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Interactions of 2,3‐benzodiazepines and cydothiazide at AMPA receptors: patch clamp recordings in cultured neurones and area CA1 in hippocampal slices

1996; Wiley; Volume: 117; Issue: 6 Linguagem: Inglês

10.1111/j.1476-5381.1996.tb16718.x

1476-5381

Gerhard Rammes, Dieter Swandulla, Graham L. Collingridge, Sabine Hartmann, Chris G. Parsons,

Electrochemical Analysis and Applications

British Journal of PharmacologyVolume 117, Issue 6 p. 1209-1221 Free Access Interactions of 2,3-benzodiazepines and cydothiazide at AMPA receptors: patch clamp recordings in cultured neurones and area CA1 in hippocampal slices Gerhard Rammes, Gerhard Rammes Department of Molecular Pharmacology, Institute for Experimental and Clinical Pharmacology and Toxicology, University of Erlangen, D-91054 Erlangen, GermanySearch for more papers by this authorDieter Swandulla, Dieter Swandulla Department of Molecular Pharmacology, Institute for Experimental and Clinical Pharmacology and Toxicology, University of Erlangen, D-91054 Erlangen, GermanySearch for more papers by this authorGraham L. Collingridge, Graham L. Collingridge Department of Anatomy, The Medical School, Bristol BS8 1TD, EnglandSearch for more papers by this authorSabine Hartmann, Sabine Hartmann Department of Pharmacology, Merz + Co., D-60318 Frankfurt, GermanySearch for more papers by this authorChris G. Parsons, Corresponding Author Chris G. Parsons Department of Molecular Pharmacology, Institute for Experimental and Clinical Pharmacology and Toxicology, University of Erlangen, D-91054 Erlangen, Germany Department of Pharmacology, Merz + Co., D-60318 Frankfurt, GermanyDepartment of Molecular Pharmacology, Institute for Experimental and Clinical Pharmacology and Toxicology, University of Erlangen, D-91054 Erlangen, Germany; and Department of Pharmacology, Merz + Co., D-60318 Frankfurt, GermanySearch for more papers by this author Gerhard Rammes, Gerhard Rammes Department of Molecular Pharmacology, Institute for Experimental and Clinical Pharmacology and Toxicology, University of Erlangen, D-91054 Erlangen, GermanySearch for more papers by this authorDieter Swandulla, Dieter Swandulla Department of Molecular Pharmacology, Institute for Experimental and Clinical Pharmacology and Toxicology, University of Erlangen, D-91054 Erlangen, GermanySearch for more papers by this authorGraham L. Collingridge, Graham L. Collingridge Department of Anatomy, The Medical School, Bristol BS8 1TD, EnglandSearch for more papers by this authorSabine Hartmann, Sabine Hartmann Department of Pharmacology, Merz + Co., D-60318 Frankfurt, GermanySearch for more papers by this authorChris G. Parsons, Corresponding Author Chris G. Parsons Department of Molecular Pharmacology, Institute for Experimental and Clinical Pharmacology and Toxicology, University of Erlangen, D-91054 Erlangen, Germany Department of Pharmacology, Merz + Co., D-60318 Frankfurt, GermanyDepartment of Molecular Pharmacology, Institute for Experimental and Clinical Pharmacology and Toxicology, University of Erlangen, D-91054 Erlangen, Germany; and Department of Pharmacology, Merz + Co., D-60318 Frankfurt, GermanySearch for more papers by this author First published: March 1996 https://doi.org/10.1111/j.1476-5381.1996.tb16718.xCitations: 43AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract 1 The 2,3-benzodiazepines GYKI 52466, GYKI 53405 and GYKI 53655 antagonized AMPA-induced currents in cultured superior colliculus neurones in a non use-dependent manner (steady state IC50S: GYKI 52466 9.8±0.6 μm; GYKI 53405 3.1±0.6 μm; GYKI 53655 0.8±0.1 μm). 2 Higher concentrations of all three antagonists slowed the onset kinetics and quickened the offset kinetics of AMPA-induced currents indicative of an allosteric interaction with the AMPA recognition site. 3 Cydothiazide (3–300 μm) dramatically slowed desensitization of AMPA-induced currents and potentiated steady state currents (EC50 10.0±2.5 μm) to a much greater degree than peak currents. Both τon and τoff were also increased by cydothiazide in a concentration-dependent manner (EC50: τon 42.1±4.5 μm; τoff 31.6±6.6 μ.M). 4 Cydothiazide (10–100 μ.M) shifted the concentration-response curves of the 2,3-benzodiazepines to the right. For example, with 10 μm cydothiazide the IC50S of GYKI 52466 and GYKI 53405 on steady-state AMPA-induced currents were 57.9±9.5 and 41.6±1.5 μm respectively. 5 GYKI 53405 and GYKI 52466 concentration-dependently reversed the effects of cydothiazide (100 μm) on offset kinetics (GYKI 53405 IC50 16.6±4.2 μm). However, the 2,3-benzodiazepines were unable to reintroduce desensitization in the presence of cydothiazide and even concentration-dependently slowed the onset kinetics of AMPA responses further (GYKI 53405 EC50 8.0±2.8 μm). 6 GYKI 52466 decreased the peak amplitude of hippocampal area CA1 AMPA receptor-mediated exdtatory postsynaptic currents (e.p.s.cs) (IC50 10.8±0.8 μm) with no apparent effect on response kinetics. Cydothiazide prolonged the decay time constant of AMPA receptor-mediated e.p.s.cs (EC50 35.7±6.5 μm) with less pronounced effects in slowing e.p.s.c. onset kinetics and increasing e.p.s.c. amplitude. 7 Cydothiazide (330 μm) shifted the concentration-response curve for the effects of GYKI 52466 on AMPA receptor-mediated e.p.s.c. peak amplitude to the right (GYKI 52466 IC50 26.9±9.4 μm). Likewise, GYKI 52466 (30–100 μm)) shifted the concentration-response curve for the effects of cydothiazide on AMPA receptor-mediated e.p.s.c. decay time constants to the right. 8 In conclusion, cydothiazide and the 2,3-benzodiazepines seem to bind to different sites on AMPA receptors but exert strong allosteric interactions with one another and with other domains such as the agonist recognition site. 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