Search results for "Enzyme Activation"

showing 10 items of 304 documents

H7, a protein kinase C inhibitor, increases the glutathione content of neuroblastoma cells

1992

AbstractIt is shown that the intracellular glutathione (GSH) concentration of neuroblastoma-2a cells in culture increases with a maximum at 24 h after starting treatment with 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H7), an inhibitor of protein kinase C (PKC). Other inhibitors of this and other protein kinases, e.g. sphingosine, staurosporine, and HA 1004, at the concentrations tested, had a less marked or negligible effect on intracellular GSH concentration. 12-O-Tetradecanoylphorbol-13-acetate (TPA) was also tested and showed no significant effect 24 h after addition.

BiophysicsBiologyBiochemistryPiperazinesCellular differentiationchemistry.chemical_compoundMiceNeuroblastomaAlkaloidsStructural BiologySphingosineProtein kinase C1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineGeneticsmedicineTumor Cells CulturedStaurosporineAnimalsNeuroblastoma cellMolecular BiologyProtein kinase CSulfonamidesSphingosineKinaseCell BiologyGlutathioneIsoquinolinesStaurosporineMolecular biologyGlutathioneEnzyme ActivationBiochemistrychemistryEnzyme inhibitor1-(5-Isoquinolinylsulfonyl)-2-methylpiperazine1-(5-Isoquinolinesulfonyl)-2-Methylpiperazinebiology.proteinH7Intracellularmedicine.drugFEBS Letters
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AT1-receptor blockade by telmisartan upregulates GTP-cyclohydrolase I and protects eNOS in diabetic rats.

2008

Several enzymatic sources of reactive oxygen species (ROS) were described as potential reasons of eNOS uncoupling in diabetes mellitus. In the present study, we investigated the effects of AT1-receptor blockade with chronic telmisartan (25 mg/kg/day, 6.5 weeks) therapy on expression of the BH4-synthesizing enzyme GTP-cyclohydrolase I (GCH-I), eNOS uncoupling, and endothelial dysfunction in streptozotocin (STZ, 60 mg/kg iv, 7 weeks)-induced diabetes mellitus (type I). Telmisartan therapy did not modify blood glucose and body weight. Aortas from diabetic animals had vascular dysfunction as revealed by isometric tension studies (acetylcholine and nitroglycerin potency). Vascular and cardiac RO…

Blood GlucoseMalemedicine.medical_specialtyNitric Oxide Synthase Type IIImedicine.disease_causeBiochemistryBenzoatesReceptor Angiotensin Type 1chemistry.chemical_compoundEnosPhysiology (medical)Internal medicinemedicineDiabetes MellitusAnimalsTelmisartanEndothelial dysfunctionRats WistarXanthine oxidaseGTP CyclohydrolaseNADPH oxidasebiologySuperoxideBody WeightNADPH Oxidasesmedicine.diseaseStreptozotocinbiology.organism_classificationMitochondriaRatsUp-RegulationEnzyme ActivationOxidative StressEndocrinologychemistrybiology.proteinBenzimidazolesTelmisartanAngiotensin II Type 1 Receptor BlockersOxidative stressmedicine.drugFree radical biologymedicine
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Activation of cGMP-dependent Protein Kinase Iβ Inhibits Interleukin 2 Release and Proliferation of T Cell Receptor-stimulated Human Peripheral T Cells

2000

Several major functions of type I cGMP-dependent protein kinase (cGK I) have been established in smooth muscle cells, platelets, endothelial cells, and cardiac myocytes. Here we demonstrate that cGK Ibeta is endogenously expressed in freshly purified human peripheral blood T lymphocytes and inhibits their proliferation and interleukin 2 release. Incubation of human T cells with the NO donor, sodium nitroprusside, or the membrane-permeant cGMP analogs PET-cGMP and 8-pCPT-cGMP, activated cGK I and produced (i) a distinct pattern of phosphorylation of vasodilator-stimulated phosphoprotein, (ii) stimulation of the mitogen-activated protein kinases ERK1/2 and p38 kinase, and, upon anti-CD3 stimu…

Blood PlateletsNitroprussideInterleukin 2Cell Membrane PermeabilityCD3 ComplexT-Lymphocytesp38 mitogen-activated protein kinasesT cellReceptors Antigen T-CellCell SeparationBiologyLymphocyte ActivationBiochemistryJurkat cellsJurkat CellsCyclic AMPCyclic GMP-Dependent Protein KinasesmedicineHumansProtein kinase ACyclic GMPMolecular BiologyCyclic GMP-Dependent Protein Kinase Type IKinaseCell growthMicrofilament ProteinsCell BiologyPhosphoproteinsMolecular biologyCell biologyEnzyme ActivationAlternative Splicingmedicine.anatomical_structureInterleukin-2Mitogen-Activated Protein KinasesCell Adhesion MoleculescGMP-dependent protein kinasemedicine.drugJournal of Biological Chemistry
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Phosphorylation of CalDAG-GEFI by protein kinase A prevents Rap1b activation.

2013

Summary Background Signaling via protein kinase A (PKA) and protein kinase G (PKG) is critical for maintaining platelets in the resting state. Both kinases down-regulate the activity of the small GTPase Rap1b, a critical signaling switch for integrin activation and platelet aggregation. However, the mechanism of Rap1b regulation by PKA and PKG is largely unknown. Objective To identify the PKA phosphorylation sites in calcium and diacylglycerol-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), the main GEF for Rap1b in platelets, and the effect of CalDAG-GEFI phosphorylation in Rap1b activation. Methods The phosphorylation sites in CalDAG-GEFI were identified by radio-active phos…

Blood PlateletsPlatelet AggregationMolecular Sequence DataBiologyMass SpectrometryPhosphorylation cascadeCyclic AMPGuanine Nucleotide Exchange FactorsHumansImmunoprecipitationProtein phosphorylationAmino Acid SequenceCalcium SignalingPhosphorylationProtein kinase ACalcium signalingAlanineSequence Homology Amino AcidKinaseHematologyCyclic AMP-Dependent Protein KinasesEnzyme Activationrab1 GTP-Binding ProteinsHEK293 CellsBiochemistryMutationPhosphorylationGuanine nucleotide exchange factorGuanosine TriphosphatecGMP-dependent protein kinasePlasmidsSignal TransductionJournal of thrombosis and haemostasis : JTH
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Deciphering of ADP-induced, phosphotyrosine-dependent signaling networks in human platelets by Src-homology 2 region (SH2)-profiling.

2012

Tyrosine phosphorylation plays a central role in signal transduction controlling many important biological processes. In platelets, the activity of several signaling proteins is controlled by tyrosine phosphorylation ensuring proper platelet activation and aggregation essential for regulation of the delicate balance between bleeding and hemostasis. Here, we applied Src-homology 2 region (SH2)-profiling for deciphering of the phosphotyrosine state of human platelets activated by adenosine diphosphate (ADP). Applying a panel of 31 SH2-domains, rapid and complex regulation of the phosphotyrosine state of platelets was observed after ADP stimulation. Specific inhibition of platelet P2Y receptor…

Blood PlateletsProtein tyrosine phosphataseSH2 domainBiochemistryReceptor tyrosine kinasePhosphorylation cascadesrc Homology Domainschemistry.chemical_compoundReceptors Purinergic P2Y1Tandem Mass SpectrometryHumansProtease-activated receptorProtein phosphorylationIloprostPhosphorylationPhosphotyrosineMolecular BiologybiologyTyrosine phosphorylationPlatelet ActivationCyclic AMP-Dependent Protein KinasesAdenosine MonophosphateReceptors Purinergic P2Y12Cell biologyAdenosine DiphosphateEnzyme ActivationBiochemistrychemistrybiology.proteinPurinergic P2Y Receptor AntagonistsPhosphorylationProtein Processing Post-TranslationalSignal TransductionProteomics
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Synergistic interaction of adenylate cyclase activators and nitric oxide donor SIN-1 on platelet cyclic AMP

1995

Abstract The molecular mechanism of the synergistic platelet inhibition by activators of adenylate cyclase and guanylate cyclase in human platelets was investigated. The adenylate cyclase activators iloprost and prostaglandin E 1 and the guanylate cyclase activator 3-morpholino-synonimine (SIN-1) dose-dependently inhibited thrombin-induced aggregation of washed human platelets. Furthermore, SIN-1 at a concentration inhibiting platelet aggregation by only 10% shifted the IC 50 values of iloprost and prostaglandin E 1 by one order of magnitude to the left, indicating a synergistic action of adenylate cyclase and guanylate cyclase activators. Iloprost and prostaglandin E 1 dose-dependently ele…

Blood Plateletsmedicine.medical_specialtyGUCY1B3Platelet Aggregationmedicine.medical_treatmentAdenylate kinaseIn Vitro TechniquesNitric OxideCyclasechemistry.chemical_compoundInternal medicineCyclic AMPmedicineHumansPlateletIloprostAlprostadilCyclic GMPPharmacologyForskolinGUCY1A3PhosphodiesteraseDrug SynergismEnzyme ActivationEndocrinologychemistryGuanylate CyclaseMolsidominelipids (amino acids peptides and proteins)Platelet Aggregation InhibitorsAdenylyl CyclasesProstaglandin EEuropean Journal of Pharmacology: Molecular Pharmacology
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Microglial involvement in neuroplastic changes following focal brain ischemia in rats.

2009

The pathogenesis of ischemic stroke is a complex sequence of events including inflammatory reaction, for which the microglia appears to be a major cellular contributor. However, whether post-ischemic activation of microglial cells has beneficial or detrimental effects remains to be elucidated, in particular on long term brain plasticity events. The objective of our study was to determine, through modulation of post-stroke inflammatory response, to what extent microglial cells are involved in some specific events of neuronal plasticity, neurite outgrowth and synaptogenesis. Since microglia is a source of neurotrophic factors, the identification of the brain-derived neurophic factor (BDNF) as…

Brain InfarctionMaleTime FactorsNeuriteSciencePoly (ADP-Ribose) Polymerase-1SynaptophysinSynaptogenesisCell CountEnzyme-Linked Immunosorbent AssayNerve Tissue ProteinsBrain damageBiologyBrain IschemiaProinflammatory cytokineBrain ischemiaGAP-43 ProteinNeurotrophic factorsNeuroscience/Neuronal Signaling MechanismsmedicineAnimalsRats WistarCD11b AntigenNeuronal PlasticityMultidisciplinaryMicrogliaNeuroscience/Neuronal and Glial Cell BiologyBrain-Derived Neurotrophic FactorQRNeurological Disorders/Cerebrovascular DiseaseAntigens NuclearMacrophage Activationmedicine.diseaseImmunohistochemistryNeuroregenerationRatsEnzyme ActivationProtein Transportmedicine.anatomical_structureBenzamidesImmunologyMedicineMicrogliaPoly(ADP-ribose) Polymerasesmedicine.symptomNeuroscienceResearch ArticleNeurosciencePLoS ONE
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Analysis of parathyroid graft rejection suggests alloantigen-specific production of nitric oxide by iNOS-positive intragraft macrophages

2009

Abstract Background During acute rejection of organ or tissue allografts T cells and macrophages are dominant infiltrating cells. CD4-positive T cells are important for the induction of allograft rejection and macrophages are important effector cells mediating cytotoxicity via production of nitric oxide (NO) by the inducible NO-synthase (iNOS). In the present study we analysed whether the destruction of primarily nonvascularised parathyroid allografts is also mediated by iNOS-positive macrophages. Methods Hypocalcaemic Lewis rats received parathyroid isografts (from Lewis donors) and allografts (from Wistar Furth donors), respectively, under the kidney capsule. Levels of serum calcium above…

CD4-Positive T-LymphocytesGraft RejectionMaleImmunologyThyroid GlandNitric Oxide Synthase Type IIRats Inbred WFInflammationCell CommunicationLymphocyte ActivationMajor histocompatibility complexNitric oxidechemistry.chemical_compoundAntigenCell MovementHistocompatibility AntigensmedicineAnimalsTransplantation HomologousImmunology and AllergyCytotoxic T cellMacrophageTransplantationbiologyChemistryMacrophage ActivationAntigens DifferentiationPeptide FragmentsRatsEnzyme ActivationTransplantationMononuclear cell infiltrationGene Expression RegulationRats Inbred LewImmunologyDisease ProgressionMacrophages Peritonealbiology.proteinCalciumImmunizationmedicine.symptomTransplant Immunology
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β-Catenin Signaling Drives Differentiation and Proinflammatory Function of IRF8-Dependent Dendritic Cells

2014

Abstract β-Catenin signaling has recently been tied to the emergence of tolerogenic dendritic cells (DCs). In this article, we demonstrate a novel role for β-catenin in directing DC subset development through IFN regulatory factor 8 (IRF8) activation. We found that splenic DC precursors express β-catenin, and DCs from mice with CD11c-specific constitutive β-catenin activation upregulated IRF8 through targeting of the Irf8 promoter, leading to in vivo expansion of IRF8-dependent CD8α+, plasmacytoid, and CD103+CD11b− DCs. β-Catenin–stabilized CD8α+ DCs secreted elevated IL-12 upon in vitro microbial stimulation, and pharmacological β-catenin inhibition blocked this response in wild-type cells…

CD8 AntigensCellular differentiationImmunologyReceptors Cell SurfaceVaccinia virusPyrimidinonesCD8-Positive T-LymphocytesBiologyParasite LoadArticleProinflammatory cytokineMiceAntigens CDVacciniaAnimalsImmunology and AllergyPromoter Regions Geneticbeta CateninInflammationMice KnockoutCell DifferentiationDendritic CellsT lymphocyteTh1 CellsBridged Bicyclo Compounds HeterocyclicInterleukin-12CD11c AntigenCell biologyEnzyme ActivationMice Inbred C57BLInterferon Regulatory FactorsInterleukin 12FemaleIRF8Signal transductionIntegrin alpha ChainsToxoplasmaSpleenToxoplasmosisCD8Signal TransductionInterferon regulatory factorsThe Journal of Immunology
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Novel pathway in Bcr-Abl signal transduction involves Akt-independent, PLC-γ1-driven activation of mTOR/p70S6-kinase pathway

2009

In chronic myeloid leukemia, activation of the phosphoinositide 3-kinase (PI3K)/Akt pathway is crucial for survival and proliferation of leukemic cells. Essential downstream molecules involve mammalian target of rapamycin (mTOR) and S6-kinase. Here, we present a comprehensive analysis of the molecular events involved in activation of these key signaling pathways. We provide evidence for a previously unrecognized phospholipase C-gamma1 (PLC-gamma1)-controlled mechanism of mTOR/p70S6-kinase activation, which operates in parallel to the classical Akt-dependent machinery. Short-term imatinib treatment of Bcr-Abl-positive cells caused dephosphorylation of p70S6-K and S6-protein without inactivat…

Cancer ResearchBlotting WesternMedizinFusion Proteins bcr-ablApoptosisProtein Serine-Threonine KinasesBiologyPiperazinesMiceLeukemia Myelogenous Chronic BCR-ABL Positivehemic and lymphatic diseasesGeneticsAnimalsHumansRNA Small InterferingProtein Kinase InhibitorsMolecular BiologyProtein kinase BCAMKPI3K/AKT/mTOR pathwayPhospholipase C gammaCell growthKinaseTOR Serine-Threonine KinasesRPTORIntracellular Signaling Peptides and ProteinsRibosomal Protein S6 Kinases 70-kDaCell biologyEnzyme ActivationPyrimidinesBenzamidesembryonic structuresImatinib MesylateCancer researchPhosphorylationSignal transductionProto-Oncogene Proteins c-aktSignal TransductionOncogene
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