Search results for "RECEPTORS"

showing 10 items of 3254 documents

Disruption of T helper 2-immune responses in Epstein–Barr virus-induced gene 3-deficient mice

2002

Epstein–Barr virus-induced gene 3 (EBI3) is a widely expressed IL-12p40-related protein that associates as a heterodimer with either IL-12p35 or an IL-12p35 homologue, p28, to create a new cytokine (IL-27). To define the function of EBI3in vivo, we generated knockout mice in which theebi3gene was targeted by homologous recombination. EBI3−/−mice exhibited normal numbers of both naive and mature CD4+and CD8+T cells and B cells, but markedly decreased numbers of invariant natural killer T cells (iNKT) as defined by staining with an α-galactosylceramide (αGalCer)-loaded CD1d-tetramer. iNKT cells from EBI3−/−mice exhibited decreased IL-4 and, to a lesser extent, IFN-γ production after αGalCer s…

T-Lymphocytesmedicine.medical_treatmentStimulationBiologyMinor Histocompatibility AntigensInterferon-gammaMiceTh2 CellsImmune systemmedicineAnimalsInterferon gammaReceptors CytokineInterleukin 4GlycoproteinsMultidisciplinaryInterleukinsEBI3Biological SciencesNatural killer T cellMolecular biologyMice Inbred C57BLCytokineImmunologyInterleukin-4CD8medicine.drugProceedings of the National Academy of Sciences
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Cutting Edge: A Key Pathogenic Role of IL-27 in T Cell- Mediated Hepatitis

2007

Abstract The signals driving T cell activation in T cell-mediated fulminant hepatitis are not fully understood. In this study, we identify the cytokine IL-27p28/EBI3 as a major pathogenic factor in the ConA model of T cell-mediated hepatitis. We found an up-regulation of hepatic EBI3 and p28 expression and augmented levels of IL-27 in wild-type mice after ConA administration, suggesting a potential pathogenic role of this cytokine in ConA hepatitis. Consistently, IL-27 EBI3-deficient mice were almost completely protected from ConA-induced liver damage. Such protection was associated with reduced levels of IFN-γ and its signaling proteins pSTAT-1 and T-bet. Finally, in vivo blockade of IL-27…

T-Lymphocytesmedicine.medical_treatmentT cellImmunologychemical and pharmacologic phenomenaBiologyMinor Histocompatibility AntigensInterferon-gammaMiceConcanavalin AmedicineAnimalsImmunology and AllergyReceptors CytokineReceptorFulminant hepatitisMice KnockoutHepatitisLiver injuryInterleukin-17EBI3medicine.diseaseUp-RegulationSTAT1 Transcription FactorCytokinemedicine.anatomical_structureImmunologyChemical and Drug Induced Liver InjurySignal transductionSignal TransductionThe Journal of Immunology
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Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor

2012

Facteur d'impact (5 ans) : 1,617Notoriété à 2 ans : Acceptable (biochem.res.methods); The sweet taste receptor is a heterodimeric receptor composed of the T1R2 and T1R3 subunits, while T1R1 and T1R3 assemble to form the umami taste receptor. T1R receptors belong to the family of class C G-protein coupled receptors (GPCRs). In addition to a transmembrane heptahelical domain, class C GPCRs have a large extracellular N-terminal domain (NTD), which is the primary ligand-binding site. The T1R2 and T1R1 subunits have been shown to be responsible for ligand binding, via their NTDs. However, little is known about the contribution of T1R3-NTD to receptor functions. To enable biophysical characteriza…

TASTE RECEPTORSucroseCircular dichroismcongenital hereditary and neonatal diseases and abnormalitiesProtein Conformation[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionumami receptorUmamiSWEETENERmedicine.disease_causeReceptors G-Protein-Coupledtaste03 medical and health sciencesGPCRTaste receptorPROTEIN REFOLDINGexpressionEscherichia colimedicineHumansRECOMBINANT GPCRbacteriaReceptorEscherichia coli030304 developmental biologyG protein-coupled receptorInclusion Bodies0303 health sciencesChemistrysweet receptor030302 biochemistry & molecular biologyRecombinant ProteinsTransmembrane proteinnervous system diseasesResearch NoteBACTERIAL EXPRESSIONBiochemistrysugarElectrophoresis Polyacrylamide GelHeterologous expression[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionrecombinant proteinProtein BindingBiotechnology
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Infectious Tolerance

2002

Regulatory CD4(+)CD25(+) T cells (Treg) are mandatory for maintaining immunologic self-tolerance. We demonstrate that the cell-cell contact-mediated suppression of conventional CD4(+) T cells by human CD25(+) Treg cells is fixation resistant, independent from membrane-bound TGF-beta but requires activation and protein synthesis of CD25(+) Treg cells. Coactivation of CD25(+) Treg cells with Treg cell-depleted CD4(+) T cells results in anergized CD4(+) T cells that in turn inhibit the activation of conventional, freshly isolated CD4(+) T helper (Th) cells. This infectious suppressive activity, transferred from CD25(+) Treg cells via cell contact, is cell contact-independent and partially medi…

TGF-βCD4-Positive T-Lymphocyteshuman regulatory T cellsT-LymphocytesImmunologyCellchemical and pharmacologic phenomenaIn Vitro TechniquesLymphocyte ActivationT-Lymphocytes RegulatoryImmune toleranceInterleukin 21AntigenTransforming Growth Factor betaCD4+CD25+ T cellsCell AdhesionImmune TolerancemedicineHumansImmunology and AllergyCytotoxic T cellIL-2 receptorbiologyBrief Definitive ReportModels ImmunologicalReceptors Interleukin-2hemic and immune systemsT-Lymphocytes Helper-InducerTransforming growth factor betainfectious tolerancemedicine.anatomical_structureT cell inhibitionImmunologyCancer researchbiology.proteinTransforming growth factorJournal of Experimental Medicine
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The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity

2012

SummaryRIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting chaperone protein, 14-3-3ε, as a RIG-I-binding partner and essential component of a translocation complex or “translocon” containing RIG-I, 14-3-3ε, and the TRIM25 ubiquitin ligase. The RIG-I translocon directs RIG-I redistribution from the cytosol to membranes where it mediates MAVS-dependent innate immune signaling during acute RNA virus infection. 14-3-3ε is essential for the stable inte…

TRIM25Cancer ResearchUbiquitin-Protein Ligasesviruseschemical and pharmacologic phenomenaHepacivirusMicrobiologyAntiviral AgentsModels BiologicalArticleCell LineDEAD-box RNA HelicasesTripartite Motif Proteins03 medical and health sciences0302 clinical medicineVirologyImmunology and Microbiology(all)Protein Interaction MappingHumansReceptors ImmunologicDEAD Box Protein 58Molecular Biology030304 developmental biology0303 health sciencesInnate immune systembiologyRIG-IRNAMembrane Proteinsvirus diseasesRNA virusbiochemical phenomena metabolism and nutritionbiology.organism_classificationTranslocon3. Good healthCell biology14-3-3 Proteins030220 oncology & carcinogenesisChaperone (protein)biology.proteinDEAD Box Protein 58Parasitologybiological phenomena cell phenomena and immunityMolecular ChaperonesProtein BindingTranscription FactorsCell Host & Microbe
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Talin1 sets the stage for dendritic cell activation

2020

In dendritic cells, talin1 links integrin binding to efficient TLR downstream signaling through interaction with MyD88 and PIP5K.

TalinCellular differentiationImmunologyIntegrinInsightsMiceConditional gene knockoutImmune ToleranceImmunology and AllergyAnimalsSkinMice KnockoutMembrane GlycoproteinsbiologyChemistryChemotaxisToll-Like ReceptorsNF-kappa BReceptors Interleukin-1Dendritic cellCell biologyPhosphotransferases (Alcohol Group Acceptor)Langerhans CellsMyeloid Differentiation Factor 88biology.proteinCytokinesSignal transductionSignal TransductionThe Journal of Experimental Medicine
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Activation of glycine receptors modulates spontaneous epileptiform activity in the immature rat hippocampus

2014

While the expression of glycine receptors in the immature hippocampus has been shown, no information about the role of glycine receptors in controlling the excitability in the immature CNS is available. Therefore, we examined the effect of glycinergic agonists and antagonists in the CA3 region of an intact corticohippocampal preparation of the immature (postnatal days 4-7) rat using field potential recordings. Bath application of 100 μM taurine or 10 μM glycine enhanced the occurrence of recurrent epileptiform activity induced by 20 μM 4-aminopyridine in low Mg(2+) solution. This proconvulsive effect was prevented by 3 μM strychnine or after incubation with the loop diuretic bumetanide (10 …

TaurinePhysiologyTaurineGlycinePharmacologyHippocampuschemistry.chemical_compoundNeuroscience: Development/Plasticity/RepairReceptors GlycinemedicineAnimalsRats WistarReceptorGlycine receptorCells CulturedEpilepsyChemistryGABAA receptorStrychnineRatsBiochemistrynervous systemAnimals NewbornGlycineGabazineAnticonvulsantsBumetanidemedicine.drug
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Structure-activity relationships of dimethindene derivatives as new M2-selective muscarinic receptor antagonists.

2003

A series of 2,3-disubstituted indenes, which are analogues of the widely used histamine H(1) receptor antagonist dimethindene, have been synthesized and studied as muscarinic and histamine receptor antagonists. The affinities of these compounds for the five human muscarinic receptor subtypes (M(1)-M(5)) and for human histamine H(1) receptors were determined in radioligand binding studies using membranes from transfected Chinese hamster ovary (CHO) cells and [(3)H]N-methylscopolamine ([(3)H]NMS). The results demonstrate that the diisopropyl analogue 19 has a similar high affinity as (S)-dimethindene at M(2) receptors ((S)-dimethindene: pK(i) = 7.52; (-)-19: pK(i) = 7.37) with an improved sel…

Tertiary amineStereochemistrymedicine.drug_classCHO CellsMuscarinic AntagonistsRadioligand AssayStructure-Activity RelationshipCricetinaeDrug DiscoveryMuscarinic acetylcholine receptormedicineAnimalsDimethindeneHumansReceptors Histamine H1ReceptorAcetylcholine receptorReceptor Muscarinic M2DimethindeneChemistryAntagonistStereoisomerismReceptor antagonistReceptors MuscarinicRadioligand AssayIndenesMolecular MedicineJournal of medicinal chemistry
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Nickel induces intracellular calcium mobilization and pathophysiological responses in human cultured airway epithelial cells.

2009

Abstract Environmental exposure to nickel is associated to respiratory disorders and potential toxicity in the lung but molecular mechanisms remain incompletely explored. The extracellular Ca 2+ -sensing receptor (CaSR) is widely distributed and may be activated by divalent cations. In this study, we investigated the presence of CaSR in human cultured airway epithelial cells and its activation by nickel. Nickel transiently increased intracellular calcium (−log EC 50  = 4.67 ± 0.06) in A549 and human bronchial epithelial cells as measured by epifluorescence microscopy. Nickel (20 μM)-induced calcium responses were reduced after thapsigargin or ryanodine exposure but not by Ca 2+ -free medium…

ThapsigarginInterleukin-1betachemistry.chemical_elementRespiratory MucosaBiologyCalciumToxicologyCalcium in biologychemistry.chemical_compoundNickelExtracellularHumansRNA Small InterferingCells CulturedA549 cellRyanodine receptorRyanodineTumor Necrosis Factor-alphaInositol trisphosphateEpithelial CellsGeneral MedicineEnvironmental exposureIntercellular Adhesion Molecule-1Cell biologychemistryMicroscopy FluorescenceType C PhospholipasesImmunologyGTP-Binding Protein alpha Subunits Gq-G11ThapsigarginCalciumReceptors Calcium-SensingChemico-biological interactions
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The designer cytokine hyper-interleukin-6 is a potent activator of STAT3-dependent gene transcription in vivo and in vitro.

1999

Interleukin-6 (IL-6) triggers pivotal pathways in vivo. The designer protein hyper-IL-6 (H-IL-6) fuses the soluble IL-6 receptor (sIL-6R) through an intermediate linker with IL-6. The intracellular pathways that are triggered by H-IL-6 are not defined yet. Therefore, we studied the molecular mechanisms leading to H-IL-6-dependent gene activation. H-IL-6 stimulates haptoglobin mRNA expression in HepG2 cells, which is transcriptionally mediated as assessed by run-off experiments. The increase in haptoglobin gene transcription correlates with higher nuclear translocation of tyrosine-phosphorylated STAT3 and its DNA binding. As H-IL-6 stimulates STAT3-dependent gene transcription, we compared t…

Therapeutic gene modulationSTAT3 Transcription FactorTranscriptional ActivationTranscription GeneticRecombinant Fusion ProteinsResponse elementE-boxBiologyTransfectionBiochemistryCell LineMiceSp3 transcription factorAntigens CDCytokine Receptor gp130E2F1AnimalsHumansRNA MessengerPhosphorylationMolecular BiologyCell NucleusATF3Sp1 transcription factorMice Inbred C3HMembrane GlycoproteinsHaptoglobinsInterleukin-6Liver receptor homolog-1Biological TransportCell BiologyDNAReceptors InterleukinMolecular biologyReceptors Interleukin-6DNA-Binding ProteinsGene Expression RegulationTrans-ActivatorsTyrosineThe Journal of biological chemistry
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