Search results for "Nicotinic acetylcholine receptor"

showing 10 items of 50 documents

Photoaffinity labeling of Torpedo acetylcholine receptor by physostigmine.

1993

The plant alkaloid physostigmine, an established anti-cholinesterase agent of the carbamate type, has recently been shown to bind to the nicotinic acetylcholine receptor from Torpedo marmorata electrocytes [Okonjo, K. O., Kuhlmann, J.Maelicke, A. (1991) Eur. J. Biochem. 200, 671-677]. Pharmacological studies of physostigmine-induced ion flux into nicotinic-acetylcholine-receptor-rich membrane vesicles, indicated distinct binding sites for physostigmine and acetylcholine. As shown in this study by photoaffinity labeling with [phenyl-(n)-3H](-)physostigmine, the physostigmine-binding site is located within the same subunit (alpha polypeptide) of the receptor as the acetylcholine-binding site.…

PhysostigmineStereochemistryPhotochemistryUltraviolet RaysPhysostigmineMolecular Sequence DataReceptors NicotinicTorpedoTritiumBiochemistrylaw.inventionlawmedicineAnimalsAmino Acid SequenceAcetylcholine receptorBinding SitesPhotoaffinity labelingChemistryAffinity LabelsBungarotoxinLigand (biochemistry)Nicotinic acetylcholine receptorBiochemistryTorpedoAcetylcholinemedicine.drugEuropean journal of biochemistry
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Expression and renaturation of the N-terminal extracellular domain of torpedo nicotinic acetylcholine receptor alpha-subunit.

1998

The N-terminal extracellular region (amino acids 1-209) of the alpha-subunit of the nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata electric tissue was expressed as inclusion bodies in Escherichia coli using the pET 3a vector. Employing a novel protocol of unfolding and refolding, in the absence of detergent, a water-soluble globular protein of 25 kDa was obtained displaying approximately 15% alpha-helical and 45% beta-structure. The fragment bound alpha-[3H]bungarotoxin in 1:1 stoichiometry with a KD value of 0.5 nM as determined from kinetic measurements (4 nM from equilibrium binding). The kinetics of association of toxin and fragment were of second order, with a similar …

Protein DenaturationProtein FoldingMolecular Sequence DataReceptors NicotinicTorpedoBiochemistrylaw.inventionchemistry.chemical_compoundGanglion type nicotinic receptorlawExtracellularmedicineEscherichia coliAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyMethyllycaconitineCell BiologyBungarotoxinBungarotoxinsRecombinant ProteinsNicotinic acetylcholine receptorBiochemistrychemistryAlpha-4 beta-2 nicotinic receptorTorpedoAcetylcholinemedicine.drugProtein BindingThe Journal of biological chemistry
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Species- and Subtype-Specific Recognition by Antibody WF6 of a Sequence Segment Forming an α-Bungarotoxin Binding Site on the Nicotinic Acetylcholine…

1992

The monoclonal antibody WF6 competes with acetylcholine and alpha-bungarotoxin (alpha-BGT) for binding to the Torpedo nicotinic acetylcholine receptor (nAChR) alpha 1 subunit. Using synthetic peptides corresponding to the complete Torpedo nAChR alpha 1 subunit, we previously mapped a continuous epitope recognized by WF6, and the prototope for alpha-BGT, to the sequence segment alpha 1(181-200). Single amino acid substitution analogs have been used as an initial approach to determine the critical amino acids for WF6 and alpha-BGT binding. In the present study, we continue our analysis of the structural features of the WF6 epitope by comparing its cross-reactivity with synthetic peptides corr…

Ranidaealpha7 Nicotinic Acetylcholine ReceptorMolecular Sequence DataCross ReactionsReceptors NicotinicBiologyTorpedoEpitopelaw.inventionMiceSpecies SpecificityAntibody SpecificitylawSequence Homology Nucleic AcidmedicineAnimalsHumansReceptors CholinergicAmino Acid SequenceBinding sitePharmacologyMusclesBinding proteinAntibodies MonoclonalSnakesBungarotoxinsMolecular biologyRatsNicotinic acetylcholine receptorBiochemistryCattleAlpha-4 beta-2 nicotinic receptorPeptidesTorpedoAcetylcholineCys-loop receptorsmedicine.drugJournal of Receptor Research
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Stable expression in HEK-293 cells of the rat alpha3/beta4 subtype of neuronal nicotinic acetylcholine receptor.

1996

The alpha3/beta4 subtype of neuronal nicotinic acetylcholine receptor (nAChR) was stably expressed in human embryonic kidney (HEK) 293 cells that co-expressed a voltage-gated Ca2+ channel. alpha3/beta4-nAChR-expressing clones were identified using the fura-2 Ca2+ imaging technique, and were further characterised by single-cell and whole-cell patch-clamp studies. Acetylcholine (ACh) induced fast activating currents which showed desensitisation and inward rectification. The conductance of the ACh-activated channel was 29 pS. The order of potency of the nicotinic agonists tested was cytisine approximately = nicotine > acetylcholine. The EC50 value for ACh was 145 microM; the Hill coefficient w…

Stable expressionPatch-Clamp Techniquesα3/β4 nAChRBiophysicsNicotinic AntagonistsPharmacologyReceptors NicotinicTransfectionBiochemistryCell LineGanglionic nAChRCa2+ imagingGanglion type nicotinic receptorStructural BiologyMuscarinic acetylcholine receptorGeneticsmedicineAnimalsHumansNicotinic AgonistsNicotinic AntagonistHEK cellMolecular BiologyNeuronsurogenital systemChemistryMuscarinic acetylcholine receptor M3Cell BiologyAcetylcholineRecombinant ProteinsRatsNicotinic acetylcholine receptorNicotinic agonistCalciumCalcium ChannelsAlpha-4 beta-2 nicotinic receptorAcetylcholinemedicine.drugFEBS letters
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A second pathway of activation of the Torpedo acetylcholine receptor channel

1991

We have studied the interaction of the reversible acetylcholine esterase inhibitor (-)physostigmine (D-eserine) with the nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata electric tissue by means of ligand-induced ion flux into nAChR-rich membrane vesicles and of equilibrium binding. We find that (-) physostigmine induces cation flux (and also binds to the receptor) even in the presence of saturating concentrations of antagonists of acetylcholine, such as D-tubocurarine, alpha-bungarotoxin or antibody WF6. The direct action on the acetylcholine receptor is not affected by removal of the methylcarbamate function from the drug and thus is not due to carbamylation of the receptor…

StereochemistryPhysostigmineCesiumTubocurarineReceptors NicotinicTorpedoBiochemistryIon ChannelsAcetylcholine bindingCationsMuscarinic acetylcholine receptor M5medicineAnimalsBinding siteAcetylcholine receptorElectric OrganBinding SitesChemistryCell MembraneAntibodies MonoclonalMuscarinic acetylcholine receptor M3BungarotoxinsQuaternary Ammonium CompoundsNicotinic acetylcholine receptorNicotinic agonistBiophysicsCarbamatesAcetylcholinemedicine.drugEuropean Journal of Biochemistry
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Thermodynamics and kinetics of ion permeation in wild-type and mutated open active conformation of the human α7 nicotinic receptor

2020

Molecular studies of human pentameric ligand-gated ion channels (LGICs) expressed in neurons and at neuromuscular junctions are of utmost importance in the development of therapeutic strategies for neurological disorders. We focus here on the nicotinic acetylcholine receptor nAChR-α7, a homopentameric channel widely expressed in the human brain, with a proven role in a wide spectrum of disorders including schizophrenia and Alzheimer's disease. By exploiting an all-atom structural model of the full (transmembrane and extracellular) protein in the open, agonist-bound conformation we recently developed, we evaluate the free energy and the mean first passage time of single-ion permeation using …

alpha7 Nicotinic Acetylcholine ReceptorProtein ConformationGeneral Chemical EngineeringMutantProtonationLibrary and Information SciencesMolecular Dynamics SimulationReceptors Nicotinic01 natural sciencesArticleMolecular dynamics0103 physical sciencesHumansPotential of mean forceIon channel010304 chemical physicsChemistryWild typeGeneral ChemistryTransmembrane protein0104 chemical sciencesComputer Science Applications010404 medicinal & biomolecular chemistryNicotinic acetylcholine receptorKineticsnicotinic receptor ion permeation Milestoning free energyBiophysicsThermodynamics
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Replication of the association between CHRNA4 rs1044396 and harm avoidance in a large population-based sample.

2015

Harm avoidance is a personality trait characterized by excessive worrying and fear of uncertainty, which has repeatedly been related to anxiety disorders. Converging lines of research in rodents and humans point towards an involvement of the nicotinic cholinergic system in the modulation of anxiety. Most notably, the rs1044396 polymorphism in the CHRNA4 gene, which codes for the α4 subunit of the nicotinic acetylcholine receptor, has been linked to negative emotionality traits including harm avoidance in a recent study. Against this background, we investigated the association between harm avoidance and the rs1044396 polymorphism using data from N=1673 healthy subjects, which were collected …

genetics [Receptors Nicotinic]0301 basic medicineAdultMalemedicine.medical_specialtymedia_common.quotation_subjectContext (language use)Receptors NicotinicPolymorphism Single NucleotideNicotine03 medical and health sciences0302 clinical medicineHarm ReductionGermanymedicinePersonalityHumansPharmacology (medical)ddc:610PsychiatryBiological PsychiatryGenetic Association Studiesmedia_commonPharmacologybusiness.industrySmokinggenetics [Smoking]medicine.diseasePsychiatry and Mental healthNicotinic acetylcholine receptor030104 developmental biologyNicotinic agonistNeurologygenetics [Personality]AnxietyHarm avoidanceCholinergicFemaleNeurology (clinical)medicine.symptombusinessnicotinic acetylcholine receptor alpha4 subunit030217 neurology & neurosurgerymedicine.drugPersonalityEuropean neuropsychopharmacology : the journal of the European College of Neuropsychopharmacology
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Allosteric sensitization of nicotinic receptors by galantamine, a new treatment strategy for Alzheimer’s disease

2001

Cholinesterase inhibitors are the only approved drug treatment for patients with mild to moderately severe Alzheimer's disease. Interestingly, the clinical potency of these drugs does not correlate well with their activity as cholinesterase inhibitors, nor is their action as short lived as would be expected from purely symptomatic treatment. A few cholinesterase inhibitors, including galantamine, produce beneficial effects even after drug treatment has been terminated. These effects assume modes of action other than mere esterase inhibition and are capable of inducing systemic changes. We have recently discovered a mechanism that could account, at least in part, for the above-mentioned unex…

medicine.medical_specialtyPatch-Clamp TechniquesReceptors NicotinicPharmacologyCell LineMiceAllosteric RegulationAlzheimer DiseaseInternal medicinemedicineGalantamineAnimalsHumansNootropic AgentsBiological PsychiatryCholinesteraseAcetylcholine receptorNeuronsbiologyGalantamineChemistryNicotinic acetylcholine receptorNicotinic agonistEndocrinologyMechanism of actionTacrinebiology.proteinCholinesterase Inhibitorsmedicine.symptomAllosteric SiteAcetylcholinemedicine.drugBiological Psychiatry
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The nicotinic acetylcholine receptor agonist (±)-epibatidine increases FGF-2 mRNA and protein levels in the rat brain

2000

Abstract In a previous work, we showed that acute intermittent nicotine treatment up-regulates the level of fibroblast growth factor-2 (FGF-2) mRNA in brain regions of tel- and mesencephalon of rats suggesting that neuroprotective effect of (−)nicotine may, at least in part, involve an activation of the neuronal FGF-2 signalling. The present experiments were designed to extend the study on the nicotinic receptor mediated up-regulation of FGF-2 mRNA levels to the use of the potent nicotinic acetylcholine receptor (nAChR) agonist (±)-epibatidine. The (±)-epibatidine treatment led to a strong and long lasting up-regulation of FGF-2 mRNA expression in the cerebral cortex, in the hippocampal for…

medicine.medical_specialtyTime FactorsNicotinic acetylcoline receptor agonistPyridinesBlotting WesternNerve Tissue ProteinsNicotinic AntagonistsFibroblast growth factor-2MecamylamineBiologyHippocampusRats Sprague-DawleyNicotineCellular and Molecular NeuroscienceInternal medicineMecamylaminemedicineGlial cell line-derived neurotrophic factorAnimalsGlial Cell Line-Derived Neurotrophic FactorNerve Growth FactorsNicotinic AgonistsRNA MessengerMolecular BiologyIn Situ HybridizationEpibatidineCerebral CortexBrain-derived neurotrophic factorDose-Response Relationship DrugBrain-Derived Neurotrophic FactorBrainBridged Bicyclo Compounds HeterocyclicCorpus StriatumRatsSpecific Pathogen-Free OrganismsNicotinic acetylcholine receptorEndocrinologyNicotinic agonistGene Expression RegulationEpibatidinebiology.proteinFibroblast Growth Factor 2Alpha-4 beta-2 nicotinic receptorFibroblast growth factor receptor-1medicine.drugMolecular Brain Research
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α-Conotoxins EpI and AuIB switch subtype selectivity and activity in native versus recombinant nicotinic acetylcholine receptors

2003

The Xenopus laevis oocyte expression system was used to determine the activities of alpha-conotoxins EpI and the ribbon isomer of AuIB, on defined nicotinic acetylcholine receptors (nAChRs). In contrast to previous findings on intracardiac ganglion neurones, alpha-EpI showed no significant activity on oocyte-expressed alpha3beta4 and alpha3beta2 nAChRs but blocked the alpha7 nAChR with an IC50 value of 30 nM. A similar IC50 value (103 nM) was obtained on the alpha7/5HT3 chimeric receptor stably expressed in mammalian cells. Ribbon AuIB maintained its selectivity on oocyte-expressed alpha3beta4 receptors but unlike in native cells, where it was 10-fold more potent than native alpha-AuIB, had…

α7 nicotinic acetylcholine receptorα-Conotoxin AuIBRecombinant Fusion ProteinsBiophysicsXenopusNicotinic AntagonistsReceptors NicotinicPharmacologyTransfectionBiochemistrycomplex mixturesSubstrate SpecificityInhibitory Concentration 50Xenopus laevisStructural BiologyGeneticsmedicineAnimalsConotoxinNicotinic AntagonistReceptorMolecular BiologyAcetylcholine receptorbiologyα-Conotoxin EpICell Biologybiology.organism_classificationRatsCell biologyProtein SubunitsNicotinic acetylcholine receptorNicotinic agonistnervous systemIntracardiac gangliaOocytessense organsReceptors Serotonin 5-HT3ConotoxinsAcetylcholineXenopus laevis oocytemedicine.drugFEBS Letters
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