Search results for "Acetylcholine binding"

showing 7 items of 7 documents

Expression of the Acetylcholine Receptor α-Subunit Gene is Associated with Paraneoplastic Myasthenia Gravis in Mixed Thymoma

2000

Myasthenia gravis (MG) is an autoimmune disease caused by autoantibodies against the acetylcholine receptor (AChR) at the neuromuscular junction [1]. The muscular AChR has been extensively characterized [2], but the etiology of MG is still obscure. Whether the muscular AChR or another (auto)antigen plays a role during the initiation of MG is unknown [3]. The muscular AChR is a pentameric ion channel composed of four different subunits. The α-subunit contains the acetylcholine binding site and the main epitopes recognized by MG autoantibodies [2]. The human muscle AChR α-subunit exists as two isoforms, P3A- and P3A+ [4]. This is a result of alternative splicing of the P3A exon located betwee…

Gene isoformanimal structuresChemistryAlternative splicingmusculoskeletal systemmedicine.diseasemedicine.disease_causeMolecular biologyNeuromuscular junctionMyasthenia gravisAcetylcholine bindingMolecular mimicrymedicine.anatomical_structureNicotinic agonistmedicinetissuesAcetylcholine receptor
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Acetylcholine-binding protein in the hemolymph of the planorbid snail Biomphalaria glabrata is a pentagonal dodecahedron (60 subunits).

2012

Nicotinic acetylcholine receptors (nAChR) play important neurophysiological roles and are of considerable medical relevance. They have been studied extensively, greatly facilitated by the gastropod acetylcholine-binding proteins (AChBP) which represent soluble structural and functional homologues of the ligand-binding domain of nAChR. All these proteins are ring-like pentamers. Here we report that AChBP exists in the hemolymph of the planorbid snail Biomphalaria glabrata (vector of the schistosomiasis parasite) as a regular pentagonal dodecahedron, 22 nm in diameter (12 pentamers, 60 active sites). We sequenced and recombinantly expressed two ∼25 kDa polypeptides (BgAChBP1 and BgAChBP2) wit…

Macromolecular AssembliesProtein StructureProtein FoldingScienceBiophysicsBiochemistryProtein ChemistryHomology (biology)Ion ChannelsProtein Structure Secondarylaw.inventionDodecahedronAcetylcholine bindinglawHemolymphHemolymphMacromolecular Structure AnalysisBiomphalaria glabrataAnimal PhysiologyAnimalsBiomacromolecule-Ligand InteractionsBiologyAcetylcholine receptorMultidisciplinaryHemoproteinsbiologyBiomphalariaQRActive siteProteinsComputational BiologyAnatomybiology.organism_classificationRecombinant ProteinsAcetylcholineProtein Structure TertiaryBiochemistryAcetylcholine Receptorsbiology.proteinRecombinant DNAMedicineCarrier ProteinsZoologyResearch ArticlePLoS ONE
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Conformational changes in acetylcholine binding protein investigated by temperature accelerated molecular dynamics.

2014

Despite the large number of studies available on nicotinic acetylcholine receptors, a complete account of the mechanistic aspects of their gating transition in response to ligand binding still remains elusive. As a first step toward dissecting the transition mechanism by accelerated sampling techniques, we study the ligand-induced conformational changes of the acetylcholine binding protein (AChBP), a widely accepted model for the full receptor extracellular domain. Using unbiased Molecular Dynamics (MD) and Temperature Accelerated Molecular Dynamics (TAMD) simulations we investigate the AChBP transition between the apo and the agonist-bound state. In long standard MD simulations, both confo…

Nicotinic Acetylcholine ReceptorsProtein ConformationGatingMolecular DynamicsLigandsBiochemistryBiophysics SimulationsIon ChannelsMolecular dynamicsAcetylcholine bindingComputational ChemistryBiochemical SimulationsNicotinic AgonistsBiomacromolecule-Ligand InteractionsBiochemistry SimulationsMultidisciplinaryHydrogen bondChemistryPhysicsQTemperatureRLigand (biochemistry)nicotinic receptor molecular dynamics tamd acethylcholine binding proteinChemistryNicotinic agonistBiochemistryMedicineBiophysic Al SimulationsResearch ArticleProtein BindingProtein subunitScienceBiophysicsMolecular Dynamics SimulationProtein ChemistryStatistical MechanicsChemical BiologyAnimalsBiologyAcetylcholine receptorBinding SitesProteinsComputational BiologyHydrogen BondingSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein SubunitsMolluscaAcetylcholine ReceptorsBiophysicsLobelineCarrier ProteinsPLoS ONE
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Desensitization is a property of the cholinergic binding region of the nicotinic acetylcholine receptor, not of the receptor-integral ion channel

1991

AbstractThe reversible acetylcholine esterase inhibitor (−)-physostigmine (eserine) is the prototype of a new class of nicotinic acetylcholine receptor (nAChR) activating ligands: it induces cation fluxes into nAChR-rich membrane vesicles from Torpedo marmorala electric tissue even under conditions of antagonist blocked acetylcholine binding sites (Okonjo, Kuhlmann, Maclicke, Neuron, in press). This suggests that eserine exerts its channel-activating property via binding sites at the nAChR separate from those of the natural transmitter. We now report that eserine can activate the channel even when the receptor has been preincubated (desensitized) with elevated concentrations of acetylcholin…

Nicotinic acetylcholine receptorStereochemistryAcetylcholine-gated cation channelPhysostigmineBiophysicsCesiumIon fluxDesensitizationIn Vitro TechniquesReceptors NicotinicTorpedoBiochemistryIon ChannelsAnticholinesteraseAcetylcholine bindingGanglion type nicotinic receptorStructural BiologyMuscarinic acetylcholine receptor M5GeneticsmedicineAnimalsMolecular BiologyAcetylcholine receptorBinding SitesChemistryCell BiologyBungarotoxinsAcetylcholineNicotinic acetylcholine receptorNicotinic agonistCarbamateBiophysicsCholinergicAcetylcholineEserinemedicine.drugFEBS Letters
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Biochemical Characterization of a Novel Channel-Activating Site on Nicotinic Acetylcholine Receptors

1993

We have studied the interaction of the reversible acetylcholine esterase inhibitor (-)physostigmine and several structurally related compounds with the nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata electric tissue by means of ligand-induced ion flux into nAChR-rich membrane vesicles, direct binding studies and photoaffinity labeling. (-)Physostigmine acts as a channel-activating ligand at low concentrations and as a direct channel blocker at elevated concentrations. Channel activation is not inhibited by desensitizing concentrations of ACh or ACh-competitive ligands (including alpha-bungarotoxin and D-tubocurarine) but is inhibited by antibody FK1 and several other compoun…

PharmacologyPhotoaffinity labelingChemistryPhysostigmineMolecular Sequence DataIn Vitro TechniquesReceptors NicotinicTorpedoIon ChannelsAcetylcholine bindingNicotinic acetylcholine receptorNicotinic agonistnervous systemBiochemistrymedicineAnimalsChannel blockerAmino Acid SequenceBinding siteAcetylcholineAcetylcholine receptormedicine.drugJournal of Receptor Research
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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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Cigarette smoke alters non-neuronal cholinergic system components inducing MUC5AC production in the H292 cell line.

2013

Abstract Cigarette smoke extract (CSE) affects the expression of Choline Acetyl-Transferase (ChAT), muscarinic acetylcholine receptors, and mucin production in bronchial epithelial cells. Mucin 5AC (MUC5AC), muscarinic acetylcholine receptor M3, ChAT expression, acetylcholine levels and acetylcholine binding were measured in a human pulmonary mucoepidermoid carcinoma cell line (H292) stimulated with CSE. We performed ChAT/RNA interference experiments in H292 cells stimulated with CSE to study the role of ChAT/acetylcholine in MUC5AC production. The effects of Hemicholinium-3 (HCh-3) (50 μM) (a potent and selective choline uptake blocker) and Tiotropium bromide (Spiriva ® ) (100 nM), alone o…

medicine.medical_specialtyScopolamine DerivativesBronchiComplex MixturesMucin 5ACCholinergic AntagonistsCholine O-Acetyltransferasechemistry.chemical_compoundAcetylcholine bindingInternal medicineCell Line TumorSmokeparasitic diseasesMuscarinic acetylcholine receptorTobaccomedicineCholineHumansSecretionAlbuterolNeurotransmitter Uptake InhibitorsTiotropium BromideAutocrine signallingSalmeterol XinafoatePharmacologyReceptor Muscarinic M3Epithelial CellsHemicholinium 3respiratory systemCholine acetyltransferaseAcetylcholineBronchodilator AgentsAndrostadienesEndocrinologychemistryCell cultureFluticasoneRNA InterferenceAcetylcholinemedicine.drugEuropean journal of pharmacology
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