Abstract
N-Methyl-D-aspartic acid (NMDA)-sensitive subclass of the synaptic receptors for central excitatory amino acid neurotransmitters is supposed to form a receptor ion channel complex with modulatory glycine (Gly) binding sites which are insensitive to a classical Gly antagonist strychnine (for example, see review by Robinson and Coyle, 1987), based on the electrophysiological findings that Gly drastically potentiates in a strychnine-insensitive manner currents mediated by the NMDA-sensitive subclass without affecting those mediated by the other subclasses in cultured neuronal cells (Johnson and Ascher, 1987). The complex consists of at least three distinctly different sites; 1) NMDA recognition sites, 2) ion channel sites and 3) Gly recognition sites. The latter strychnine-insensitive Gly sites are referred to as GlyB sites to differentiate them from the strychnine-sensitive GlyA sites just for convenience’ sake (Ogita et al., 1989).
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© 1991 Plenum Press, New York
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Yoneda, Y., Ogita, K. (1991). Novel Fourth Binding Sites of [3H]Spermidine within the NMDA Receptor Complex. In: Kito, S., Segawa, T., Olsen, R.W. (eds) Neuroreceptor Mechanisms in Brain. Advances in Experimental Medicine and Biology, vol 287. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5907-4_40
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