Search results for "cGMP-dependent protein kinase"

showing 9 items of 9 documents

Pharmacological modulation of protein kinases as a new approach to treat addiction to cocaine and opiates.

2016

Drug addiction shares brain mechanisms and molecular substrates with learning and memory processes, such as the stimulation of glutamate receptors and their downstream signalling pathways. In the present work we provide an up-to-date review of studies that have demonstrated the implication of the main memory-related calcium-dependent protein kinases in opiate and cocaine addiction. The effects of these drugs of abuse in different animal models of drug reward, dependence and addiction are altered by manipulation of the mitogen-activated protein kinase (MAPK) family, particularly extracellular signal regulated kinase (ERK), calcium/calmodulin-dependent kinase II (CaMKII), the protein kinase C…

0301 basic medicineMAPK/ERK pathwaymedia_common.quotation_subjectIntracellular SpacePharmacology03 medical and health sciencesCocaine-Related Disorders0302 clinical medicineCa2+/calmodulin-dependent protein kinaseMedicineAnimalsHumansProtein kinase AProtein kinase Cmedia_commonPharmacologybusiness.industryKinaseAddictionCyclin-dependent kinase 5Opioid-Related Disorders030104 developmental biologybusinesscGMP-dependent protein kinaseProtein Kinases030217 neurology & neurosurgeryEuropean journal of pharmacology
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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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Effects of inhibitors of cGMP-dependent protein kinase in atrial heart and aortic smooth muscle from rats

1995

Several activators of cGMP-dependent protein kinase (protein kinase G) such as 8-Br-cGMP reduced force of contraction in rat left atria. Inhibitors of protein kinase G antagonized the negative inotropic effect of 8-Br-cGMP but not of acetylcholine in atria. However, the acetylcholine-induced relaxation in aortic rings was significantly inhibited by protein kinase G inhibition. It is concluded that the reduction by 8-Br-cGMP of force of contraction in atria is related to activation of protein kinase G. In response to acetylcholine, activation of protein kinase G is probably a major step in smooth muscle relaxation but is not involved in the reduction of force of contraction in atria.

medicine.medical_specialtyContraction (grammar)Muscle RelaxationAorta ThoracicIn Vitro TechniquesMuscle Smooth VascularIsometric ContractionInternal medicineCyclic GMP-Dependent Protein KinasesmedicineAnimalsHeart AtriaProtein kinase ACyclic GMPRho-associated protein kinasePharmacologybiologyHeartMyocardial ContractionAcetylcholineRatsEnzyme ActivationEndocrinologyEnzyme inhibitorSecond messenger systemcardiovascular systembiology.proteinmedicine.symptomcGMP-dependent protein kinaseAcetylcholineMuscle Contractionmedicine.drugMuscle contractionEuropean Journal of Pharmacology
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Potential and limitations of PKA/ PKG inhibitors for platelet studies

2021

Cyclic nucleotides (cAMP and cGMP) and corresponding protein kinases, protein kinase A (PKA) and protein kinase G (PKG), are the main intracellular mediators of endothelium-derived platelet inhibitors. Pharmacological PKA/PKG inhibitors are often used to discriminate between these two kinase activities and to analyze their underlying mechanisms. Previously we showed that all widely used PKG inhibitors (KT5823, DT3, RP isomers) either did not inhibit PKG or inhibited and even activated platelets independently from PKG. In this study, we examined several PKA inhibitors as well as inhibitors of adenylate and guanylate cyclases to reveal their effects on platelets and establish whether they are…

Blood PlateletsKinaseIntracellular Signaling Peptides and ProteinsAdenylate kinaseHematologyGeneral MedicineKT5720Cyclic AMP-Dependent Protein Kinaseschemistry.chemical_compoundchemistryBiochemistryCyclic AMPCyclic GMP-Dependent Protein Kinasescardiovascular systemHumansPlateletPlatelet activationProtein kinase ACyclic GMPcGMP-dependent protein kinaseIntracellularPlatelets
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Increased protein kinase A regulatory subunit content and cGMP binding in erythrocyte membranes in liver cirrhosis

2003

Abstract Background/Aims : Patients with liver disease show increased plasma cGMP and decreased intracellular cGMP in lymphocytes. The initial aim of this work was to assess whether decreased intracellular cGMP and increased plasma cGMP may be due to increased ATP-dependent release of cGMP from cells. The results obtained led to a new aim: to identify and quantify a protein responsible for the increased cGMP binding found in erythrocyte membranes from patients with liver disease. Methods : ATP-dependent cGMP transport was determined in inside-out vesicles from erythrocyte membranes. cGMP-binding proteins were isolated from the membranes and identified by MALDI-TOF peptide mass fingerprint. …

AdultLiver CirrhosisMalemedicine.medical_specialtyProtein subunitPhosphodiesterase 3Biological Transport ActiveIn Vitro TechniquesBiologyInternal medicinemedicineHumansProtein kinase ACyclic GMPAgedCGMP bindingHepatologyErythrocyte MembraneMiddle AgedCyclic AMP-Dependent Protein KinasesMolecular WeightKineticsProtein SubunitsEndocrinologyCase-Control StudiesSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationCGMP transportbiology.proteinFemaleProtein AcGMP-dependent protein kinaseIntracellularJournal of Hepatology
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Receptor identification and physiological characterisation of glucagon-like peptide-2 in the rat heart.

2010

Abstract Background and aims The anorexigenic glucagon-like peptide (GLP)-2 is produced by intestinal L cells and released in response to food intake. It affects intestinal function involving G-protein-coupled receptors. To verify whether GLP-2 acts as a cardiac modulator in mammals, we analysed, in the rat heart, the expression of GLP-2 receptors and the myocardial and coronary responses to GLP-2. Methods and results GLP-2 receptors were detected on ventricular extracts by quantitative real-time polymerase chain reaction (Q-RT-PCR) and Western blotting. Cardiac GLP-2 effects were analysed on Langendorff perfused hearts. Intracellular GLP-2 signalling was investigated on Langendorff perfuse…

Maleendocrine systemmedicine.medical_specialtyCardiotonic AgentsNitric Oxide Synthase Type IIIMAP Kinase Signaling SystemG proteinEndocrinology Diabetes and MetabolismBlotting WesternMedicine (miscellaneous)Enzyme-Linked Immunosorbent AssayStimulationIn Vitro TechniquesBiologyReal-Time Polymerase Chain Reactionglucagon-like peptides-2 gut peptides cardiac performanceSettore BIO/09 - FisiologiaGlucagon-Like Peptide-1 Receptorchemistry.chemical_compoundInternal medicineCyclic AMPCyclic GMP-Dependent Protein KinasesGlucagon-Like Peptide 2Receptors GlucagonmedicineAnimalsCyclic adenosine monophosphatePhosphorylationRats WistarReceptorNutrition and Dieteticsdigestive oral and skin physiologyHeartPeptide FragmentsRatsPhospholambanEndocrinologyGene Expression RegulationchemistryInotropismGlucagon-Like Peptide-2 ReceptorCardiology and Cardiovascular MedicinecGMP-dependent protein kinasehormones hormone substitutes and hormone antagonistsIntestinal L CellsSignal Transduction
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Inhibition of ovarian steroidogenesis by cyclic-GMP in a fly

2003

1479-6805 0022-0795; Previous investigations in the female blowfly Phormia regina have shown that 3-isobutyl-1-methylxanthine (IBMX), a broad spectrum inhibitor of phosphodiesterases (PDEs), fails to mimic the steroidogenic effects of cAMP on ovaries, although it efficiently increases the concentrations of this second messenger. In this study, experiments carried out to clear up this contradiction demonstrated that IBMX, besides its effect on cAMP, also increased cGMP concentrations in blowfly ovary and that these two cyclic nucleotides controlled ovarian steroidogenesis antagonistically. In particular, a selective inhibitor of cGMP-specific PDEs, unlike IBMX, had a very strong negative eff…

medicine.medical_specialtyIBMXIndolesPhosphodiesterase InhibitorsEndocrinology Diabetes and MetabolismCarbazolesOvarySteroid biosynthesisBiologychemistry.chemical_compoundEndocrinologyAlkaloidsOrgan Culture TechniquesInternal medicine1-Methyl-3-isobutylxanthinemedicineCyclic AMPCyclic GMP-Dependent Protein KinasesAnimalsAutocrine signallingCyclic GMPAdenineDipteraColforsinOvaryPhosphodiesteraseBrainEcdysteroidsStimulation ChemicalEndocrinologymedicine.anatomical_structurechemistrySecond messenger systemQuinazolinesFemalePDE10ACalcium ChannelscGMP-dependent protein kinaseSignal Transduction
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The evolution of nitric oxide signalling diverges between the animal and the green lineages

2019

AbstractNitric oxide (NO) is a ubiquitous signalling molecule with widespread distribution in prokaryotes and eukaryotes where it is involved in countless physiological processes. While the mechanisms governing nitric oxide (NO) synthesis and signalling are well established in animals, the situation is less clear in the green lineage. Recent investigations have shown that NO synthase, the major enzymatic source for NO in animals, is absent in land plants but present in a limited number of algae. The first detailed analysis highlighted that these new NO synthases are functional but display specific structural features and probably original catalytic activities. Completing this picture, analy…

[SDE] Environmental Sciences0106 biological sciencesAlgaePhysiologyLineage (evolution)[SDV]Life Sciences [q-bio]RegulatorPlant ScienceSignalling01 natural sciencesNitric oxideEvolution Molecular03 medical and health scienceschemistry.chemical_compoundcyclic nucleotide-gated channel[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyAnimals[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyPhosphodiesteraseCyclic GMPComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesCGMPbiologyMechanism (biology)KinaseNitric oxide synthaseNitric oxidePlantPlantsGuanylate cyclaseCell biology[SDV] Life Sciences [q-bio]Nitric oxide synthaseSignallingchemistrycGMP-dependent protein kinase[SDE]Environmental Sciencesbiology.proteincGMP-dependent protein kinase010606 plant biology & botanySignal Transduction
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