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http://purl.uniprot.org/citations/12117536http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12117536http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12117536http://www.w3.org/2000/01/rdf-schema#comment"The native cholinergic receptor that mediates synaptic transmission between olivocochlear fibers and outer hair cells of the cochlea is permeable to Ca(2+) and is thought to be composed of both the alpha 9 and the alpha 10 cholinergic nicotinic subunits. The aim of the present work was to study the permeability of the recombinant alpha 9 alpha 10 nicotinic acetylcholine receptor to Ca(2+), Ba(2+) and Mg(2+) and its modulation by these divalent cations. Experiments were performed, by the two-electrode voltage-clamp technique, in Xenopus laevis oocytes injected with alpha 9 and alpha 10 cRNA. The relative divalent to monovalent cation permeability was high ( approximately 10) for Ca(2+), Ba(2+) and Mg(2+). Currents evoked by acetylcholine (ACh) were potentiated by either Ca(2+) or Ba(2+) up to 500 microM but were blocked by higher concentrations of these cations. Potentiation by Ca(2+) was voltage-independent, whereas blockage was stronger at hyperpolarized than at depolarized potentials. Mg(2+) did not potentiate but it blocked ACh-evoked currents (IC(50)=0.38 mM). In the absence of Ca(2+), the EC(50) for ACh was higher (48 microM) than that obtained with 1.8 mM Ca(2+) (14.3 microM), suggesting that potentiation by Ca(2+) involves changes in the apparent affinity of the alpha 9 alpha 10 receptor for ACh."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.org/dc/terms/identifier"doi:10.1016/s0378-5955(02)00380-5"xsd:string
http://purl.uniprot.org/citations/12117536http://purl.org/dc/terms/identifier"doi:10.1016/s0378-5955(02)00380-5"xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/author"Elgoyhen A.B."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/author"Elgoyhen A.B."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/author"Katz E."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/author"Katz E."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/author"Vetter D.E."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/author"Vetter D.E."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/author"Weisstaub N."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/author"Weisstaub N."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/name"Hear. Res."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/name"Hear. Res."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/pages"122-135"xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/pages"122-135"xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/title"The alpha9alpha10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/title"The alpha9alpha10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations."xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/volume"167"xsd:string
http://purl.uniprot.org/citations/12117536http://purl.uniprot.org/core/volume"167"xsd:string
http://purl.uniprot.org/citations/12117536http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12117536
http://purl.uniprot.org/citations/12117536http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12117536