Search results for "Retinoic acid receptor beta"

showing 7 items of 7 documents

Somatic copy number alterations are associated with EGFR amplification and shortened survival in patients with primary glioblastoma.

2019

Glioblastoma (GBM) is the most common malignant primary tumor of the central nervous system. With no effective therapy, the prognosis for patients is terrible poor. It is highly heterogeneous and EGFR amplification is its most frequent molecular alteration. In this light, we aimed to examine the genetic heterogeneity of GBM and to correlate it with the clinical characteristics of the patients. For that purpose, we analyzed the status of EGFR and the somatic copy number alterations (CNAs) of a set of tumor suppressor genes and oncogenes. Thus, we found GBMs with high level of EGFR amplification, low level and with no EGFR amplification. Highly amplified tumors showed histological features of…

0301 basic medicineMaleCancer ResearchBiopsyL-amp GB EGFR-low amplified glioblastomamedicine.disease_causewt wildtypeMYBPC3 myosin-binding protein C0302 clinical medicineHIC1 hypermethylated in cancer 1Gene duplicationIn Situ Hybridization FluorescenceIDH2 isocitrate dehydrogenase 2MutationRB-pat RB signaling pathwayEGFRvIII epidermal growth factor receptor variant number IIIPAH phenylalanine hydroxylaseGBM glioblastoma IDH-wildtype (glioblastoma multiforme primary glioblastoma).ANOVA ANalysis Of VArianceN-amp GB EGFR-no amplified glioblastomaMiddle AgedCDKN2A cyclin-dependent kinase inhibitor 2Alcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensPrognosisPrimary tumorImmunohistochemistryH-amp GB EGFR-high amplified glioblastomaErbB ReceptorsTKR-pat tyrosine-kinase receptors signaling pathway030220 oncology & carcinogenesisDisease ProgressionCDK6 cyclin-dependent kinase 6CDH1 Cadherin 1FemaleCREM cAMP response element modulatorIHC immunohistochemistryAdultOriginal articleDNA Copy Number VariationsCDKN1B cyclin-dependent kinase inhibitor 1BBiologyRARB retinoic acid receptor betaCNS central nervous systemlcsh:RC254-282IDH1 isocitrate dehydrogenase 1BCL2 B-cell cll/ lymphoma 2CNAs copy number algerationsWHO World Health Organization03 medical and health sciencesYoung Adultp53-pat p53 signaling pathwaymedicineBiomarkers TumorTMA tissue microarrayPTENHumansProtein kinase BPI3K/AKT/mTOR pathwaySurvival analysisAgedGenetic heterogeneityGene AmplificationGFAP glial fibrillary acidic proteinMLPA multiplex ligation-dependent probe amplificationmedicine.diseaseFISH fluorescence in situ hibridizationSurvival AnalysisCDKN2B cyclin-dependent kinase inhibitor 2BPTEN phosphatase and tensin homologEGFR epidermal growth factor receptorCNV-load load of copy number variations030104 developmental biologyMutationPARK2 parkinCancer researchbiology.proteinTCGA The Cancer Genome AtlasLARGE1 acetylglucosaminyltransferase-like protein 1GlioblastomaCHD7 Chromodomain Helicase DNA Binding Protein 7DAPI 4′6-diamidino-2-phenylindoleNeoplasia (New York, N.Y.)
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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
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Retinol oxidation to retinoic acid in human thyroid glandular cells.

2014

Abstract Retinoic acid is regarded as the retinol metabolite that controls proliferation and differentiation of epithelial cells. In the present study, we investigated the potential role of xanthine dehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC). In particular, we observed that cellular retinoids binding proteins (CRBPs) are also implicated in the biosynthetic pathway leading to retinoic acid formation in primary cultures of HTGC, as we have already reported for human mammary epithelial cells (HMEC). After partial protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its …

AdultMaleXanthine DehydrogenasePrimary Cell CultureRetinoic acidThyroid GlandOxypurinolRetinoic acid receptor betaTretinoinBiologyXanthinechemistry.chemical_compoundBiosynthesisSettore BIO/10 - BiochimicaDrug DiscoveryHumansEnzyme InhibitorsVitamin AEnzyme AssaysPharmacologyImmunoassayRetinolEpithelial CellsRetinol-Binding Proteins CellularGeneral MedicineMiddle AgedXanthineUric AcidRetinoic acid receptorchemistryXanthine dehydrogenaseBiochemistryCRABPs CRBPs human glandular cells. retinoic acid biosynthesis. retinol oxidation xanthine dehydrogenaseUric acidFemaleOxidation-ReductionJournal of enzyme inhibition and medicinal chemistry
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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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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
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Xanthine dehydrogenase processes retinol to retinoic acid in human mammary epithelial cells

2008

Retinoic acid is considered to be the active metabolite of retinol, able to control differentiation and proliferation of epithelia. Retinoic acid biosynthesis has been widely described with the implication of multiple enzymatic activities. However, our understanding of the cell biological function and regulation of this process is limited. In a recent study we evidenced that milk xanthine oxidase (E.C. 1.17.3.2.) is capable to oxidize all-trans-retinol bound to CRBP (holo-CRBP) to all-trans-retinaldehyde and then to all-trans-retinoic acid. To get further knowledge regarding this process we have evaluated the biosynthetic pathway of retinoic acid in a human mammary epithelial cell line (HME…

Receptors Retinoic AcidXanthine dehydrogenaseCellRetinoic acidOxypurinolTretinoinRetinoic acid receptor betaBiologychemistry.chemical_compoundSettore BIO/10 - BiochimicaDrug DiscoverymedicineHumansMammary Glands HumanVitamin AXanthine oxidaseHMECPharmacologyRetinolEpithelial CellsRetinol-Binding Proteins CellularGeneral MedicineMilk ProteinsNADRetinoic acid receptormedicine.anatomical_structurechemistryBiochemistryXanthine dehydrogenaseRetinol oxidationRetinoic acid receptor alphaRetinoid AcidMetabolic Networks and PathwaysJournal of Enzyme Inhibition and Medicinal Chemistry
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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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