Search results for "cyclic AMP"

showing 10 items of 177 documents

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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Reciprocal regulation of human platelet function by endogenous prostanoids and through multiple prostanoid receptors

2014

Platelets are permanently exposed to a variety of prostanoids formed by blood cells or the vessel wall. The two major prostanoids, prostacyclin and thromboxane act through well established pathways mediated by their respective G-protein coupled receptors inhibiting or promoting platelet aggregation accordingly. Yet the role of other prostanoids and prostanoid receptors for platelet function regulation has not been thoroughly investigated. We aimed at a comprehensive analysis of prostanoid effects on platelets, the receptors and pathways involved and functional consequences. We analyzed cAMP formation and phosphorylation of proteins pivotal to platelet function as well as functional platelet…

Blood PlateletsSerotoninmedicine.medical_specialtyPlatelet AggregationProstaglandin E2 receptorReceptors ProstaglandinProstaglandinProstacyclinchemistry.chemical_compoundAdenosine TriphosphateP2Y12Internal medicineCyclic AMPmedicineHumansPlateletPlatelet activationReceptorMitogen-Activated Protein Kinase KinasesPharmacologyChemistryMicrofilament Proteinsrap1 GTP-Binding ProteinsProstanoidrespiratory systemPhosphoproteinsCell biologyAdenosine DiphosphateP-SelectinEndocrinologyProstaglandinscardiovascular systemCalciumlipids (amino acids peptides and proteins)Cell Adhesion Moleculesmedicine.drugEuropean Journal of Pharmacology
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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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Decrease of mRNA levels and biosynthesis of sucrase-isomaltase but not dipeptidylpeptidase IV in forskolin or monensin-treated Caco-2 cells.

1991

International audience; Treatment for 48 h of differentiated, confluent Caco-2 cells with 2.5 10(-5) M forskolin or 10(-6) M monensin, which produces a significant decrease of the de novo biosynthesis of sucrase-isomaltase, does not change quantitatively the de novo biosynthesis of dipeptidylpeptidase IV. Western blot analysis and silver nitrate staining indicate that neither drug induces any modification in the steady state expression of these two brush border hydrolases. Northern blot analysis shows that the level of dipeptidylpeptidase IV mRNA does not change in treated as compared to control Caco-2 cells. In contrast, forskolin and monensin dramatically decrease the level of sucrase-iso…

Brush borderDipeptidyl Peptidase 4Blotting WesternAdenocarcinomaBiology03 medical and health sciencesCellular and Molecular Neurosciencechemistry.chemical_compoundWestern blot[ CHIM.ORGA ] Chemical Sciences/Organic chemistryCyclic AMPTumor Cells CulturedmedicineHumansRNA MessengerNorthern blotMonensinDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMolecular Biology030304 developmental biologyPharmacology0303 health sciencesForskolinmedicine.diagnostic_test[CHIM.ORGA]Chemical Sciences/Organic chemistryColforsin030302 biochemistry & molecular biologyMonensinAntibodies MonoclonalCell BiologyMetabolismBlotting Northern[CHIM.ORGA] Chemical Sciences/Organic chemistrySucrase-Isomaltase ComplexGlucosechemistryBiochemistryCell cultureColonic NeoplasmsMolecular MedicineSucrase-isomaltase
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Cyclic AMP-mediated upregulation of the expression of neuronal NO synthase in human A673 neuroepithelioma cells results in a decrease in the level of…

2004

The expression level of neuronal nitric oxide synthase (nNOS) can vary depending on the (patho)physiological conditions. Here we document a marked induction of nNOS mRNA, protein, and total NO production in response to dibutyryl cyclic AMP (db-cAMP) in human A673 neuroepithelial cells. However, the upregulation of nNOS was associated with a decreased level of production of bioactive NO and by an increase in the level of generation of reactive oxygen species (ROS). ROS production could be prevented by the NOS inhibitor L-NAME, suggesting nNOS itself is involved in ROS generation. Sepiapterin supplementation of db-cAMP-treated A673 cells could restore full bioactive NO production, most likely…

CAMP-Responsive Element ModulatorNitric Oxide Synthase Type IBiologyCREBNitric OxideBiochemistryAdenylyl cyclaseCyclic AMP Response Element Modulatorchemistry.chemical_compoundMiceNeuroblastomaCoactivatorComplement C3b Inactivator ProteinsCyclic AMPAnimalsHumansNeuroectodermal Tumors Primitive PeripheralCREB-binding proteinEnzyme InhibitorsProtein kinase AeducationCyclic AMP Response Element-Binding ProteinGTP CyclohydrolaseCAMP response element bindingHomeodomain ProteinsNeuronseducation.field_of_studyForskolinPhosphoric Diester HydrolasesIntracellular Signaling Peptides and ProteinsBlood ProteinsLIM Domain ProteinsMolecular biologyCyclic AMP-Dependent Protein KinasesPterinsUp-RegulationDNA-Binding ProteinsRepressor ProteinsAntisense Elements (Genetics)NG-Nitroarginine Methyl EsterchemistryBucladesineGene Expression RegulationComplement Factor Hbiology.proteinNitric Oxide SynthaseReactive Oxygen SpeciesSignal TransductionBiochemistry
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Expression of metabotropic glutamate receptors in murine thymocytes and thymic stromal cells

2000

RT-PCR combined with immunoblotting showed the expression of group-I (mGlu1 and 5) and group-II (mGlu2 and 3) metabotropic glutamate receptors in whole mouse thymus, isolated thymocytes and TC-1S thymic stromal cell line. Cytofluorimetric analysis showed that mGlu-5 receptors were absent in CD4(-)/CD8(-) but present in more mature CD4(+) CD8(+) and CD4(+)CD8(-) thymocytes. mGlu-1a receptors showed an opposite pattern of expression with respect to mGlu5, whereas mGlu2/3 receptor expression did not differ between double negative and double positive cells. mGlu receptors expressed in both thymic cell components were functional, as indicated by measurements of polyphosphoinositide hydrolysis or…

CD4-Positive T-LymphocytesMalemedicine.medical_specialtyStromal cellNeuroimmunomodulationReceptor expressionBlotting WesternImmunologyGene ExpressionThymus GlandCD8-Positive T-LymphocytesReceptors Metabotropic GlutamateCell LineMicePhosphatidylinositol PhosphatesInternal medicineCyclic AMPmedicineAnimalsImmunology and AllergyCycloleucineRNA MessengerReceptorReverse Transcriptase Polymerase Chain ReactionChemistryMetabotropic glutamate receptor 5HydrolysisMetabotropic glutamate receptor 6Flow CytometryCell biologyMice Inbred C57BLNeuroprotective AgentsEndocrinologyMetabotropic receptormetabotropic glutamate receptors; tc-1s cells; thymocytesNeurologyMetabotropic glutamate receptorMetabotropic glutamate receptor 1Neurology (clinical)Stromal CellsSignal TransductionJournal of Neuroimmunology
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Postsynaptic Secretion of BDNF and NT-3 from Hippocampal Neurons Depends on Calcium–Calmodulin Kinase II Signaling and Proceeds via Delayed Fusion Po…

2007

The mammalian neurotrophins (NTs) NGF, BDNF, NT-3, and NT-4 constitute a family of secreted neuronal growth factors. In addition, NTs are implicated in several forms of activity-dependent synaptic plasticity. Although synaptic secretion of NTs has been described, the intracellular signaling cascades that regulate synaptic secretion of NTs are far from being understood. Analysis of NT secretion at the subcellular level is thus required to resolve the role of presynaptic and postsynaptic NT secretion for synaptic plasticity. Here, we transfected cultures of dissociated rat hippocampal neurons with green fluorescent protein-tagged versions of BDNF and NT-3, respectively, and identified NT vesi…

Calcium Channels L-TypeBiologyNeurotransmissionInhibitory postsynaptic potentialHippocampusReceptors N-Methyl-D-AspartateSynaptic TransmissionExocytosisNeurotrophin 3Postsynaptic potentialCa2+/calmodulin-dependent protein kinaseAnimalsCalcium SignalingNeuronsBrain-Derived Neurotrophic FactorGeneral NeuroscienceRyanodine Receptor Calcium Release ChannelLong-term potentiationArticlesCyclic AMP-Dependent Protein KinasesRatsCell biologynervous systemBiochemistryTrk receptorCalcium-Calmodulin-Dependent Protein KinasesSynapsesSynaptic plasticityThapsigarginCalcium-Calmodulin-Dependent Protein Kinase Type 2Postsynaptic densityThe Journal of Neuroscience
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Dibutyryl cyclic AMP and adrenaline increase contractile force and 45Ca uptake in mammalian cardiac muscle

1973

The effects of dibutyryl cyclic AMP (DB-AMP; 10−3M) and adrenaline (2.2×10−6 M) on contractile force, 45Ca uptake, and total myocardial Ca concentration were investigated in electrically driven left auricles isolated from rat hearts. The experiments were performed at an extracellular Ca concentration of 0.45 mM and at low frequency of stimulation (15 beats/min). 45Ca exposure was 5 min. Under the conditions used, both drugs increased contractile force and enhanced 45Ca uptake (expressed as relative specific activity) by about 30% (DB-AMP) and 40% (adrenaline), respectively. Thus, the results provide evidence that the effects of adrenaline on 45Ca uptake in mammalian cardiac muscle can be mi…

Calcium Isotopesmedicine.medical_specialtyContraction (grammar)Epinephrinechemistry.chemical_elementStimulationIn Vitro TechniquesCalciumInternal medicineCyclic AMPmedicineExtracellularAnimalsCa uptakeCardiac OutputPharmacologyMyocardiumCardiac muscleHeartGeneral MedicineDibutyryl Cyclic AMPRatsEndocrinologymedicine.anatomical_structurechemistryCalciumFemaleSpecific activityNaunyn-Schmiedeberg's Archives of Pharmacology
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Phosphorylation of carcinogen metabolizing enzymes: regulation of the phosphorylation status of the major phenobarbital inducible cytochromes P-450 i…

1989

We present data showing that the major phenobarbital inducible cytochromes P-450 (cytochrome P-450IIB1 and cytochrome P-450IIB2) were phosphorylated in intact hepatocytes. This phosphorylation was greatly increased by the cAMP derivatives N6-dibutyryl-cAMP and 8-thiomethyl-cAMP mediated by a cAMP-dependent protein kinase. Most importantly the phosphorylation status of cytochromes P-450 was shown to change in the hepatocytes after treatment with glucagon, which is known to increase the level of cAMP in hepatocytes. The observed impact of the hormone glucagon on the phosphorylation of distinct cytochrome P-450 forms in intact hepatocytes reveals the possibility that the enzyme activity of cyt…

Cancer ResearchCytochromeBlotting WesternGlucagonMixed Function OxygenasesCytochrome P-450 Enzyme SystemCyclic AMPmedicineAnimalsPhosphorylationEnzyme inducerProtein kinase AbiologyChemistryCytochrome P450General MedicineThionucleotidesGlucagonRatsmedicine.anatomical_structureBucladesineLiverBiochemistryPhenobarbitalHepatocytebiology.proteinPhosphorylationElectrophoresis Polyacrylamide GelPhenobarbitalmedicine.drugCarcinogenesis
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Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1

1999

The DNA repair protein apurinic endonuclease (APE/Ref-1) exerts several physiological functions such as cleavage of apurinic/apyrimidinic sites and redox regulation of the transcription factor AP-1, whose activation is part of the cellular response to DNA damaging treatments. Here we demonstrate that APE/Ref-1 is phosphorylated by casein kinase II (CKII). This was shown for both the recombinant APE/Ref-1 protein (Km=0.55 mM) and for APE/Ref-1 expressed in COS cells. Phosphorylation of APE/Ref-1 did not alter the repair activity of the enzyme, whereas it stimulated its redox capability towards AP-1, thus promoting DNA binding activity of AP-1. Inhibition of CKII mediated phosphorylation of A…

Cancer ResearchDNA RepairProto-Oncogene Proteins c-junDNA repairDNA damageCarbon-Oxygen LyasesCHO CellsProtein Serine-Threonine KinasesBiologyTransfectionSubstrate SpecificityCricetinaeDNA Repair ProteinDNA-(Apurinic or Apyrimidinic Site) LyaseGeneticsAnimalsHumansAP sitePhosphorylationCasein Kinase IIProtein kinase AMolecular BiologyMethyl MethanesulfonateCyclic AMP-Dependent Protein KinasesMolecular biologyDNA-(apurinic or apyrimidinic site) lyaseTranscription Factor AP-1COS CellsPhosphorylationCasein kinase 2Oxidation-ReductionDNA DamageHeLa CellsMutagensOncogene
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