Search results for "Cyclic GMP-Dependent Protein Kinases"

showing 7 items of 17 documents

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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Explaining the phenomenon of nitrate tolerance.

2005

During the last century, nitroglycerin has been the most commonly used antiischemic and antianginal agent. Unfortunately, after continuous application, its therapeutic efficacy rapidly vanishes. Neurohormonal activation of vasoconstrictor signals and intravascular volume expansion constitute early counter-regulatory responses (pseudotolerance), whereas long-term treatment induces intrinsic vascular changes, eg, a loss of nitrovasodilator-responsiveness (vascular tolerance). This is caused by increased vascular superoxide production and a supersensitivity to vasoconstrictors secondary to a tonic activation of protein kinase C. NADPH oxidase(s) and uncoupled endothelial nitric oxide synthase …

PhysiologyVasodilator AgentsPharmacologymedicine.disease_causeNitric OxideProstacyclin synthaseNitric oxidechemistry.chemical_compoundNitroglycerinSuperoxidesPeroxynitrous AcidmedicineCyclic GMP-Dependent Protein KinasesAnimalsHumansBiotransformationchemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologyChemistrySuperoxidePhosphoric Diester HydrolasesAldehyde Dehydrogenase MitochondrialDrug ToleranceAldehyde DehydrogenaseCyclic Nucleotide Phosphodiesterases Type 1VasodilationOxidative StressBiochemistryVasoconstrictioncardiovascular systembiology.proteinEndothelium VascularCardiology and Cardiovascular MedicineSoluble guanylyl cyclaseReactive Oxygen SpeciesPeroxynitriteOxidative stressSignal TransductionCirculation research
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Two distinct Ca2+ influx pathways activated by the bradykinin B2 receptor.

1996

The hormone-induced depletion of cellular Ca stores provides a signal for the Ca2+ influx into electrically non-excitable cells; however, the underlying molecular mechanisms remain elusive. Therefore, we analyzed bradykinin-activated Ca2+ influx into human foreskin fibroblast cells, HF-15, by fura-2 and 45Ca labeling to discriminate between Ca2+ influx into the fura-sensitive compartment and Ca uptake into fura-insensitive Ca stores. Bradykinin-activated CaZt influx into the fura-sensitive compartment was blocked by inhibitors of NO synthases. These inhibitors also suppressed bradykinin-activated increases in cGMP, indicating that the NO-dependent increase in cGMP is involved in the activat…

Receptor Bradykinin B2BradykininBradykininNitric OxideBiochemistryNitric oxideCell Linechemistry.chemical_compoundmedicineCyclic GMP-Dependent Protein KinasesHumansFibroblastCyclic GMPInterphaseFluorescent DyesIon TransportCell growthChemistryKinaseReceptors BradykininCa2 influxCompartment (chemistry)Calcium Channel BlockersCell biologymedicine.anatomical_structureBiochemistryCytoplasmCalciumFura-2Cell DivisionEuropean journal of biochemistry
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Biochemistry and pharmacology of novel anthranilic acid derivatives activating heme-oxidized soluble guanylyl cyclase.

2005

The heme-enzyme soluble guanylyl cyclase (sGC) is an ubiquitous NO receptor, which mediates NO downstream signaling by the generation of cGMP. We studied the mechanism of action of the anthranilic acid derivatives 5-chloro-2-(5-chloro-thiophene-2-sulfonylamino-N-(4-(morpholine-4-sulfonyl)-phenyl)-benzamide sodium salt (HMR1766) (proposed international nonproprietary name, ataciguat sodium) and 2-(4-chloro-phenylsulfonylamino)-4,5-dimethoxy-N-(4-(thiomorpholine-4-sulfonyl)-phenyl)-benzamide (S3448) as a new class of sGC agonists. Both compounds activated different sGC preparations (purified from bovine lung, or crude from human corpus cavernosum) in a concentration-dependent and quickly reve…

Vasodilator AgentsBlood PressureHemePharmacologychemistry.chemical_compoundEnzyme activatorAnthranilic acidmedicineCyclic GMP-Dependent Protein KinasesAnimalsortho-AminobenzoatesReceptorHemePharmacologySulfonamidesProtoporphyrin IXActivator (genetics)Enzyme ActivationchemistryMechanism of actionBiochemistryGuanylate CyclaseMolecular MedicineCattlemedicine.symptomSoluble guanylyl cyclaseOxidation-ReductionMolecular pharmacology
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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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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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NADPH Oxidase Accounts for Enhanced Superoxide Production and Impaired Endothelium-Dependent Smooth Muscle Relaxation in BKβ1 −/− Mice

2006

Objective— Nitric oxide (NO)-induced vasorelaxation involves activation of large conductance Ca 2+ -activated K + channels (BK). A regulatory BKβ1 subunit confers Ca 2+ , voltage, and NO/cGMP sensitivity to the BK channel. We investigated whether endothelial function and NO/cGMP signaling is affected by a deletion of the β1-subunit. Methods and Results— Vascular superoxide in BKβ1 −/− was measured using the fluorescent dye hydroethidine and lucigenin-enhanced chemiluminescence. Vascular NO formation was analyzed using electron paramagnetic resonance (EPR), expression of NADPH oxidase subunits, the endothelial NO synthase (eNOS), the soluble guanylyl cyclase (sGC), as well as the activity a…

medicine.medical_specialtyNitric Oxide Synthase Type IIIEndotheliumAorta ThoracicNitric OxideMuscle Smooth VascularNitric oxideMicechemistry.chemical_compoundSuperoxidesInternal medicineCyclic GMP-Dependent Protein KinasesmedicineAnimalsHumansProtein IsoformsNADH NADPH OxidoreductasesLarge-Conductance Calcium-Activated Potassium ChannelsMice KnockoutNADPH oxidasebiologySuperoxideMicrofilament ProteinsNADPH OxidasesPhosphoproteinsMolecular biologyVasodilationEndocrinologymedicine.anatomical_structurechemistryGuanylate CyclaseNAD(P)H oxidaseNOX1ApocyninNADPH Oxidase 1biology.proteinEndothelium VascularCardiology and Cardiovascular MedicineSoluble guanylyl cyclaseCell Adhesion MoleculesSignal TransductionArteriosclerosis, Thrombosis, and Vascular Biology
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