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Journal Article

γ-aminobutyric acidA receptor α5-subunit creates novel type II benzodiazepine receptor pharmacology

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Pritchett, D. B., & Seeburg, P. H. (1990). γ-aminobutyric acidA receptor α5-subunit creates novel type II benzodiazepine receptor pharmacology. Journal of Neurochemistry: official journal of the International Society for Neurochemistry, 54(5), 1802-1804. doi:10.1111/j.1471-4159.1990.tb01237.x.

Cite as: https://hdl.handle.net/21.11116/0000-0000-7FEC-9
A cDNA encoding a protein with 70% amino acid identity to the previously characterized gamma-aminobutyric acidA (GABAA) receptor alpha-subunits was isolated from a rat brain cDNA library by homology screening. As observed for alpha 1-, alpha 2-, and alpha 3-subunits, coexpression of this new alpha-subunit (alpha 5) with a beta- and gamma 2-subunit in cultured cells produces receptors displaying high-affinity binding sites for both muscimol, a GABA agonist, and benzodiazepines. Characteristic of GABAA/benzodiazepine type II sites, receptors containing alpha 2-, alpha 3- or alpha 5-subunits have low affinities for several type I-selective compounds. However, alpha 5-subunit-containing receptors have lower affinities for zolpidem (30-fold) and Cl 218 872 (three-fold) than measured previously using recombinantly expressed type II receptors containing either alpha 2- or alpha 3-subunits. Based on these findings, a reclassification of the GABAA/benzodiazepine receptors is warranted.