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Modulation by zinc ions of native rat and recombinant human inhibitory glycine receptors.

Laube, Bodo ; Kuhse, J. ; Rundström, N. ; Kirsch, J. ; Schmieden, V. ; Betz, H. (1995)
Modulation by zinc ions of native rat and recombinant human inhibitory glycine receptors.
In: The Journal of physiology, 483
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

1. The effect of the divalent cation Zn2+ on inhibitory glycine receptor (GlyR) currents was investigated in rat embryonic spinal cord neurons and Xenopus oocytes expressing recombinant GlyRs. 2. In cultured spinal neurons, Zn2+ potentiated glycine-induced whole-cell currents about 3-fold when applied extracellularly at concentrations of 0.5-10 microM. In contrast, higher concentrations (> 100 microM) of Zn2+ decreased the glycine response. 3. A similar biphasic modulation of glycine-induced currents by Zn2+ was also found with recombinant homo- and hetero-oligomeric GlyRs generated in Xenopus oocytes. Dose-response analysis showed that both the potentiating and inhibitory effects of Zn2+ result from changes in apparent agonist affinity. 4. Analysis of chimeric constructs of the GlyR alpha 1- and beta-subunits revealed that the positive and negative modulatory effects of Zn2+ are mediated by different regions of the alpha 1-subunit. 5. Our data indicate the existence of distinct high- and low-affinity Zn2+ binding sites on the ligand-binding alpha-subunits of the GlyR. These sites may be implicated in the regulation of synaptic efficacy within glycinergic pathways.

Typ des Eintrags: Artikel
Erschienen: 1995
Autor(en): Laube, Bodo ; Kuhse, J. ; Rundström, N. ; Kirsch, J. ; Schmieden, V. ; Betz, H.
Art des Eintrags: Bibliographie
Titel: Modulation by zinc ions of native rat and recombinant human inhibitory glycine receptors.
Sprache: Englisch
Publikationsjahr: 1995
Titel der Zeitschrift, Zeitung oder Schriftenreihe: The Journal of physiology
Jahrgang/Volume einer Zeitschrift: 483
Kurzbeschreibung (Abstract):

1. The effect of the divalent cation Zn2+ on inhibitory glycine receptor (GlyR) currents was investigated in rat embryonic spinal cord neurons and Xenopus oocytes expressing recombinant GlyRs. 2. In cultured spinal neurons, Zn2+ potentiated glycine-induced whole-cell currents about 3-fold when applied extracellularly at concentrations of 0.5-10 microM. In contrast, higher concentrations (> 100 microM) of Zn2+ decreased the glycine response. 3. A similar biphasic modulation of glycine-induced currents by Zn2+ was also found with recombinant homo- and hetero-oligomeric GlyRs generated in Xenopus oocytes. Dose-response analysis showed that both the potentiating and inhibitory effects of Zn2+ result from changes in apparent agonist affinity. 4. Analysis of chimeric constructs of the GlyR alpha 1- and beta-subunits revealed that the positive and negative modulatory effects of Zn2+ are mediated by different regions of the alpha 1-subunit. 5. Our data indicate the existence of distinct high- and low-affinity Zn2+ binding sites on the ligand-binding alpha-subunits of the GlyR. These sites may be implicated in the regulation of synaptic efficacy within glycinergic pathways.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme
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Hinterlegungsdatum: 12 Apr 2011 11:20
Letzte Änderung: 05 Mär 2019 06:48
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