Search results for "RECEPTORS"

showing 10 items of 3254 documents

Nuclear aggregation of olfactory receptor genes governs their monogenic expression.

2012

SummaryGene positioning and regulation of nuclear architecture are thought to influence gene expression. Here, we show that, in mouse olfactory neurons, silent olfactory receptor (OR) genes from different chromosomes converge in a small number of heterochromatic foci. These foci are OR exclusive and form in a cell-type-specific and differentiation-dependent manner. The aggregation of OR genes is developmentally synchronous with the downregulation of lamin b receptor (LBR) and can be reversed by ectopic expression of LBR in mature olfactory neurons. LBR-induced reorganization of nuclear architecture and disruption of OR aggregates perturbs the singularity of OR transcription and disrupts the…

Transcription GeneticCytoplasmic and NuclearChromosomal Proteins Non-HistoneDown-RegulationReceptors Cytoplasmic and NuclearLamin B receptorBiologyReceptors OdorantMedical and Health SciencesGeneral Biochemistry Genetics and Molecular BiologyFluorescenceOlfactory Receptor NeuronsArticle03 medical and health sciencesMice0302 clinical medicineDownregulation and upregulationGeneticTranscription (biology)HeterochromatinGene expressionReceptorsmedicineGeneticsAnimalsGeneIn Situ HybridizationIn Situ Hybridization Fluorescence030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesOlfactory receptorBiochemistry Genetics and Molecular Biology(all)Neurosciencesta1182Non-HistoneBiological SciencesCell biologyChromosomal Proteinsmedicine.anatomical_structureOdorantGene Expression RegulationEctopic expressionTranscription030217 neurology & neurosurgeryDevelopmental BiologyCell
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Characterization and DNA-binding properties of GRF, a novel monomeric binding orphan receptor related to GCNF and betaFTZ-F1

1999

0014-2956 (Print) Comparative Study Journal Article Research Support, Non-U.S. Gov't; A PCR approach has been used to isolate, from Bombyx mori, a cDNA encoding a novel orphan receptor (GRF) that is most closely related to Bombyx betaFTZ-F1 and to the vertebrate germ cell nuclear factor. The major GRF mRNA is detected in most tissues as an 8-kb transcript whose amount follows the circulating ecdysteroid concentration with a delay. The expression pattern of GRF is similar to that of the Bombyx homologue of the Drosophila early-late gene DHR3, and precedes that of betaFTZ-F1 in all stages and tissues examined. The GRF protein is thus likely to be required in many tissues, but in a temporally …

Transcription GeneticReceptors Cytoplasmic and NuclearFushi Tarazu Transcription FactorsSequence HomologyGenes InsectDevelopmental/drug effectsSteroidogenic Factor 1BiochemistryBombyx/*chemistry/growth & developmentDNA/*metabolismNuclear Receptor Subfamily 6 Group A Member 1ReceptorsCloning MolecularReceptorRegulation of gene expressionOrphan receptorbiologyGene Expression Regulation DevelopmentalDNA-Binding ProteinsEcdysterone/pharmacologyAmino AcidEcdysteroneInsect Proteins/genetics/*isolation & purification/metabolismInsect ProteinsRecombinant Fusion Proteins/metabolismTranscriptionProtein StructureRecombinant Fusion ProteinsGerm cell nuclear factorMolecular Sequence DataGeneticComplementary DNAAnimalsAmino Acid SequenceBinding siteBombyxHomeodomain ProteinsBinding Sitespurification/metabolismSequence Homology Amino AcidBase SequencefungiMolecularCytoplasmic and Nuclear/chemistryDNABombyxbiology.organism_classificationMolecular biologyProtein Structure TertiaryTranscription Factors/chemistry/genetics/*isolation &Nuclear receptorGene Expression RegulationGenesDNA-Binding Proteins/chemistry/genetics/*isolation &InsectSequence AlignmentTertiaryTranscription FactorsCloning
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Targeting the aryl hydrocarbon receptor with a novel set of triarylmethanes

2020

International audience; The aryl hydrocarbon receptor (AhR) is a chemical sensor upregulating the transcription of responsive genes associated with endocrine homeostasis, oxidative balance and diverse metabolic, immunological and inflammatory processes, which have raised the pharmacological interest on its modulation. Herein, a novel set of 32 unsymmetrical triarylmethane (TAM) class of structures has been synthesized, characterized and their AhR transcriptional activity evaluated using a cell-based assay. Eight of the assayed TAM compounds (14, 15, 18, 19, 21, 22, 25, 28) exhibited AhR agonism but none of them showed antagonist effects. TAMs bearing benzotrifluoride, naphthol or heteroarom…

Transcriptional ActivationAgonistmedicine.drug_classStereochemistryIn silicoCYP1A101 natural sciences03 medical and health scienceschemistry.chemical_compoundTriarylmethaneDrug DiscoverymedicineHumans[CHIM]Chemical SciencesMolecular Targeted TherapyTranscription factor030304 developmental biologyADMEPharmacologyIndole test0303 health sciencesbiology010405 organic chemistryChemistryOrganic ChemistryQuinolineHep G2 CellsGeneral MedicineDruglikenessAryl hydrocarbon receptor3. Good health0104 chemical sciencesMolecular Docking SimulationReceptors Aryl HydrocarbonAh receptorbiology.proteinTranscription factorMethaneAgonistic activityProtein Binding
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Epigenetic activation of a cryptic TBC1D16 transcript enhances melanoma progression by targeting EGFR

2015

Metastasis is respoMetastasis is responsible for most cancer-related deaths, and, among common tumor types, melanoma is one with great potential to metastasize. Here we study the contribution of epigenetic changes to the dissemination process by analyzing the changes that occur at the DNA methylation level between primary cancer cells and metastases. We found a hypomethylation event that reactivates a cryptic transcript of the Rab GTPase activating protein TBC1D16 (TBC1D16-47 kDa; referred to hereafter as TBC1D16-47KD) to be a characteristic feature of the metastatic cascade. This short isoform of TBC1D16 exacerbates melanoma growth and metastasis both in vitro and in vivo. By combining imm…

Transcriptional ActivationGTPase-activating proteinImmunoprecipitationMice NudeEditorials: Cell Cycle FeaturesBiologyBioinformaticsMethylationGeneral Biochemistry Genetics and Molecular BiologyEpigenesis GeneticMetastasisMetastasisEpigènesiMetàstasiCell Line TumormedicineAnimalsImmunoprecipitationProtein IsoformsRNA MessengerEpigeneticsNeoplasm MetastasisRNA Small InterferingPromoter Regions GeneticProteïnes supressores de tumorsProtein Kinase InhibitorsMelanomaMelanomaGTPase-Activating ProteinsGeneral MedicineMethylationDNA MethylationPrognosismedicine.diseaseTumor suppressor proteinErbB ReceptorsMolecular WeightTreatment Outcomerab GTP-Binding ProteinsDNA methylationDisease ProgressionCancer researchRabMetilacióProtein BindingSignal TransductionEpigenesisNature Medicine
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Peroxisome-proliferator-activated receptors as physiological sensors of fatty acid metabolism: molecular regulation in peroxisomes

2001

The enzymes required for the beta-oxidation of fatty acyl-CoA are present in peroxisomes and mitochondria. Administration of hypolipidaemic compounds such as clofibrate to rodents leads to an increase in the volume and density of peroxisomes in liver cells. These proliferators also induce simultaneously the expression of genes encoding acyl-CoA oxidase, enoyl-CoA hydratase-hydroxyacyl-CoA dehydrogenase (multifunctional enzyme) and thiolase (3-ketoacyl-CoA thiolase). All these enzymes are responsible for long-chain and very-long-chain fatty acid beta-oxidation in peroxisomes. Similar results were observed when rat hepatocytes, or liver-derived cell lines, were cultured with a peroxisome prol…

Transcriptional ActivationGuinea PigsResponse elementReceptors Cytoplasmic and NuclearBiologyBiochemistryGene Expression Regulation EnzymologicMicechemistry.chemical_compoundPeroxisomesAnimalsAcetyl-CoA C-AcetyltransferasePhosphorylationTranscription factorProtein Kinase Cchemistry.chemical_classificationFatty acid metabolismThiolaseFatty AcidsFatty acidPeroxisomeRatsLiverchemistryBiochemistryAcetyl-CoA C-acetyltransferasePeroxisome proliferator-activated receptor alphaSignal TransductionTranscription FactorsBiochemical Society Transactions
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Peroxisome proliferators and peroxisome proliferator activated receptors (PPARs) as regulators of lipid metabolism.

1997

Peroxisome proliferation (PP) in mammalian cells, first described 30 years ago, represents a fascinating field of modern research. Major improvements made in its understanding were obtained through basic advances that have opened up new areas in cell biology, biochemistry and genetics. A decade after the first report on PP, a new metabolic pathway (peroxisomal beta-oxidation) and its inducibility by peroxisome proliferators were discovered. More recently, a new type of nuclear receptor, the peroxisome proliferator-activated receptor (PPAR), has been described. The first PPAR was discovered in 1990. Since then, many other PPARs have been characterized. This original class of nuclear receptor…

Transcriptional ActivationPeroxisome ProliferationPeroxisome proliferator-activated receptorReceptors Cytoplasmic and NuclearBiologyLigandsBiochemistryMicrobodiesGene Expression Regulation EnzymologicMicrosomesAnimalsHumansReceptorHypolipidemic Agentschemistry.chemical_classificationFatty AcidsLipid metabolismGeneral MedicinePeroxisomeLipid MetabolismCell biologyMitochondriaBiochemistrychemistryNuclear receptorLiverlipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaAcyl-CoA OxidaseSignal transductionOxidoreductasesOxidation-ReductionSignal TransductionTranscription FactorsBiochimie
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Regulation of the peroxisomal β-oxidation-dependent pathway by peroxisome proliferator-activated receptor α and kinases

2000

The first PPAR (peroxisome proliferator-activated receptor) was cloned in 1990 by Issemann and Green (Nature 347:645-650). This nuclear receptor was so named since it is activated by peroxisome proliferators including several drugs of the fibrate family, plasticizers, and herbicides. This receptor belongs to the steroid receptor superfamily. After activation by a specific ligand, it binds to a DNA response element, PPRE (peroxisome proliferator response element), which is a DR-1 direct repeat of the consensus sequence TGACCT x TGACCT. This mechanism leads to the transcriptional activation of target genes (Motojima et al., J Biol Chem 273:16710-16714, 1998). After the first discovery, severa…

Transcriptional ActivationPeroxisome proliferator-activated receptor gammamedicine.drug_classReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorFibrateBiologyBiochemistryPhosphatidylinositol 3-KinasesmedicineAnimalsHumansPhosphorylationProtein kinase AProtein Kinase CPharmacologychemistry.chemical_classificationPeroxisomeNuclear receptorchemistryBiochemistryPeroxisome Proliferatorslipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaSignal transductionSignal TransductionTranscription FactorsBiochemical Pharmacology
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Heterocycle-containing retinoids. Discovery of a novel isoxazole arotinoid possessing potent apoptotic activity in multidrug and drug-induced apoptos…

2001

In a search for retinoic acid (RA) receptor ligands endowed with potent apoptotic activity, a series of novel arotinoids were prepared. Because the stereochemistry of the C9-alkenyl portion of natural 9-cis-RA and the olefinic moiety of the previously synthesized isoxazole retinoid 4 seems to have particular importance for their apoptotic activity, novel retinoid analogues with a restricted or, vice versa, a larger flexibility in this region were designed and prepared. The new compounds were evaluated in vitro for their ability to activate natural retinoid receptors and for their differentiation-inducing activity. Cytotoxic and apoptotic activities were, in addition, evaluated. In general, …

Transcriptional ActivationProgrammed cell deathTetrahydronaphthalenesmedicine.drug_classReceptors Retinoic AcidRetinoic acidAntineoplastic AgentsApoptosisBenzoateschemistry.chemical_compoundInhibitory Concentration 50RetinoidsDrug DiscoverymedicineTumor Cells CulturedHumansRetinoidIsoxazoleCytotoxicityReceptorCell DifferentiationIsoxazolesIn vitroDrug Resistance MultipleBiochemistrychemistryApoptosisDrug Resistance NeoplasmMolecular MedicineDrug Screening Assays AntitumorCell DivisionJournal of medicinal chemistry
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The Wilms' tumor suppressor gene (wt1) product regulates Dax-1 gene expression during gonadal differentiation.

1999

Gonadal differentiation is dependent upon a molecular cascade responsible for ovarian or testicular development from the bipotential gonadal ridge. Genetic analysis has implicated a number of gene products essential for this process, which include Sry, WT1, SF-1, and DAX-1. We have sought to better define the role of WT1 in this process by identifying downstream targets of WT1 during normal gonadal development. We have noticed that in the developing murine gonadal ridge, wt1 expression precedes expression of Dax-1, a nuclear receptor gene. We document here that the spatial distribution profiles of both proteins in the developing gonad overlap. We also demonstrate that WT1 can activate the D…

Transcriptional Activationcongenital hereditary and neonatal diseases and abnormalitiesGenes Wilms TumorReceptors Retinoic AcidTATA boxMolecular Sequence DataMutagenesis (molecular biology technique)Biologyurologic and male genital diseasesResponse ElementsTransactivationMiceGene expressionAnimalsHumansGonadsPromoter Regions GeneticWT1 ProteinsMolecular BiologyGeneCell Growth and DevelopmentCell Line TransformedGonadal ridgeBase Sequenceurogenital systemDAX-1 Orphan Nuclear ReceptorfungiGene Expression Regulation DevelopmentalCell Biologyfemale genital diseases and pregnancy complicationsCell biologyDNA-Binding ProteinsRepressor ProteinsTestis determining factorNuclear receptorCOS CellsCancer researchTranscription FactorsMolecular and cellular biology
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Physiological activation of the IgH 3' enhancer in B lineage cells is not blocked by Pax-5.

1996

The mouse 3' enhancer contains a high-affinity binding site for the paired box protein Pax-5. Here, we demonstrate by genomic footprinting that the rat 3' enhancer contains a low-affinity binding site for Pax-5, which is occupied in activated splenic B cells. Thus, binding of Pax-5 to the IgH 3' enhancer appears to be evolutionarily conserved in rodents. Analysis of Pax-5 expression in primary B cells demonstrates that Pax-5 remains expressed after 4 days of lipopolysaccharide (LPS) induction, but is down-regulated in 5-day stimulated cells. Similarly, the expression of Pax-5 is down-regulated in vivo in activated large splenocytes, in contrast to small resting cells. Multimerization of the…

Transcriptional Activationcongenital hereditary and neonatal diseases and abnormalitiesanimal structuresImmunologyCD40 LigandDNA FootprintingHeterologousDown-RegulationReceptors Antigen B-CellEnhancer RNAsLymphocyte ActivationMiceGene expressionImmunology and AllergyAnimalsBinding siteEnhancerTranscription factorCells CulturedReporter geneB-LymphocytesCD40Membrane GlycoproteinsbiologyGenes ImmunoglobulinPAX5 Transcription FactorNuclear ProteinsMolecular biologyRatsUp-Regulationbody regionsDNA-Binding ProteinsRepressor ProteinsEnhancer Elements GeneticGene Expression Regulationembryonic structuresbiology.proteinTrans-Activatorssense organsTranscription FactorsEuropean journal of immunology
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