Glutamate and glycine decrease the affinity of [3H]MK-801 binding in the presence of Mg2+.

G von Euler; Y Liu

doi:10.1016/0922-4106(93)90102-f

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Glutamate and glycine decrease the affinity of [3H]MK-801 binding in the presence of Mg2+.

G von Euler·Y Liu

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Abstract

The NMDA receptor is coupled to a cation-selective ion channel, which has been implicated in important brain functions such as long-term potentiation and burst firing, and in neuronal death associated with stroke and epilepsy. We have investigated the binding properties of [3H]MK-801, which binds selectively to the open state of the NMDA channel, at physiological concentrations of Mg2+ in membrane preparations of the rat cerebral cortex. Glutamate and glycine were found to enhance [3H]MK-801 binding at low concentrations and inhibit [3H]MK-801 binding at high concentrations. The inhibition of [3H]MK-801 binding was due to an enhancement of the dissociation rate constant and was reversed by competitive glutamate and glycine antagonists. These findings could be explained by a glutamate- and glycine-induced decrease in the affinity of [3H]MK-801 binding sites within activated NMDA channels, in the presence of Mg2+. This decrease in [3H]MK-801 affinity may correspond to a decreased affinity of the site where Mg2+ causes a voltage-dependent block of the NMDA channel.

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Animals Binding, Competitive Cerebral Cortex Dizocilpine Maleate Glutamates Glutamic Acid Glycine In Vitro Techniques Ion Channels Magnesium Male Rats Rats, Sprague-Dawley Receptors, N-Methyl-D-Aspartate Journal Article Research Support, Non-U.S. Gov't

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G von Euler, Y Liu. 1993-05-15. Glutamate and glycine decrease the affinity of [3H]MK-801 binding in the presence of Mg2+.. https://doi.org/10.1016/0922-4106(93)90102-f

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