Article date: 1988/12/2
PubMed ID: 2848320
Journal name: Science (New York, N.Y.) (ISSN: 0036-8075)
Human gamma-aminobutyric acid A (GABAA) receptor subunits were expressed transiently in cultured mammalian cells. This expression system allows the simultaneous characterization of ligand-gated ion channels by electrophysiology and by pharmacology. Thus, coexpression of the alpha and beta subunits of the GABAA receptor generated GABA-gated chloride channels and binding sites for GABAA receptor ligands. Channels consisting of only alpha or beta subunits could also be detected. These homomeric channels formed with reduced efficiencies compared to the heteromeric receptors. Both of these homomeric GABA-responsive channels were potentiated by barbiturate, indicating that sites for both ligand-gating and allosteric potentiation are present on receptors assembled from either subunit.
Author List: Pritchett D B, Sontheimer H, Gorman C M, Kettenmann H, Seeburg P H, Schofield P R
Publication Types: Journal Article; Research Support, Non-U.S. Gov't
Substances mentioned in the article: Chloride Channels; Chlorides; Macromolecular Substances; Membrane Proteins; Receptors, GABA-A; Muscimol;
Mesh terms: Allosteric Regulation; Blotting, Northern; Cells, Cultured; Chloride Channels; Chlorides/physiology; Cloning, Molecular; Electric Conductivity; Humans; Macromolecular Substances; Membrane Proteins/physiology; Muscimol/metabolism; Receptors, GABA-A/physiology; Structure-Activity Relationship; Transfection;