Search results for "Cys-loop receptors"

showing 3 items of 3 documents

Altered receptor subtypes in the forebrain of GABAA receptor δ subunit-deficient mice: recruitment of γ2 subunits

2002

A GABA(A) receptor delta subunit-deficient mouse line was created by homologous recombination in embryonic stem cells to investigate the role of the subunit in the brain GABA(A) receptors. High-affinity [(3)H]muscimol binding to GABA sites as studied by ligand autoradiography was reduced in various brain regions of delta(-/-) animals. [(3)H]Ro 15-4513 binding to benzodiazepine sites was increased in delta(-/-) animals, partly due to an increment of diazepam-insensitive receptors, indicating an augmented forebrain assembly of gamma 2 subunits with alpha 4 subunits. In the western blots of forebrain membranes of delta(-/-) animals, the level of gamma 2 subunit was increased and that of alpha …

MaleAzidesProtein subunitBiologyTritiumSynaptic TransmissionIon ChannelsGABAA-rho receptorInterleukin 10 receptor alpha subunitBenzodiazepinesMiceRadioligand Assaychemistry.chemical_compoundAnimalsReceptorGABA Agonistsgamma-Aminobutyric AcidMice KnockoutNeuronsBinding SitesMuscimolGABAA receptorGeneral NeuroscienceBrainAffinity LabelsNeural InhibitionReceptors GABA-AMolecular biologynervous systemMuscimolchemistryMutationForebrainFemaleCys-loop receptorsNeuroscience
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New Hyperekplexia Mutations Provide Insight into Glycine Receptor Assembly, Trafficking, and Activation Mechanisms*

2013

Hyperekplexia is a syndrome of readily provoked startle responses, alongside episodic and generalized hypertonia, that presents within the first month of life. Inhibitory glycine receptors are pentameric ligand-gated ion channels with a definitive and clinically well stratified linkage to hyperekplexia. Most hyperekplexia cases are caused by mutations in the α1 subunit of the human glycine receptor (hGlyR) gene (GLRA1). Here we analyzed 68 new unrelated hyperekplexia probands for GLRA1 mutations and identified 19 mutations, of which 9 were novel. Electrophysiological analysis demonstrated that the dominant mutations p.Q226E, p.V280M, and p.R414H induced spontaneous channel activity, indicat…

MaleProtein subunitMutation MissenseBiologyBiochemistryProtein Structure SecondaryReceptors GlycinemedicineHumansHyperekplexiaReceptorMolecular BiologyGlycine receptorIon channelGeneticsWild typeMolecular Bases of DiseaseCell BiologyMuscle RigidityProtein Structure TertiaryAmino Acid SubstitutionGene Expression RegulationFemalemedicine.symptomIon channel linked receptorsCys-loop receptors
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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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