Search results for "CGMP"

showing 10 items of 27 documents

Type 5 phosphodiesterase (PDE5) and the vascular tree: from embryogenesis to aging and disease

2020

Highlights • Vascular development depends on the timely differentiation of endothelial and smooth muscle cells, that mutually influence their developmental fate. • Endothelial and vascular smooth muscle cell (VSMC) compartments can mutually influence cell and tissue modifications during vascular aging and in vascular disease. • Keeping in mind that PDE5 is mainly expressed in VSMCs, we surveyed the literature on the role of PDE5 in vascular development, aging and disease. • Although most results have been obtained by PDE5 pharmacological inhibition, no data are available, to date, on vascular development, aging or disease following PDE5 genetic ablation.

0301 basic medicineCell typeAgingVascular smooth muscleMyocytes Smooth MuscleVSMCsEmbryonic DevelopmentECsContext (language use)DiseaseBiologyMuscle Smooth VascularArticle03 medical and health sciences0302 clinical medicinenitric oxidevascular smooth muscle cellsHumansBioresorbable vascular scaffoldCyclic Nucleotide Phosphodiesterases Type 5ECEmbryogenesisPhosphodiesteraseVascular agingCell biologycGMPSettore MED/23ECs; PDE5; VSMCs; cGMP; nitric oxide030104 developmental biologyVascular aging; vascular smooth muscle cells; phosphodiesterasePDE5phosphodiesterase030217 neurology & neurosurgeryFunction (biology)Developmental Biology
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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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Regulation of cyclooxygenase-2 expression by cyclic AMP.

2007

Abstract Prostaglandins (PG) regulate many biological processes, among others inflammatory reactions. Cyclooxygenases-1 and -2 (COX-1 and COX-2) catalyse PG synthesis. Since this step is rate limiting, the regulation of COX expression is of critical importance to PG biology. Contrary to COX-1, which is constitutively expressed, COX-2 expression is subject to regulation. For example, COX-2 levels are increased in inflammatory reactions. Many signalling pathways can regulate COX-2 expression, not least those involving receptors for COX products themselves. Analysis of the intracellular signal transducers involved reveals a crucial role for cAMP, albeit as a modulator rather than direct induce…

Cell typeMessenger RNAProstaglandinPhosphodiesteraseCell BiologyBiologyCREBGene Expression Regulation EnzymologiccGMPBiochemistryCyclooxygenase 2cAMPbiology.proteincAMP-responsive elementCyclic AMPAdenylate cyclaseAnimalsHumansPhosphodiesteraseCyclooxygenaseReceptorMolecular BiologyGeneIntracellularSignal TransductionBiochimica et biophysica acta
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Role of K+ and Ca2+ fluxes in the cerebroarterial vasoactive effects of sildenafil

2007

The aim of this study was to assess the role of K(+) and Ca(2+) fluxes in the cerebroarterial vasoactive effects of the phosphodiesterase-5 inhibitor sildenafil. We used isolated rabbit basilar arteries to assess the effects of extracellular K(+) raising on sildenafil-induced vasodilatation, and studied the pharmacological interaction of sildenafil with selective modulators of membrane K(+) and Ca(2+) channels. Expression of Kv1 subunits of K(+) channels was assessed at messenger and protein levels. Parallel experiments were carried out with zaprinast for comparison. Sildenafil (10 nM-0.1 mM) induced concentration-dependent relaxation of endothelin-1 (10 nM)-precontracted arteries, which wa…

Malemedicine.medical_specialtyCalcium Channels L-Typemedicine.drug_mechanism_of_actionPhosphodiesterase InhibitorsVasodilationIn Vitro TechniquesPharmacologyPiperazinesSildenafil Citratechemistry.chemical_compoundInternal medicinemedicineAnimalsChannel blockerRNA MessengerSulfonesPharmacologyTetraethylammoniumDose-Response Relationship DrugChemistryDepolarization3-Pyridinecarboxylic acid 14-dihydro-26-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)- Methyl esterIberiotoxinEndocrinologyPurinesBasilar ArterycGMP-specific phosphodiesterase type 5PotassiumShaker Superfamily of Potassium ChannelsCalciumRabbitsZaprinastPhosphodiesterase 5 inhibitorEuropean 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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Nitric oxide synthases: regulation and function

2011

Nitric oxide (NO), the smallest signalling molecule known, is produced by three isoforms of NO synthase (NOS; EC 1.14.13.39). They all utilize l-arginine and molecular oxygen as substrates and require the cofactors reduced nicotinamide-adenine-dinucleotide phosphate (NADPH), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), and (6R-)5,6,7,8-tetrahydrobiopterin (BH(4)). All NOS bind calmodulin and contain haem. Neuronal NOS (nNOS, NOS I) is constitutively expressed in central and peripheral neurons and some other cell types. Its functions include synaptic plasticity in the central nervous system (CNS), central regulation of blood pressure, smooth muscle relaxation, and vasodila…

medicine.medical_specialtyNitric Oxide Synthase Type IIIEndotheliumNeovascularization PhysiologicNitric Oxide Synthase Type IIVasodilationNitric Oxide Synthase Type IReviewArginineNitric OxideEndothelial NOSNitric oxideMicechemistry.chemical_compoundEnosInternal medicineRenin–angiotensin systemmedicineAnimalsHumansbiologybusiness.industryCardiovascular AgentsGenetic Therapybiology.organism_classificationBiopterinIsoenzymesNitric oxide synthaseEndocrinologymedicine.anatomical_structurechemistryCardiovascular DiseasescGMP-specific phosphodiesterase type 5biology.proteinEndothelium VascularHydroxymethylglutaryl-CoA Reductase InhibitorsNitric Oxide SynthaseCardiology and Cardiovascular MedicinebusinessEuropean Heart Journal
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Alteraciones de la neurotransmisión en hipocampo de ratas hiperamonémicas. papel de la neuroinflamación. modulación por GMPc extracelular

2021

La Encefalopatía Hepática (EH) es un síndrome neuropsiquiátrico complejo producido por un fallo hepático. Cuando el hígado falla se producen hiperamonemia (HA) e inflamación que actúan sinérgicamente produciendo neuroinflamación, lo que da lugar a alteraciones en la neurotransmisión y alteraciones cognitivas y motoras. Estudios anteriores del grupo han demostrado que el aumento de los niveles de GMPc extracelular disminuye la neuroinflamación y revierte las alteraciones cognitivas y motoras observadas en ratas hiperamonémicas. Sin embargo, los mecanismos responsables se desconocían. En la presente tesis doctoral hemos demostrado que la hiperamonemia crónica reduce la respuesta de los recept…

GABAextracellular cGMPnervous systemhyperammonemiaNMDAAMPAUNESCO::CIENCIAS DE LA VIDA:CIENCIAS DE LA VIDA [UNESCO]neuroinflammation
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Effects of nitric oxide-active drugs on the discharge of subthalamic neurons: microiontophoretic evidence in the rat.

2006

The presence of nitric oxide (NO) synthase and of soluble guanylyl cyclase, the main NO-activated metabolic pathway, has been demonstrated in many cells of the subthalamic nucleus. In this study, the effects induced on the firing of 96 subthalamic neurons by microiontophoretically administering drugs modifying NO neurotransmission were explored in anaesthetized rats. Recorded neurons were classified into regularly and irregularly discharging on the basis of their firing pattern. Nω-nitro-l-arginine methyl ester (L-NAME; a NO synthase inhibitor), 3-morpholino-sydnonimin-hydrocloride (SIN-1; a NO donor), S-nitroso-glutathione (SNOG; another NO donor) and 8-Br-cGMP (a cell-permeable analogue o…

MaleTime FactorsAction PotentialsNeurotransmissionInhibitory postsynaptic potentialNitric OxideSettore BIO/09 - FisiologiaNitric oxideS-Nitrosoglutathionechemistry.chemical_compoundSubthalamic NucleusAnimalsNitric Oxide DonorsEnzyme InhibitorsRats WistarCyclic GMPNeuronsAnalysis of VarianceIontophoresisDose-Response Relationship DrugChemistryGeneral Neuroscience8-Br-cGMP L-NAME SIN-1 SNOG subthalamic nucleusIontophoresisThionucleotidesRatsEnzyme ActivationSubthalamic nucleusNG-Nitroarginine Methyl EsterMolsidomineS-NitrosoglutathioneExcitatory postsynaptic potentialSoluble guanylyl cyclaseNeuroscience
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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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