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• W2049949416 abstract "The α7 neuronal nicotinic acetylcholine receptor subtype forms a Ca2+-permeable homooligomeric ion channel sensitive to α-bungarotoxin in Xenopus oocytes. In this study, we have stably and functionally expressed the human α7 cDNA in a mammalian cell line, HEK-293 and examined its pharmacologic properties. [125I]α-Bungarotoxin bound to transfected cellswith a Kd value of 0.7 nM and a Bmax value of 973 pmol/mg protein. No specific binding was detected in untransfected cells. Specific binding could be displaced by unlabeled α-bungarotoxin (Ki = 0.5 nM and an excellent correlation was observed between binding affinities of a series of nicotinic cholinergic ligands in transfected cells and those in the human neuroblastoma IMR-32 cell line. Additionally, cell surface expression of α7 receptors was detected by fluorescein isothiocyanate-conjugated α-bungarotoxin in transfected cells. Whole cell currents sensitive to blockade by α-bungarotoxin, and with fast kinetics of activation and inactivation, were recorded from transfected cells upon rapid application of (−)-nicotine or acetylcholine with EC50 values of 49 μM and 155 μM respectively. We conclude that the human α7 subunit when expressed alone can form functional ion channels and that the stably transfected HEK-293 cell line serves as a unique system for studying human μ7 nicotinic receptor function and regulation, and for examining ligand interactions." @default.
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• W2049949416 date "1995-08-01" @default.
• W2049949416 modified "2023-10-11" @default.
• W2049949416 title "Stable expression and pharmacological properties of the human α7 nicotinic acetylcholine receptor" @default.
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• W2049949416 doi "https://doi.org/10.1016/0922-4106(95)00083-6" @default.
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