Search results for "channels"

showing 10 items of 411 documents

Xenopus Oocyte’s Conductance for Bioactive Compounds Screening and Characterization

2019

Background: Astaxanthin (ATX) is a lipophilic compound found in many marine organisms. Studies have shown that ATX has many strong biological properties, including antioxidant, antiviral, anticancer, cardiovascular, anti-inflammatory, neuro-protective and anti-diabetic activities. However, no research has elucidated the effect of ATX on ionic channels. ATX can be extracted from shrimp by-products. Our work aims to characterize ATX cell targets to lend value to marine by-products. Methods: We used the Xenopus oocytes cell model to characterize the pharmacological target of ATX among endogenous Xenopus oocytes&rsquo

AntioxidantSodiummedicine.medical_treatmentXenopuschemistry.chemical_elementEndogeny+Sodium ChannelsCatalysisArticleAmilorideInorganic Chemistrylcsh:ChemistryXenopus laevischemistry.chemical_compoundXenopus oocyte INaAstaxanthinDrug DiscoverymedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyIC50lcsh:QH301-705.5SpectroscopyXenopus oocyte INa+Biological Productsbioactive compoundsbiologySodium channelOrganic Chemistry<i>Xenopus</i> oocyte INa<sup>+</sup>marine natural productsGeneral Medicinebiology.organism_classificationElectrophysiological PhenomenaComputer Science ApplicationsShrimpastaxanthinchemistryBiochemistrylcsh:Biology (General)lcsh:QD1-999OocytesInternational Journal of Molecular Sciences
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Opposite vascular activity of (R)-apomorphine and its oxidised derivatives. Endothelium-dependent vasoconstriction induced by the auto-oxidation meta…

2003

We have synthetised a series of oxidised apomorphine derivatives (orto and para quinones 2-5), in order to analyse their vascular activity. We have performed radioligand binding assays on rat cortical membranes and functional studies on rat aortic rings. Instead the relaxant activity exhibited by (R)-apomorphine, o-quinones 2, 4, show contractile activity dependent on endothelium in rat aortic rings. Compound 2, the main metabolite of (R)-apomorphine auto-oxidation, was the product which showed enhanced contractile activity by a complex mechanism related to activation of Ca(2+) channels through release and/or inhibition of endothelial factors. Moreover, this compound disrupts the endothelia…

ApomorphineCalcium Channels L-TypeEndotheliumMetaboliteRadioligand Assaychemistry.chemical_compoundDrug DiscoverymedicineAnimalsVasoconstrictor AgentsEnzyme InhibitorsRats WistarAortaCerebral CortexPharmacologyDose-Response Relationship DrugbiologyOrganic ChemistryQuinonesStereoisomerismGeneral MedicineReceptors Adrenergic alphaReceptors GABA-AAcetylcholineIn vitroRatsApomorphineNitric oxide synthasemedicine.anatomical_structureBiochemistrychemistryVasoconstrictionBiophysicsbiology.proteinFemaleEndothelium VascularNitric Oxide Synthasemedicine.symptomOxidation-ReductionVasoconstrictionAcetylcholineBlood vesselmedicine.drugEuropean Journal of Medicinal Chemistry
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Superoxide Flux in Endothelial Cells via the Chloride Channel-3 Mediates Intracellular Signaling

2007

Reactive oxygen species (ROS) have been implicated in both cell signaling and pathology. A major source of ROS in endothelial cells is NADPH oxidase, which generates superoxide (O2.−) on the extracellular side of the plasma membrane but can result in intracellular signaling. To study possible transmembrane flux of O2.−, pulmonary microvascular endothelial cells were preloaded with the O2.−-sensitive fluorophore hydroethidine (HE). Application of an extracellular bolus of O2.−resulted in rapid and concentration-dependent transient HE oxidation that was followed by a progressive and nonreversible increase in nuclear HE fluorescence. These fluorescence changes were inhibited by superoxide dism…

ApoptosisMembrane PotentialsSuperoxide dismutasechemistry.chemical_compoundChloride ChannelsSuperoxidesExtracellularAnimalsHumansEnzyme InhibitorsRNA Small InterferingMolecular BiologyLungCells CulturedFluorescent Dyeschemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologySuperoxideAngiotensin IIThrombinAcetophenonesEndothelial CellsNADPH OxidasesCell BiologyArticlesCell biologyMitochondriaPhenanthridinesOxygenchemistryDIDSbiology.proteinCalciumSignal transductionOxidation-ReductionIntracellularSignal Transduction
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Vascular Activity of (-)-Anonaine, (-)-Roemerine and (-)-Pukateine, Three Natural 6a(R)-1,2-Methylenedioxyaporphines with Different Affinities for α1…

2004

We have studied the mechanism of action of three 6a( R)-1,2-methylenedioxyaporphines as vasorelaxant compounds. The alkaloids assayed showed different affinities for the three human cloned alpha (1)-adrenoceptor (AR) subtypes stably expressed in rat-1 fibroblasts, showing lower affinity for alpha(1B)-AR with regard to the alpha(1A)- or alpha(1D)-subtypes. These three natural compounds are more potent inhibitors of [ (3)H]-prazosin binding than of [ (3)H]-diltiazem binding to rat cerebral cortical membranes. As all these alkaloids inhibited noradrenaline (NA)-induced [ (3)H]-inositol phosphate formation in cerebral cortex and rat tail artery, they may be safely viewed as alpha (1)-AR antagon…

AporphinesPhosphodiesterase InhibitorsStereochemistryPharmaceutical ScienceAorta ThoracicDioxolesBiologyMuscle Smooth VascularAnalytical ChemistryHydroxylationchemistry.chemical_compoundAlkaloidsDrug DiscoverymedicineAnonaineAnimalsHumansAporphineRats WistarBinding sitePukateineCerebral CortexPharmacologyPlants MedicinalVoltage-dependent calcium channelAlkaloidOrganic ChemistryArteriesReceptors Adrenergic alphaIsoquinolinesRatsComplementary and alternative medicineMechanism of actionchemistryMolecular MedicineFemaleCalcium Channelsmedicine.symptomDrugs Chinese HerbalPhytotherapyPlanta Medica
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Arginine-rich peptides are blockers of VR-1 channels with analgesic activity

2000

Vanilloid receptors (VRs) play a fundamental role in the transduction of peripheral tissue injury and/or inflammation responses. Molecules that antagonize VR channel activity may act as selective and potent analgesics. We report that synthetic arginine-rich hexapeptides block heterologously expressed VR-1 channels with submicromolar efficacy in a weak voltage-dependent manner, consistent with a binding site located near/at the entryway of the aqueous pore. Dynorphins, natural arginine-rich peptides, also blocked VR-1 activity with micromolar affinity. Notably, synthetic and natural arginine-rich peptides attenuated the ocular irritation produced by topical capsaicin application onto the eye…

ArginineReceptors DrugBiophysicsTRPV Cation ChannelsPainDynorphinPharmacologyArginineEyeDynorphinsBiochemistryInhibitory Concentration 50MiceXenopus laevisDynorphinchemistry.chemical_compoundStructural BiologyNon-competitive antagonistGeneticsAnimalsChannel blockerAmino Acid SequenceBinding siteReceptorMolecular BiologyNon-competitive antagonistAnalgesicsChemistryElectric ConductivityNociceptorCell BiologyCapsaicinIonic poreOocytesNociceptorCapsaicinPeptidesFEBS Letters
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Distal Arthrogryposis type 5 in an Italian family due to an autosomal dominant gain-of-function mutation of the PIEZO2 gene

2022

Abstract Background Arthrogryposis multiplex congenita (AMC) is a group of clinically and etiologically heterogeneous conditions, characterized by prenatal onset contractures affecting two or more joints. Its incidence is about 1 in 3000 live births. AMC may be distinguished into amyoplasia, distal and syndromic arthrogryposis. Distal arthrogryposis (DA) predominantly affects hands and feet. It is currently divided into more than ten subtypes (DA1, DA2A/B, DA3–10), based on clinical manifestations, gene mutations and inheritance pattern. Among them, only a few patients with DA5 have been reported. It is associated to a gain-of-function pathogenic variant of the PIEZO2 gene, encoding for an …

ArthrogryposisContractureOphthalmoplegiaArthrogryposis multiplex congenita Case report DA5 Gain-of-function mutation NGS Ophthalmoplegia PIEZO2 gene Gain of Function Mutation Humans Infant Newborn Inheritance Patterns Ion Channels Mutation Pedigree Retinal Diseases Arthrogryposis Contracture OphthalmoplegiaRetinal DiseasesGain of Function MutationMutationInfant NewbornInheritance PatternsHumansGeneral MedicineIon ChannelsPedigreeItalian Journal of Pediatrics
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Non-adrenergic non-cholinergic nerve-mediated inhibitory control of pigeon oesophageal muscle.

1996

Pigeon oesophageal smooth muscle in vitro has spontaneous electromechanical activity. In the presence of atropine and guanethidine, electrical field stimulation evokes a transient TTX-sensitive response comprising inhibition of electric bursting activity and muscular relaxation. This NANC inhibitory response was analysed using the K+ channel blockers TEA and apamin, TEA perfusion (0.1-5 mM) induced a concentration-dependent reduction in amplitude of EFS-evoked relaxation. Responses to higher stimulation frequencies were more sensitive to TEA than those to lower ones. The maximum reduction in amplitude (29% of control) was obtained on 30 Hz EFS evoked responses during 5 mM TEA perfusion. In …

AtropineGuanethidinemedicine.medical_specialtyPotassium ChannelsPhysiologyStimulationTetrodotoxinBiologyInhibitory postsynaptic potentialApaminchemistry.chemical_compoundEsophagusPhysiology (medical)Internal medicinemedicineAnimalsChannel blockerColumbidaeEvoked PotentialsGuanethidineDose-Response Relationship DrugTetraethylammoniumMuscle SmoothNeural InhibitionGeneral MedicineTetraethylammonium CompoundsElectrophysiologyAtropineEndocrinologychemistryApaminPerfusionmedicine.drugArchives of physiology and biochemistry
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The Low-Affinity ATP Binding Site of the Escherichia coli SecA Dimer Is Localized at the Subunit Interface

1997

The homodimeric SecA protein is the ATP-dependent force generator in the Escherichia coli precursor protein translocation cascade. SecA contains two essential nucleotide binding sites (NBSs), i.e., NBS1 and NBS2 that hind ATP with high and low affinity, respectively. The photoactivatable bifunctional cross-linking agent 3'-arylazido-8-azidoadenosine 5'-triphosphate (diN(3)ATP) was used to investigate the spatial arrangement of the nucleotide binding sites of SecA, DiN(3)ATP is an authentic ATP analogue as it supports SecA-dependent precursor protein translocation and translocation ATPase, UV-induced photo-cross-linking of the diN(3)ATP-bound SecA results in the formation of stable dimeric s…

AzidesUltraviolet RaysProtein subunitATPaseDimerMutantPhotoaffinity LabelsBiologymedicine.disease_causeESSENTIAL COMPONENTenvironment and public healthBiochemistryBACILLUS-SUBTILISchemistry.chemical_compoundAdenosine TriphosphateBacterial ProteinsPROTON MOTIVE FORCEEscherichia colimedicinePRECURSOR PROTEIN TRANSLOCATIONNucleotideBinding siteEscherichia coliAdenosine Triphosphataseschemistry.chemical_classificationBinding SitesSecA ProteinsNucleotidesChemiosmosisEscherichia coli ProteinsMembrane Transport ProteinsPHOTOAFFINITY CROSS-LINKINGCross-Linking ReagentschemistryBiochemistryMEMBRANE-VESICLES REQUIRESPLASMA-MEMBRANE3'-ARYLAZIDO-BETA-ALANYL-8-AZIDO ATPCYTOPLASMIC MEMBRANEbiology.proteinPREPROTEIN TRANSLOCASEbacteriaDimerizationSEC Translocation ChannelsBiochemistry
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11,12-EET Stimulates the Association of BK Channel α and β1 Subunits in Mitochondria to Induce Pulmonary Vasoconstriction

2012

In the systemic circulation, 11,12-epoxyeicosatrienoic acid (11,12-EET) elicits nitric oxide (NO)- and prostacyclin-independent vascular relaxation, partially through the activation of large conductance Ca(2+)-activated potassium (BK) channels. However, in the lung 11,12-EET contributes to hypoxia-induced pulmonary vasoconstriction. Since pulmonary artery smooth muscle cells also express BK channels, we assessed the consequences of BKβ(1) subunit deletion on pulmonary responsiveness to 11,12-EET as well as to acute hypoxia. In buffer-perfused mouse lungs, hypoxia increased pulmonary artery pressure and this was significantly enhanced in the presence of NO synthase (NOS) and cyclooxygenase (…

BK channelAnatomy and PhysiologyLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsRespiratory Systemlcsh:MedicineCardiovascularCardiovascular SystemBiochemistryIon ChannelsMembrane PotentialsMice81114-Eicosatrienoic AcidHypoxic pulmonary vasoconstrictionHypoxiaLarge-Conductance Calcium-Activated Potassium Channel alpha Subunitslcsh:ScienceLungEnergy-Producing OrganellesEpoxide HydrolasesMembrane Potential MitochondrialMembrane potentialMultidisciplinarybiologyChemistryDepolarizationHyperpolarization (biology)IberiotoxinMitochondriaBiochemistryCirculatory Physiologycardiovascular systemMedicinelipids (amino acids peptides and proteins)medicine.symptomResearch ArticleCell Physiologymedicine.medical_specialtyPulmonary ArteryBioenergeticsCardiovascular PharmacologyInternal medicinemedicineAnimalsHumansArterial Pressureddc:610Protein InteractionsBiologylcsh:RProteinsCalcium-activated potassium channelMice Inbred C57BLHEK293 CellsEndocrinologyVasoconstrictionbiology.proteinlcsh:QGene DeletionVasoconstrictionPLoS ONE
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Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus alpha-toxin in planar lipid bilayers.

2000

Staphylococcal alpha-toxin forms homo-oligomeric channels in lipid bilayers and cell membranes. Here, we report that electrophysiological monitoring of single-channel function using a derivatized cysteine substitution mutant allows accurate determination of the subunit stoichiometry of the oligomer in situ. The electrophysiological phenotype of channels formed in planar lipid bilayers with the cysteine replacement mutant I7C is equal to that of the wild type. When pores were formed with I7C, alterations of several channel properties were observed upon modification with SH reagents. Decreases in conductance then occurred that were seen only as negative voltage was applied. At the level of si…

Bacterial ToxinsLipid BilayersWild typeConductanceBiologyMicrobiologyOligomerIon ChannelsElectrophysiologychemistry.chemical_compoundHemolysin ProteinsStructure-Activity RelationshipMembranechemistryBiochemistryMutationBiophysicsCysteineLipid bilayerMolecular BiologyIon channelStaphylococcus aureus alpha toxinCysteineMolecular microbiology
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