8
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Retinol, at concentrations greater than the physiological limit, induces oxidative stress and apoptosis in human dermal fibroblasts

2004

We have investigated the dose (in the range of microM) and time-dependent effects of four different retinoids (retinol, retinal, retinoic acid and retinol palmitate) on human dermal fibroblasts cultivated in vitro. Retinol and retinal, at a concentration of 20 microM, caused cell damage as evaluated by lactate dehydrogenase activity released into the culture medium. The oxidised glutathione (GSSG)/reduced glutathione (GSH) ratio and malondialdehyde production indicated that 20 microM of retinol provoked oxidative stress in the cultivated human fibroblasts. In the first 8 h after retinol treatment the levels of p53 and Bax proteins as well as caspase 3 activity increased, suggesting apoptoti…

Malemedicine.medical_specialtyAntioxidantmedicine.medical_treatmentRetinoic acidApoptosisTretinoinDermatologyBiologymedicine.disease_causeBiochemistryAntioxidantsRetinoidschemistry.chemical_compoundSkin Physiological PhenomenaInternal medicinemedicineHumansVitamin AMolecular BiologyCells CulturedSkinCell DeathDose-Response Relationship DrugGlutathione DisulfideL-Lactate DehydrogenaseVitamin EInfant NewbornRetinolRetinalGlutathioneFibroblastsMalondialdehydeGlutathioneOxidative StressEndocrinologychemistryOxidative stressExperimental Dermatology
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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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Mucoadhesive PEGylated inulin-based self-assembling nanoparticles: In vitro and ex vivo transcorneal permeation enhancement of corticosteroids

2019

Abstract As transcorneal drug delivery is still a challenge, the scope of the present study was to prepare useful nanosystems able to enhance transcorneal permeation/penetration of drugs. Moreover, this work aims to evaluate the effectiveness of inulin-based nanosystems in the specific field of ocular drug delivery and the effect of PEG chains to promote mucoadhesion, stability and transcorneal penetration/permeation enhancer effect of self-assembling nanoparticles in vitro (transwell systems and HCE) and ex vivo (Franz cells and bovine cornea). In particular, inulin was chosen as the starting natural polysaccharide polymer to design a novel amphiphilic derivative named INU-EDA-RA-PEG capab…

Polyethylene glycolInulin Self-assembling nanoparticles Transcorneal delivery Retinoic acid Polyethylene glycolTranscorneal deliveryInulinInulinSelf-assembling nanoparticlesPharmaceutical ScienceNanoparticle02 engineering and technologyPenetration (firestop)Permeation021001 nanoscience & nanotechnology030226 pharmacology & pharmacy03 medical and health scienceschemistry.chemical_compound0302 clinical medicinechemistrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoDrug deliveryAmphiphilePEG ratioRetinoic acidMucoadhesionBiophysics0210 nano-technologyJournal of Drug Delivery Science and Technology
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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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