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J Neurophysiol 85: 912-925, 2001;
0022-3077/01 $5.00
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The Journal of Neurophysiology Vol. 85 No. 2 February 2001, pp. 912-925
Copyright ©2001 by the American Physiological Society

High-Affinity Zinc Potentiation of Inhibitory Postsynaptic Glycinergic Currents in the Zebrafish Hindbrain

Hiroshi Suwa,1 Louis Saint-Amant,3 Antoine Triller,2 Pierre Drapeau,3 and Pascal Legendre1

 1Institut des Neurosciences, Université Pierre et Marie Curie, 75252 Paris Cedex 05;  2Institut National de la Santé et de la Recherche Médicale U 497, Ecole Normale Superieure, 75005 Paris, France; and  3Center for Research in Neuroscience, McGill University, and Montreal General Hospital Research Institute, Montreal, Quebec H3G 1A4, Canada

Suwa, Hiroshi, Louis Saint-Amant, Antoine Triller, Pierre Drapeau, and Pascal Legendre. High-Affinity Zinc Potentiation of Inhibitory Postsynaptic Glycinergic Currents in the Zebrafish Hindbrain. J. Neurophysiol. 85: 912-925, 2001. Zinc has been reported to potentiate glycine receptors (GlyR), but the physiological significance of this observation has been put in doubt by the relatively high values of the EC50, 0.5-1 µM, since such concentrations may not be attained in the synaptic cleft of glycinergic synapses. We have re-evaluated this observation in the frame of the hypothesis that contaminant heavy metals present in usual solutions may have lead to underestimate the affinity of the zinc binding site, and therefore to underestimate the potential physiological role of zinc. Using chelators either to complex heavy metals or to apply zinc at controlled concentrations, we have examined the action of zinc on GlyR kinetics in outside-out patches from 50-h-old zebrafish Mauthner cells. Chelating contaminating heavy metals with tricine or N,N,N',N'-tetrakis-(2-pyridylmethyl)-ethylenediamine (TPEN) decreased the duration of the currents evoked by glycine, confirming that traces of heavy metals alter the GlyR response in control conditions. Using tricine- (10 mM) buffered zinc solution, we then showed that zinc increases the amplitude of outside-out responses evoked by 0.1-0.5 mM glycine with an EC50 of 15 nM. In contrast zinc had no effect on the amplitude of currents evoked by a saturating concentration (3-10 mM) of glycine. This suggests that zinc enhances GlyR apparent affinity for glycine. The study of the effects of zinc on the kinetics of the response indicates that this increase of apparent affinity is due to a decrease of the glycine dissociation rate constant. We then analyzed the effects of zinc on postsynaptic GlyRs in whole cell recordings of glycinergic miniature inhibitory postsynaptic currents (mIPSCs). Chelation of contaminant heavy metals decreased the amplitude and the duration of the mIPSCs; inverse effects were observed by adding zinc in buffered solutions containing nanomolar free zinc concentrations. Zinc plus tricine or tricine alone did not change the coefficient of variation (approx 0.85) of the mIPSC amplitude distributions. These results suggest that postsynaptic GlyRs are not saturated after the release of one vesicle.




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