Search results for "alpha7 Nicotinic Acetylcholine Receptor"

showing 10 items of 10 documents

Closed-Locked and Apo-Resting State Structures of the Human α7 Nicotinic Receptor: A Computational Study

2018

International audience; Nicotinic acetylcholine receptors, belonging to the Cys-loop super-family of ligand-gated ion channels (LGICs), are membrane proteins present in neurons and at neuromuscular junctions. They are responsible for signal transmission, and their function is regulated by neurotransmitters, agonists and antagonists drugs. A detailed knowledge of their conformational transition in response to ligand binding is critical to understand the basis of ligand-receptor interaction, in view of new pharmacological approaches to control receptor activity. However, the scarcity of experimentally derived structures of human channels makes this perspective extremely challenging. To contri…

0301 basic medicinealpha7 Nicotinic Acetylcholine ReceptorProtein ConformationGeneral Chemical EngineeringMolecular Dynamics SimulationLibrary and Information Sciences03 medical and health sciencesMolecular dynamics0302 clinical medicineHumansHomology modelingReceptorIon channelAcetylcholine receptor[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Protein StabilityChemistryWaterHydrogen BondingGeneral ChemistryLigand (biochemistry)molecular dynamicsComputer Science Applications[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsTransmembrane domain030104 developmental biologyNicotinic agonistBiophysics[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Conotoxinsligand gated ion channel030217 neurology & neurosurgery
researchProduct

A possible desensitized state conformation of the human α7 nicotinic receptor: A molecular dynamics study

2017

International audience; The determination of the conformational states corresponding to diverse functional roles of ligand gated ion channels is subject of intense investigation with various techniques, from X-rays structure determination to electrophysiology and computational modeling. Even with a certain number of structures becoming recently available, only few major structural features distinguishing conductive open channel from the non conductive resting protein have been highlighted, while high-resolution details are still missing. The characterization of the desensitized conformation(s) is even more complex, and only few specific characteristics have been identified. Furthermore, exp…

0301 basic medicinealpha7 Nicotinic Acetylcholine ReceptorStereochemistryPyridinesBiophysicsMolecular Dynamics SimulationBiochemistry03 medical and health sciencesMolecular dynamicsmedicineHumansHomology modelingnicotinic receptor epibatidine molecular dynamics inactive stateIon channel[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryProtein StabilityOrganic ChemistryHydrogen BondingBridged Bicyclo Compounds HeterocyclicSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein Structure Tertiary[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsElectrophysiology030104 developmental biologyNicotinic agonistα7 nicotinic receptorEpibatidineLigand-gated ion channel[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]medicine.drug
researchProduct

Behavioral effects of different enriched environments in mice treated with the cholinergic agonist PNU-282987.

2013

Abstract Environmental enrichment is an experimental model in which rodents are housed in complex environments that favor lower levels of anxiety-like behavior. PNU-282987 (PNU) is a α7 nicotinic acetylcholine receptor agonist with beneficial effects on learning though its effects on anxiety are unclear. Our main aim was to carry out a study of its effects in NMRI ( n  = 96) mice reared in different environments: environmental enrichment (EE), Marlau™ cages (MC) and standard environment (SE). After a 4-month period, mice received acute treatment of PNU (2.5, 5 and 10 mg/kg) and were evaluated in the elevated plus-maze (EPM) and hole-board (HB). In the EPM, both EE and MC reared mice showed …

AgonistMalemedicine.medical_specialtyElevated plus mazealpha7 Nicotinic Acetylcholine Receptormedicine.drug_classAnxietyEnvironmentMotor ActivityDevelopmental psychologyBehavioral NeuroscienceBridged Bicyclo CompoundsMiceα7 nicotinic acetylcholine receptorInternal medicinemedicineAnimalsNicotinic AgonistsBeneficial effectsEnvironmental enrichmentBehavior AnimalExperimental modelGeneral MedicineNicotinic agonistEndocrinologyBenzamidesExploratory BehaviorCholinergicAnimal Science and ZoologyPsychologyInjections IntraperitonealBehavioural processes
researchProduct

α7 Nicotinic acetylcholine receptors and modulation of gabaergic synaptic transmission in the hippocampus

2000

The present report provides new findings regarding modulation of gamma-aminobutyric acid (GABA) transmission by alpha7 nicotinic receptor activity in CA1 interneurons of rat hippocampal slices. Recordings were obtained from tight-seal cell-attached patches of the CA1 interneurons, and agonists were delivered to the neurons via a modified U-tube. Application for 6 s of the alpha7 nicotinic receptor-selective agonist choline (or =1 mM) to all CA1 interneurons tested triggered action potentials that were detected as fast current transients. The activity triggered by choline terminated well before the end of the agonist pulse, was blocked by the alpha7 nicotinic receptor antagonist methyllycaco…

Agonistmedicine.medical_specialtyalpha7 Nicotinic Acetylcholine ReceptorInterneuronmedicine.drug_classAction PotentialsIn Vitro TechniquesReceptors NicotinicBiologyHippocampusSynaptic TransmissionCholinechemistry.chemical_compoundGanglion type nicotinic receptorInterneuronsInternal medicinemedicineAnimalsNeurotransmittergamma-Aminobutyric AcidPharmacologyMethyllycaconitineDose-Response Relationship DrugRatsElectrophysiologyEndocrinologymedicine.anatomical_structureNicotinic agonistchemistryBiophysicsAlpha-4 beta-2 nicotinic receptorAcetylcholinemedicine.drugEuropean Journal of Pharmacology
researchProduct

The copy number variant involving part of the α7 nicotinic receptor gene contains a polymorphic inversion.

2008

The alpha7 nicotinic acetylcholine receptor gene (CHRNA7) is located at 15q13-q14 in a region that is strongly linked to the P50 sensory gating deficit, an endophenotype of schizophrenia and bipolar disorder. Part of the gene is a copy number variant, due to a duplication of exons 5-10 and 3' sequence in CHRFAM7A, which is present in many but not all humans. Maps of this region show that the two genes are in opposite orientation in the individual mainly represented in the public access human DNA sequence database (Build 36), suggesting that an inversion had occurred since the duplication. We have used fluorescent in situ hybridization to investigate this putative inversion. Analysis of inte…

Genetic MarkersMaleLinkage disequilibriumBipolar DisorderPan troglodytesalpha7 Nicotinic Acetylcholine ReceptorReceptors NicotinicLinkage DisequilibriumExonGene duplicationGeneticsSettore MED/48 -Scienze Infermierist. e Tecn. Neuro-Psichiatriche e Riabilitat.AnimalsHumansCopy-number variationGeneSettore MED/25 - PsichiatriaGenetics (clinical)Sequence DeletionSegmental duplicationChromosomal inversionGeneticsChromosomes Human Pair 15Polymorphism GeneticBase SequencebiologyCHRNA7Chromosome Mappinginversion schizophrenia bipolar disorder 15q13–q14 CHRNA7 segmental duplicationChromosome InversionSchizophreniabiology.proteinFemale
researchProduct

The Ras/Raf-1/MEK1/ERK Signaling Pathway Coupled to Integrin Expression Mediates Cholinergic Regulation of Keratinocyte Directional Migration

2005

The physiologic mechanisms that determine directionality of lateral migration are a subject of intense research. Galvanotropism in a direct current (DC) electric field represents a natural model of cell re-orientation toward the direction of future migration. Keratinocyte migration is regulated through both the nicotinic and muscarinic classes of acetylcholine (ACh) receptors. We sought to identify the signaling pathway mediating the cholinergic regulation of chemotaxis and galvanotropism. The pharmacologic and molecular modifiers of the Ras/Raf-1/MEK1/ERK signaling pathway altered both chemotaxis toward choline and galvanotropism toward the cathode in a similar way, indicating that the sam…

KeratinocytesMAPK/ERK pathwayIntegrinsalpha7 Nicotinic Acetylcholine ReceptorMAP Kinase Signaling SystemIntegrinMAP Kinase Kinase 1Receptors NicotinicBiologyTransfectionBiochemistryMuscarinic acetylcholine receptormedicineHumansRNA Small InterferingKeratinocyte migrationExtracellular Signal-Regulated MAP KinasesMolecular BiologyCells CulturedChemotaxisReceptor Muscarinic M1ChemotaxisCell BiologyAcetylcholineUp-RegulationCell biologyElectrophysiologyras Proteinsbiology.proteinraf KinasesLamellipodiumSignal transductionAcetylcholineSignal Transductionmedicine.drugJournal of Biological Chemistry
researchProduct

Further delineation of eye manifestations in homozygous 15q13.3 microdeletions including TRPM1: a differential diagnosis of ceroid lipofuscinosis.

2014

The 15q13.3 heterozygous microdeletion is a fairly common microdeletion syndrome with marked clinical variability and incomplete penetrance. The average size of the deletion, which comprises six genes including CHRNA7, is 1.5 Mb. CHRNA7 has been identified as the gene responsible for the neurological phenotype in this microdeletion syndrome. Only seven patients with a homozygous microdeletion that includes at least CHRNA7, and is inherited from both parents have been described in the literature. The aim of this study was to further describe the distinctive eye manifestations from the analysis in the three French patients diagnosed with the classical 1.5 Mb homozygous microdeletion. Patients…

MalePathologymedicine.medical_specialtygenetic structuresalpha7 Nicotinic Acetylcholine ReceptorEncephalopathyTRPM Cation ChannelsChromosome DisordersBiologyBlindnessEyePupilNeuronal Ceroid-LipofuscinosesNight BlindnessSeizuresIntellectual DisabilityRetinal DystrophiesGeneticsmedicineElectroretinographyMyopiaHumansEye AbnormalitiesChildGenetics (clinical)TRPM1Genetic Association StudiesCongenital stationary night blindnessGeneticsChromosomes Human Pair 15DystrophyEye Diseases HereditaryGenetic Diseases X-LinkedOptic NerveMicrodeletion syndromemedicine.diseasePenetranceChild PreschoolFemalesense organsDifferential diagnosisChromosome DeletionAmerican journal of medical genetics. Part A
researchProduct

A Structural Model of the Human α7 Nicotinic Receptor in an Open Conformation

2015

International audience; Nicotinic acetylcholine receptors (nAchRs) are ligand-gated ion channels that regulate chemical transmission at the neuromuscular junction. Structural information is available at low resolution from open and closed forms of an eukaryotic receptor, and at high resolution from other members of the same structural family, two prokaryotic orthologs and an eukary- otic GluCl channel. Structures of human channels however are still lacking. Homology modeling and Molecular Dynamics simulations are valuable tools to predict structures of unknown proteins, however, for the case of human nAchRs, they have been unsuccessful in providing a stable open structure so far. This is du…

Models MolecularHydrogen bondingalpha7 Nicotinic Acetylcholine ReceptorProtein ConformationMolecular Sequence DataMESH: Sequence Alignmentligand gated ion channles molecular dynamics simulation epibatidine waterlcsh:MedicineSequence alignmentMESH: Amino Acid SequenceMolecular Dynamics SimulationMESH: Models Molecular*Molecular dynamicsProtein structureSequence alignmentCationsHumansMESH: Molecular Dynamics SimulationHomology modelingAmino Acid SequenceNicotinic Receptorlcsh:ScienceBiochemical simulationsIon channelAcetylcholine receptorIonsMESH: Protein Conformation*MultidisciplinaryMESH: HumansMESH: Molecular Sequence DataChemistryMESH: Protein Multimerizationlcsh:RMESH: alpha7 Nicotinic Acetylcholine Receptor/chemistry*[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]Transmembrane proteinSimulation and modelingNicotinic agonistBiochemistryBiophysicsProtein structurelcsh:QProtein MultimerizationResearch ArticleStructural Model
researchProduct

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
researchProduct

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
researchProduct