Abstract
FAST excitatory transmission in the vertebrate central nervous system is mediated mainly by L-glutamate. On the basis of pharmacological, physiological and agonist binding properties, the ionotropic glutamate receptors are classified into NMDA (N-methyl-D-aspartate), AMPA (α-amino-3-hydroxy-5-methyl-isoxazoIe-4-propionate) and kainate subtypes1. Sequence homology between complementary DNA clones encoding non-NMDA glutamate receptor subunits reveals at least two subunit classes: the GluRl to GluR4 class2–6 and the GluRS class7. Here we report the cloning and expression of a functional rat glutamate receptor subunit cDNA, GluR6, which has a very different pharmacology from that of the GluRl–GluR4 class. Receptors generated from the GluRl-GluR4 class have a higher apparent affinity for AMPA than for kainate3–6. When expressed in Xenopus oocytes the homomeric GluR6 receptor is activated by kainate, quisqualate and L-glutamate but not by AMPA, and the apparent affinity for kainate is higher than for receptors from the GluRl–GluR4 class. Desensitization of the receptor was observed with continuous application of agonist. The homomeric GluR6 glutamate receptor exhibits an outwardly rectifying current–voltage relationship. In situ hybridizations reveal a pattern of GluR6 gene expression reminiscent of the binding pattern obtained with [3H]kainate.
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Egebjerg, J., Bettler, B., Hermans-Borgmeyer, I. et al. Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA. Nature 351, 745–748 (1991). https://doi.org/10.1038/351745a0
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DOI: https://doi.org/10.1038/351745a0
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