Search results for "GUANYLATE CYCLASE"

showing 7 items of 47 documents

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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Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors.

1999

The assembly of signalling molecules into macromolecular complexes (transducisomes) provides specificity, sensitivity and speed in intracellular signalling pathways. Rod photoreceptors in the eye contain an unusual set of glutamic-acid-rich proteins (GARPs) of unknown function. GARPs exist as two soluble forms, GARP1 and GARP2, and as a large cytoplasmic domain (GARP' part) of the beta-subunit of the cyclic GMP-gated channel. Here we identify GARPs as multivalent proteins that interact with the key players of cGMP signalling, phosphodiesterase and guanylate cyclase, and with a retina-specific ATP-binding cassette transporter (ABCR), through four, short, repetitive sequences. In electron mic…

genetic structuresPhosphodiesterase InhibitorsMolecular Sequence DataCyclic Nucleotide-Gated Cation ChannelsGlutamic AcidNerve Tissue ProteinsPlasma protein bindingBiologyIn Vitro TechniquesRetinal Rod Photoreceptor CellsAnimalsAmino Acid SequenceTransducinEye ProteinsPeptide sequenceCyclic GMPMultidisciplinaryPhosphoric Diester HydrolasesPhosphodiesteraseProteinsTransporterGlutamic acidRod Cell Outer SegmentRecombinant ProteinsCell biologyBiochemistryCytoplasmGuanylate CyclaseATP-Binding Cassette TransportersCattleTransducinSignal transductionProtein BindingSignal TransductionNature
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Adrenergic Stimulation of Cyclic GMP Formation Requires NO-Dependent Activation of Cytosolic Guanylate Cyclase in Rat Pinealocytes

1993

Cyclic GMP (cGMP) formation in rat pinealocytes is regulated through a synergistic dual receptor mechanism involving beta- and alpha 1-adrenergic receptors. The effects of NG-monomethyl-L-arginine (NMMA), which inhibits nitric oxide (NO) synthase and NO-mediated activation of cytosolic guanylate cyclase, and methylene blue (MB), which inhibits cytosolic guanylate cyclase, were investigated in an attempt to understand the role of NO in adrenergic cGMP formation. Both NMMA and MB inhibited beta-adrenergic stimulation of cGMP formation as well as alpha 1-adrenergic potentiation of beta-adrenergic stimulation of cGMP formation, whereas they had no effect in unstimulated pinealocytes. The inhibi…

medicine.medical_specialtyGUCY1B3AdrenergicStimulationArginineNitric OxidePineal GlandBiochemistryPinealocyteNitric oxideCellular and Molecular Neurosciencechemistry.chemical_compoundCytosolInternal medicinemedicineAnimalsSympathomimeticsCyclic GMPCells Culturedomega-N-MethylargininebiologyChemistryGUCY1A3Guanylate cyclase 2CRatsEnzyme ActivationMethylene BlueNitric oxide synthaseEndocrinologyGuanylate Cyclasebiology.proteinJournal of Neurochemistry
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Stabilization of Perivascular Mast Cells by Endothelial CNP (C-Type Natriuretic Peptide)

2020

Objective: Activated perivascular mast cells (MCs) participate in different cardiovascular diseases. Many factors provoking MC degranulation have been described, while physiological counterregulators are barely known. Endothelial CNP (C-type natriuretic peptide) participates in the maintenance of vascular barrier integrity, but the target cells and mechanisms are unclear. Here, we studied whether MCs are regulated by CNP. Approach and Results: In cultured human and murine MCs, CNP activated its specific GC (guanylyl cyclase)-B receptor and cyclic GMP signaling. This enhanced cyclic GMP–dependent phosphorylation of the cytoskeleton-associated VASP (vasodilator-stimulated phosphoprotein) and…

medicine.medical_specialtyMice 129 StrainMedizinMyocardial Reperfusion InjuryCell DegranulationCell LineMicrocirculationCapillary PermeabilityCyclic gmpAdenosine TriphosphateInternal medicineParacrine CommunicationmedicineAnimalsMast CellsPhosphorylationCyclic GMPMice KnockoutChemistryMicrofilament ProteinsDegranulationEndothelial CellsNatriuretic Peptide C-TypeThrombosisPhosphoproteinsMice Inbred C57BLDisease Models AnimalEndocrinologyNeutrophil InfiltrationC-type natriuretic peptideCardiology and Cardiovascular MedicineCell Adhesion MoleculesReceptors Atrial Natriuretic FactorSignal TransductionGuanylate cyclase
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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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Vasoactive intestinal peptide stimulation of cyclic guanosine monophosphate formation: further evidence for a role of nitric oxide synthase and cytos…

1993

In the rat pineal gland vasoactive intestinal peptide (VIP) and beta-adrenergic agonists stimulate cyclic guanosine monophosphate (cGMP) formation and their action is amplified by alpha 1-adrenergic agonists. Since beta-adrenergic stimulation of cGMP is suggested to involve activation of nitric oxide (NO) synthase and NO-mediated activation of cytosolic guanylate cyclase (GC), we investigated the effects of the NO synthase inhibitor N-monomethyl-L-arginine (L-NMMA) and of the cytosolic GC inhibitor methylene blue (MB) on VIP receptor-stimulated cGMP formation. Both L-NMMA and MB depressed VIP-induced cGMP formation as well as alpha 1-adrenergic potentiation of VIP-stimulated cGMP formation …

medicine.medical_specialtyVasoactive intestinal peptideArgininePineal GlandPinealocyteNitric oxidechemistry.chemical_compoundPhenylephrineEndocrinologyCytosolInternal medicinemedicineAnimalsCyclic guanosine monophosphateCyclic GMPomega-N-MethylarginineATP synthasebiologyDrug SynergismRatsNitric oxide synthaseMethylene BlueEndocrinologychemistryGuanylate CyclaseSecond messenger systembiology.proteinOmega-N-MethylarginineAmino Acid OxidoreductasesNitric Oxide Synthasehormones hormone substitutes and hormone antagonistsVasoactive Intestinal PeptideEndocrinology
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A single transient episode of hyperammonemia induces long-lasting alterations in protein kinase A.

2007

A single transient episode of hyperammonemia induces long-lasting alterations in protein kinase A. Am J Physiol Gastrointest Liver Physiol 292: G305-G314,2007; doi:10.1152/ajpgi.00100.2006.-Hepatic encephalopathy in patients with liver disease is associated with poor prognosis. This could be due to the induction by the transient episode of hepatic encephalopathy of long-lasting alterations making patients more susceptible. We show that a single transient episode of hyperammonemia induces long-lasting alterations in signal transduction. The content of the regulatory subunit of the protein kinase dependent on cAMP (PKA-RI) is increased in erythrocytes from cirrhotic patients. This increase is…

soluble guanylate cyclaseAdultLiver CirrhosisMalemedicine.medical_specialtyCirrhosisErythrocytesPhysiologyliver cirrhosisEncephalopathyhepatic encephalopathyBiologyHepatitisLiver diseaseLiver Function TestsReference ValuesPhysiology (medical)Internal medicinemedicineAnimalsHumansHyperammonemiaRats WistarProtein kinase AHepatic encephalopathyAgedHepatologyPortacaval anastomosisMetabolic disorderErythrocyte MembraneGastroenterologyAscitesHyperammonemiaMiddle Agedmedicine.diseaseCyclic AMP-Dependent Protein KinasesRatsDisease Models AnimalEndocrinologyChronic Diseaserat modelsFemaleLiver FailureAmerican journal of physiology. Gastrointestinal and liver physiology
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