Search results for " Cytoplasmic and Nuclear"

showing 10 items of 80 documents

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
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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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Identification of novel peroxisome proliferator-activated receptor alpha (PPARalpha) target genes in mouse liver using cDNA microarray analysis.

2001

Peroxisome proliferators, which function as peroxisome proliferator-activated receptor-alpha (PPARalpha) agonists, are a group of structurally diverse nongenotoxic hepatocarcinogens including the fibrate class of hypolipidemic drugs that induce peroxisome proliferation in liver parenchymal cells. Sustained activation of PPARalpha by these agents leads to the development of liver tumors in rats and mice. To understand the molecular mechanisms responsible for the pleiotropic effects of these agents, we have utilized the cDNA microarray to generate a molecular portrait of gene expression in the liver of mice treated for 2 weeks with Wy-14,643, a potent peroxisome proliferator. PPARalpha activa…

Mice KnockoutPeroxisome proliferator-activated receptor gammaDNA ComplementaryChemistryMicroarray analysis techniquesGene Expression ProfilingPeroxisome ProliferationReceptors Cytoplasmic and NuclearPeroxisomeArticleCell biologyGene expression profilingMice Inbred C57BLMicePyrimidinesLiverGene expressionGeneticsAnimalsPeroxisome proliferator-activated receptor deltaPeroxisome proliferator-activated receptor alphaMolecular BiologyOligonucleotide Array Sequence AnalysisTranscription FactorsGene expression
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Structural and Functional Similarity of Amphibian Constitutive Androstane Receptor with Mammalian Pregnane X Receptor

2016

The nuclear receptors and xenosensors constitutive androstane receptor (CAR, NR1I3) and pregnane X receptor (PXR, NR1I2) induce the expression of xenobiotic metabolizing enzymes and transporters, which also affects various endobiotics. While human and mouse CAR feature a high basal activity and low induction upon ligand exposure, we recently identified two constitutive androstane receptors in Xenopus laevis (xlCARá and â) that possess PXR-like characteristics such as low basal activity and activation in response to structurally diverse compounds. Using a set of complementary computational and biochemical approaches we provide evidence for xlCARá being the structural and functional counterpa…

Models MolecularReceptors SteroidReceptors Cytoplasmic and Nuclearlcsh:MedicineMolecular Dynamics SimulationPharmacologyBiologyCrystallography X-Raydigestive systemAmphibian ProteinsCell LineXenopus laevischemistry.chemical_compoundChlorocebus aethiopsConstitutive androstane receptorCoactivatorAnimalsHumansBinding sitelcsh:ScienceReceptorConstitutive Androstane ReceptorPregnane X receptorBinding SitesMultidisciplinarylcsh:RPregnane X ReceptorCorrectionLigand (biochemistry)digestive system diseasesCell biologychemistryNuclear receptorCOS Cellslcsh:QAndrostanePLOS ONE
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Evolutionary aspects of peroxisomes as cell organelles, and of genes encoding peroxisomal proteins

2001

Peroxisomes are present in most eukaryotic cell types, and have different enzymatic content and metabolic functions throughout the life scale. The endosymbiotic origin of these DNA-devoid organelles is supported by evolutionary data concerning genes encoding not only most peroxisomal proteins, but also several transcriptional factors regulating their expression such as peroxisome proliferator-activated receptors.

OrganellesNuclear ProteinsReceptors Cytoplasmic and NuclearCell BiologyGeneral MedicinePlantsMitochondrionPeroxisomeBiologyMicrobodiesCell biologyEvolution MolecularGene Expression RegulationBiochemistryPhylogeneticsOrganellePeroxisomesAnimalsHumansMicrobodyReceptorTranscription factorGeneTranscription FactorsBiology of the Cell
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The expression level of the orphan nuclear receptor GCNF (germ cell nuclear factor) is critical for neuronal differentiation.

2004

The germ cell nuclear factor (GCNF) is essential for normal embryonic development and gametogenesis. To test the prediction that GCNF is additionally required for neuronal differentiation, we used the mouse embryonal carcinoma cell line PCC7-Mz1, which represents an advantageous model to study neuronal cells from the stage of fate choice until the acquirement of functional competence. We generated stable transfectants that express gcnf sense or antisense RNA under the control of a tetracycline-regulated promoter. After retinoic acid-induced withdrawal from the cell cycle, sense clones developed a neuron network with changed properties, and the time course of neuron maturation was shortened.…

Patch-Clamp TechniquesGerm cell nuclear factorSynaptophysinDown-RegulationGene ExpressionReceptors Cytoplasmic and NuclearNerve Tissue ProteinsTretinoinBiologyNestinMiceEndocrinologyGAP-43 ProteinIntermediate Filament ProteinsNuclear Receptor Subfamily 6 Group A Member 1AnimalsRNA AntisenseMolecular BiologyNeuronsCell CycleCell PolarityCell DifferentiationGeneral MedicineCell cycleNestinCell biologyUp-RegulationNeuroepithelial cellDNA-Binding Proteinsnervous systemNeuron maturationSynaptophysinbiology.proteinNeuron differentiationStem cellMicrotubule-Associated ProteinsMolecular endocrinology (Baltimore, Md.)
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Phosphorylation of peroxisome proliferator-activated receptor α in rat Fao cells and stimulation by ciprofibrate

1999

The basic mechanism(s) by which peroxisome proliferators activate peroxisome proliferator-activated receptors (PPARs) is (are) not yet fully understood. Given the diversity of peroxisome proliferators, several hypotheses of activation have been proposed. Among them is the notion that peroxisome proliferators could activate PPARs by changing their phosphorylation status. In fact, it is well known that several members of the nuclear hormone receptor superfamily are regulated by phosphorylation. In this report, we show that the rat Fao hepatic-derived cell line, known to respond to peroxisome proliferators, exhibited a high content of PPARalpha. Alkaline phosphatase treatment of Fao cell lysat…

Peroxisome proliferator-activated receptor gammaPhosphataseReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorBiologyMicrobodiesBiochemistryCell LineClofibric AcidmedicineAnimalsEnzyme InhibitorsPhosphorylationPharmacologychemistry.chemical_classificationFibric Acidsfood and beveragesPeroxisomePhosphoric Monoester HydrolasesRatsGene Expression RegulationBiochemistryNuclear receptorchemistryPhosphorylationPeroxisome Proliferatorslipids (amino acids peptides and proteins)Acyl-CoA OxidasePeroxisome proliferator-activated receptor alphaCiprofibrateOxidoreductasesTranscription Factorsmedicine.drugBiochemical Pharmacology
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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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Functional characterization of a peroxisome proliferator response-element located in the intron 3 of rat peroxisomal thiolase B gene.

2003

Expression of the rat peroxisomal 3-ketoacyl-CoA thiolase gene B is induced by peroxisome proliferators. Although a sequence element like a peroxisome proliferator-activated receptor (PPAR)-binding site is located in the promoter region of this gene, we previously found that this element is competent for the activation by hepatocyte nuclear factor-4, but not functional with PPARalpha. We describe here a new peroxisome proliferator-response element located in the intron 3 (+1422/+1434) that binds in vitro the PPARalpha/retinoid X receptor alpha heterodimer and confers the induction by PPARalpha in transfection assays. We propose a model of regulation of the rat thiolase B gene involving thos…

Peroxisome proliferator-activated receptor gammaResponse elementBiophysicsPeroxisome proliferator-activated receptorReceptors Cytoplasmic and NuclearRetinoid X receptorBiochemistryGene Expression Regulation EnzymologicStructure-Activity RelationshipPeroxisomesAnimalsAcetyl-CoA C-AcetyltransferaseMolecular BiologyCells Culturedchemistry.chemical_classificationThiolaseChemistryCell BiologyPhosphoproteinsMolecular biologyIntronsRatsDNA-Binding ProteinsBiochemistryHepatocyte Nuclear Factor 4LiverPeroxisome proliferator-activated receptor deltaPeroxisome ProliferatorsPeroxisome proliferator-activated receptor alphaPPARGC1BTranscription FactorsBiochemical and biophysical research communications
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The Concise Guide To Pharmacology 2021/22: G Protein-Coupled Receptors

2021

The Concise Guide to PHARMACOLOGY 2021/22 is the fifth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of nearly 1900 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes over 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will s…

RMCytoplasmic and NuclearComputer scienceDatabases PharmaceuticalHumans; Ion Channels; Ligands; Receptors Cytoplasmic and Nuclear; Receptors G-Protein-Coupled; Databases Pharmaceutical; PharmacologyReceptors Cytoplasmic and NuclearIN-VITRO CHARACTERIZATIONPharmacologyLigandsIon ChannelsNORSlaw.inventionReceptors G-Protein-CoupledG-Protein-CoupledDatabases03 medical and health sciencesCALCIUM-SENSING RECEPTOR0302 clinical medicineDELTA-OPIOID RECEPTORlawSummary informationReceptorsHumansHISTAMINE H-3 RECEPTORFATTY-ACID RECEPTORMETABOTROPIC GLUTAMATE-RECEPTOR030304 developmental biologyG protein-coupled receptorPharmacologyGONADOTROPIN-RELEASING-HORMONE0303 health sciencesClinical pharmacologyFORMYL PEPTIDE RECEPTORMUSCARINIC ACETYLCHOLINE-RECEPTOR3. Good health317 Pharmacy030220 oncology & carcinogenesisPharmaceuticalNEGATIVE ALLOSTERIC MODULATORCatalytic receptors
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