Inverse but not full benzodiazepine agonists modulate recombinant α6β2γ2 GABAA 
receptors in transfected human embryonic kidney cells

Kleingoor, Claudia; Ewert, Markus; von Blankenfeld, G.; Seeburg, Peter H.; Kettenmann, Helmut

doi:10.1016/0304-3940(91)90389-B

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Inverse but not full benzodiazepine agonists modulate recombinant α6β2γ2 GABAA receptors in transfected human embryonic kidney cells

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Ewert, Markus
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Seeburg, Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/030439409190389B/pdf?md5=53e998a914816861c51a32b534066359&pid=1-s2.0-030439409190389B-main.pdf
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Citation

Kleingoor, C., Ewert, M., von Blankenfeld, G., Seeburg, P. H., & Kettenmann, H. (1991). Inverse but not full benzodiazepine agonists modulate recombinant α6β2γ2 GABAA receptors in transfected human embryonic kidney cells. Neuroscience Letters, 130(2), 169-172. doi:10.1016/0304-3940(91)90389-B.

Cite as: https://hdl.handle.net/21.11116/0000-0000-6F09-B

Abstract

We compared the modulation of GABA (γ-aminobutyric acid)-activated currents by benzodiazepines in recombinant (GABAA receptors containing either one of two α subunits, α1 or α6. Lüddens et al. (Nature, 346 (1990) 648–651) have previously demonstrated that the α6 subunit is part of a cerebellar receptor subtype which selectively binds Ro15–4513, an antagonist of alcohol-induced motor ataxia. Here we report that the imidazobenzodiazepine Ro15–4513 (ethyl 8-azido-5,6-dihydro-5-methyl-6-oxo-4H-imidazo-(1,5-a) (1,4)benzodiazepine-3-carboxylate) reduced GABA-activated currents in recombinant α6β2γ2 and α1β2γ2 receptors, thus acting consistently as an inverse agonist. Moreover, another well characterized negative modulator, DMCM (methyl-4-ethyl-6,7-dimethoxy-β-carboline-3-carboxylate), also reduces GABA activated-currents in both receptors. In contrast, flunitrazepam (FNZM), a benzodiazepine agonist, increases GABA-activated currents in α1β2γ2 receptors, but not in α6β2γ2 receptors. This study lends further support to the hypothesis that the binding sites of full and partial inverse agonists are different.