Search results for "binding proteins"

showing 10 items of 911 documents

Interferon-α Suppresses cAMP to Disarm Human Regulatory T Cells

2013

Abstract IFN-α is an antineoplastic agent in the treatment of several solid and hematologic malignancies that exerts strong immune- and autoimmune-stimulating activity. However, the mechanisms of immune activation by IFN-α remain incompletely understood, particularly with regard to CD4+CD25highFoxp+ regulatory T cells (Treg). Here, we show that IFN-α deactivates the suppressive function of human Treg by downregulating their intracellular cAMP level. IFN-α–mediated Treg inactivation increased CD4+ effector T-cell activation and natural killer cell tumor cytotoxicity. Mechanistically, repression of cAMP in Treg was caused by IFN-α–induced MAP–ERK kinase (MEK)/extracellular signal-regulated ki…

MAPK/ERK pathwayCancer Researchmedicine.medical_treatmentGraft vs Host DiseaseAutoimmunitychemical and pharmacologic phenomenaBiologyLymphocyte ActivationT-Lymphocytes RegulatoryNatural killer cellMiceImmune systemDownregulation and upregulationT-Lymphocyte SubsetsCyclic AMPmedicineAnimalsHumansIL-2 receptorPhosphorylationExtracellular Signal-Regulated MAP KinasesCells CulturedMitogen-Activated Protein Kinase KinasesInterleukin-2 Receptor alpha SubunitInterferon-alphaFOXP3hemic and immune systemsDNA-Binding ProteinsKiller Cells NaturalSTAT Transcription Factorsmedicine.anatomical_structureCytokineOncologyHumanized mouseImmunologyCancer researchCancer Research
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Coupling of endothelin receptors to the ERK/MAP kinase pathway. Roles of palmitoylation and G(alpha)q.

2001

Endothelins are potent mitogens that stimulate extracellular signal-regulated kinases (ERK/MAP kinases) through their cognate G-protein-coupled receptors, ET(A) and ET(B). To address the role of post-translational ET receptor modifications such as acylation on ERK activation and to identify relevant downstream effectors coupling the ET receptor to the ERK signaling cascades we have constructed a panel of palmitoylation-deficient ET receptor mutants with differential G(alpha) protein binding capacity. Endothelin-1 stimulation of wild-type ET(A) or ET(B) induced a fivefold to sixfold increase in ERK in COS-7 and CHO cells whereas full-length nonpalmitoylated ET(A) and ET(B) mutants failed to …

MAPK/ERK pathwayGs alpha subunitInsectaMAP Kinase Signaling SystemBlotting WesternMolecular Sequence DataPalmitic AcidSRC Family Tyrosine KinaseBiochemistryCell LineCricetinaeArrestinTumor Cells CulturedAnimalsHumansAmino Acid SequenceReceptorMitogen-Activated Protein Kinase 1KinaseChemistryReceptors EndothelinCell MembraneHeterotrimeric GTP-Binding ProteinsCell biologyEnzyme ActivationErbB ReceptorsType C PhospholipasesCOS CellsMutationcardiovascular systemMutagenesis Site-DirectedPhosphorylationGTP-Binding Protein alpha Subunits Gq-G11Mitogen-Activated Protein KinasesProto-oncogene tyrosine-protein kinase SrcEuropean journal of biochemistry
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Down-regulation of human CYP3A4 by the inflammatory signal interleukin-6: molecular mechanism and transcription factors involved.

2002

The hepatic drug-metabolizing cytochrome P-450 (CYP) enzymes are down-regulated during inflammation. In vitro studies with hepatocytes have shown that the cytokines released during inflammatory responses are largely responsible for this CYP repression. However, the signaling pathways and the cytokine-activated factors involved remain to be properly identified. Our research has focused on the negative regulation of CYP3A4 (the major drug-metabolizing human CYP) by interleukin 6 (IL-6) (the principal regulator of the hepatic acute-phase response). CYP3A4 down-regulation by IL-6 requires activation of the glycoprotein receptor gp130; however, it does not proceed through the JAK/STAT pathway, a…

MAPK/ERK pathwaySTAT3 Transcription FactorMAP Kinase Signaling Systemp38 mitogen-activated protein kinasesDown-RegulationBiologyBiochemistryTransactivationCytochrome P-450 Enzyme SystemAntigens CDGeneticsCCAAT-Enhancer-Binding Protein-alphaCytokine Receptor gp130Tumor Cells CulturedCytochrome P-450 CYP3AHumansRNA MessengerSTAT3Molecular BiologyTranscription factorCells CulturedMembrane GlycoproteinsDose-Response Relationship DrugInterleukin-6Reverse Transcriptase Polymerase Chain ReactionCCAAT-Enhancer-Binding Protein-betaJAK-STAT signaling pathwayProtein-Tyrosine KinasesGlycoprotein 130Molecular biologyDNA-Binding ProteinsGene Expression Regulationbiology.proteinHepatocytesTrans-ActivatorsSignal transductionBiotechnologyAcute-Phase ProteinsSignal TransductionTranscription FactorsFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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A follow-up study of a genome-wide association scan identifies a susceptibility locus for venous thrombosis on chromosome 6p24.1.

2010

International audience; To identify genetic susceptibility factors conferring increased risk of venous thrombosis (VT), we conducted a multistage study, following results of a previously published GWAS that failed to detect loci for developing VT. Using a collection of 5862 cases with VT and 7112 healthy controls, we identified the HIVEP1 locus on chromosome 6p24.1 as a susceptibility locus for VT. Indeed, the HIVEP1 rs169713C allele was associated with an increased risk for VT, with an odds ratio of 1.20 (95% confidence interval 1.13-1.27, p = 2.86 x 10(-9)). HIVEP1 codes for a protein that participates in the transcriptional regulation of inflammatory target genes by binding specific DNA …

MESH : Transcription Factors[SDV]Life Sciences [q-bio]Genome-wide association study030204 cardiovascular system & hematologyMESH : Chromosomes Human Pair 60302 clinical medicineGenetics(clinical)Genetics (clinical)GeneticsVenous Thrombosis0303 health sciencesMESH: Polymorphism Single NucleotideMESH : Polymorphism Single NucleotideMESH: Genetic Predisposition to DiseaseMESH: Follow-Up StudiesMESH: Transcription FactorsMESH : Venous ThrombosisMESH: Case-Control StudiesDNA-Binding ProteinsChromosomes Human Pair 6MESH : DNA-Binding ProteinsErratumMESH : Genome-Wide Association StudyMESH : Case-Control StudiesMESH: Chromosomes Human Pair 6Locus (genetics)BiologyPolymorphism Single NucleotideGenetic determinism03 medical and health sciencesReportGenetic predispositionGeneticsHumansGenetic Predisposition to DiseaseAlleleGene030304 developmental biologyMESH: Humans[ SDV ] Life Sciences [q-bio]MESH : Humanslinking inflammation protein atherothrombosis sequence riskCase-control studyChromosomeMESH : Follow-Up StudiesCase-Control StudiesMESH: Genome-Wide Association StudyMESH: Venous ThrombosisMESH : Genetic Predisposition to Disease030217 neurology & neurosurgeryMESH: DNA-Binding ProteinsFollow-Up StudiesGenome-Wide Association StudyTranscription Factors
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The nuclear receptor PPARγ selectively inhibits Th17 differentiation in a T cell–intrinsic fashion and suppresses CNS autoimmunity

2009

T helper cells secreting interleukin (IL)-17 (Th17 cells) play a crucial role in autoimmune diseases like multiple sclerosis (MS). Th17 differentiation, which is induced by a combination of transforming growth factor (TGF)-beta/IL-6 or IL-21, requires expression of the transcription factor retinoic acid receptor-related orphan receptor gamma t (ROR gamma t). We identify the nuclear receptor peroxisome proliferator-activated receptor gamma (PPAR gamma) as a key negative regulator of human and mouse Th17 differentiation. PPAR gamma activation in CD4(+) T cells selectively suppressed Th17 differentiation, but not differentiation into Th1, Th2, or regulatory T cells. Control of Th17 differentia…

MESH: Nuclear Receptor Subfamily 1 Group F Member 3Helper-InducerReceptors Retinoic AcidT-LymphocytesMESH: Interleukin-17Cellular differentiationRetinoic AcidPeroxisome proliferator-activated receptorNeurodegenerativeInbred C57BLMedical and Health SciencesMiceInterleukin 210302 clinical medicineGroup FRAR-related orphan receptor gammaMESH: Nuclear Receptor Co-Repressor 2Receptors2.1 Biological and endogenous factorsThyroid HormoneImmunology and AllergyMESH: AnimalsAetiologyEncephalomyelitisPromoter Regions Geneticchemistry.chemical_classificationOrphan receptor0303 health sciencesReceptors Thyroid HormoneInterleukin-17Cell DifferentiationT-Lymphocytes Helper-InducerNuclear Receptor Subfamily 1 Group F Member 33. Good healthCell biologyDNA-Binding Proteinsmedicine.anatomical_structureMESH: Repressor Proteins[SDV.IMM]Life Sciences [q-bio]/ImmunologyInterleukin 17MESH: Cell Differentiationmedicine.medical_specialtyEncephalomyelitis Autoimmune ExperimentalMultiple SclerosisNuclear Receptor Subfamily 1Member 31.1 Normal biological development and functioningT cellImmunologyBiologyAutoimmune DiseasePromoter RegionsExperimental03 medical and health sciencesGeneticUnderpinning researchMESH: Mice Inbred C57BLInternal medicineMESH: Promoter Regions GeneticGeneticsmedicineAnimalsHumansNuclear Receptor Co-Repressor 2MESH: Receptors Thyroid HormoneMESH: T-Lymphocytes Helper-InducerMESH: Encephalomyelitis Autoimmune ExperimentalMESH: Mice030304 developmental biologyMESH: Receptors Retinoic AcidMESH: HumansInflammatory and immune systemNeurosciencesBrief Definitive ReportCorrectionMESH: Multiple SclerosisBrain DisordersMice Inbred C57BLPPAR gammaRepressor ProteinsEndocrinologyMESH: PPAR gammaNuclear receptorchemistryMESH: DNA-Binding Proteins030217 neurology & neurosurgeryAutoimmuneJournal of Experimental Medicine
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Cloning of Rac and Rho-GDI from tobacco using an heterologous two-hybrid screen.

2000

International audience; To examine whether molecular similarities exist between the animal and plant Rho GTPase signaling pathways, we have developed a heterologous two-hybrid screening method. By this technique, we have cloned a cDNA encoding a tobacco Rac-like protein able to interact with a mammalian Rho-GDI. In a second screen this tobacco Rac was used as a bait and a tobacco homologue of Rho-GDI was identified. These results show that some components of the animal and plant Rac signaling pathways are similar enough to allow their interaction in an heterologous approach. Moreover these data suggest a similar regulation of Rho GTPases in animals and plants.

MESH: Signal TransductionMESH: Plants ToxicMESH: Sequence Homology Amino Acid[SDV]Life Sciences [q-bio]Molecular Sequence DataMESH: rac GTP-Binding ProteinsMESH: Amino Acid SequenceMESH: Two-Hybrid System Techniques[SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunityMESH: Sequence AnalysisGene Expression Regulation PlantTwo-Hybrid System TechniquesTobacco[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumansrho-Specific Guanine Nucleotide Dissociation InhibitorsMESH: Guanine Nucleotide Dissociation InhibitorsMESH: Cloning Molecular[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMESH: rho-Specific Guanine Nucleotide Dissociation InhibitorsCloning MolecularMESH: Gene Expression Regulation PlantMESH: Tobacco[SDV.IMM.II] Life Sciences [q-bio]/Immunology/Innate immunityComputingMilieux_MISCELLANEOUSGuanine Nucleotide Dissociation InhibitorsPlant ProteinsMESH: HumansMESH: Molecular Sequence DataSequence Homology Amino AcidMESH: Plant ProteinsGENETIQUErac GTP-Binding Proteins[SDV] Life Sciences [q-bio]Plants ToxicSequence AnalysisSignal Transduction
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Caspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiation.

2006

Abstract Caspases have demonstrated several nonapoptotic functions including a role in the differentiation of specific cell types. Here, we show that caspase-8 is the upstream enzyme in the proteolytic caspase cascade whose activation is required for the differentiation of peripheral-blood monocytes into macrophages. On macrophage colony-stimulating factor (M-CSF) exposure, caspase-8 associates with the adaptor protein Fas-associated death domain (FADD), the serine/threonine kinase receptor-interacting protein 1 (RIP1) and the long isoform of FLICE-inhibitory protein FLIP. Overexpression of FADD accelerates the differentiation process that does not involve any death receptor. Active caspase…

Macrophage colony-stimulating factorCellular differentiationFas-Associated Death Domain ProteinImmunologyCaspase 8BiochemistryMonocytesArticle03 medical and health sciences0302 clinical medicineCell Line TumormedicineHumansFADDCaspase030304 developmental biologyDeath domain0303 health sciencesCaspase 8biologyMonocyteMacrophage Colony-Stimulating FactorMacrophagesNF-kappa BSignal transducing adaptor proteinRNA-Binding ProteinsCell DifferentiationCell BiologyHematologyMolecular biologyNuclear Pore Complex Proteinsmedicine.anatomical_structure030220 oncology & carcinogenesisbiology.proteinBlood
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Transient structural ordering of the RNA-binding domain of carnation mottle virus p7 movement protein modulates nucleic acid binding.

2005

Plant viral movement proteins bind to RNA and participate in the intra- and intercellular movement of the RNAs from plant viruses. However, the role and magnitude of the conformational changes associated with the formation of RNA-protein complexes are not yet defined. Here we describe studies on the relevance of a preexisting nascent alpha-helix at the C terminus of the RNA-binding domain of p7, a movement protein from carnation mottle virus, to RNA binding. Synthetic peptide analogues and single amino acid mutation at the RNA-binding domain of recombinant p7 protein were used to correlate the transient structural order in aqueous solution with RNA-binding potential.

Magnetic Resonance SpectroscopyMolecular Sequence DataBiochemistryViral ProteinsPlant virusAmino Acid SequenceBinding siteMovement proteinMolecular BiologyBinding SitesbiologyC-terminusOrganic ChemistryRNARNA-Binding Proteinsbiology.organism_classificationRecombinant ProteinsProtein Structure TertiarySpectrometry FluorescenceBiochemistryCarnation mottle virusMutationNucleic acidMolecular MedicineRNAPeptidesBinding domainChembiochem : a European journal of chemical biology
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De Novo Mutations in SLC25A24 Cause a Disorder Characterized by Early Aging, Bone Dysplasia, Characteristic Face, and Early Demise

2017

International audience; A series of simplex cases have been reported under various diagnoses sharing early aging, especially evident in congenitally decreased subcutaneous fat tissue and sparse hair, bone dysplasia of the skull and fingers, a distinctive facial gestalt, and prenatal and postnatal growth retardation. For historical reasons, we suggest naming the entity Fontaine syndrome. Exome sequencing of four unrelated affected individuals showed that all carried the de novo missense variant c.649C>T (p.Arg217Cys) or c.650G>A (p.Arg217His) in SLC25A24, a solute carrier 25 family member coding for calcium-binding mitochondrial carrier protein (SCaMC-1, also known as SLC25A24). SLC25A24 all…

Male0301 basic medicineAgingMitochondrionPetty syndromeAntiportersATP-Mg/Pi carriersAdenosine TriphosphateCytosol0302 clinical medicineAdenine nucleotideMissense mutation[ SDV.GEN.GH ] Life Sciences [q-bio]/Genetics/Human geneticsGenetics (clinical)Exome sequencingMembrane Potential MitochondrialGeneticsProgeriaATP synthaseSCaMC-1SyndromeMitochondria3. Good healthFemalemedicine.medical_specialtylipodystrophyMolecular Dynamics SimulationBiologyPhosphatesMitochondrial Proteins03 medical and health sciencesReportInternal medicineGeneticsmedicineHumansFetal DeathBone Diseases DevelopmentalAdenineSLC25A24Calcium-Binding ProteinsagingInfant NewbornInfantprogeriaFibroblastsmedicine.diseaseMitochondrial carrierSolute carrier familyOxygenprogeroid disorder030104 developmental biologyEndocrinology[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsMutationbiology.protein030217 neurology & neurosurgery
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The nucleotide excision repair protein XPC is essential for bulky DNA adducts to promote interleukin-6 expression via the activation of p38-SAPK

2016

Polycyclic aromatic hydrocarbons (PAHs) are environmental pollutants, and many are potent carcinogens. Benzo[a]pyrene (B[a]P), one of the best-studied PAHs, is metabolized ultimately to the genotoxin anti-B[a]P-7,8-dihydrodiol-9,10-epoxide (BPDE). BPDE triggers stress responses linked to gene expression, cell death and survival. So far, the underlying mechanisms that initiate these signal transduction cascades are unknown. Here we show that BPDE-induced DNA damage is recognized by DNA damage sensor proteins to induce activation of the stress-activated protein kinase (SAPK) p38. Surprisingly, the classical DNA damage response, which involves the kinases ATM and ATR, is not involved in p38-SA…

Male0301 basic medicineCancer ResearchDNA RepairCarcinogenesisDNA damagep38 mitogen-activated protein kinases78-Dihydro-78-dihydroxybenzo(a)pyrene 910-oxideBlotting WesternEnzyme-Linked Immunosorbent AssayBiologyReal-Time Polymerase Chain ReactionTransfectionp38 Mitogen-Activated Protein KinasesDNA AdductsMice03 medical and health scienceschemistry.chemical_compoundGeneticsmedicinepolycyclic compoundsAnimalsHumansRNA Small InterferingMolecular BiologyCarcinogenMice KnockoutCisplatinInterleukin-6KinaseFibroblastsCell biologyDNA-Binding ProteinsMice Inbred C57BL030104 developmental biologychemistryCarcinogensNIH 3T3 CellsCancer researchComet AssaySignal transductionDNADNA DamageHeLa CellsMutagensSignal Transductionmedicine.drugNucleotide excision repairOncogene
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