Neuron
Volume 5, Issue 6, December 1990, Pages 867-873
Journal home page for Neuron

A single amino acid exchange alters the pharmacology of neonatal rat glycine receptor subunit

https://doi.org/10.1016/0896-6273(90)90346-HGet rights and content

Abstract

Agonist activation of the inhibitory glycine receptor (GlyR) in the adult vertebrate CNS is efficiently antagonized by the alkaloid strychnine. Here, we describe a novel rat GlyR α subunit cDNA (α2∗) that generates chloride channels of low strychnine sensitivity upon expression in Xenopus oocytes. Comparison with the highly homologous human α2 polypeptide and site-directed mutagenesis identified a single amino acid exchange at position 167 that causes the altered pharmacology of α2∗ receptors. Amplification by the polymerase chain reaction revealed a strong decrease in α2∗ mRNA abundancy during postnatal spinal cord development. These data indicate that α2∗ represents a ligand binding subunit of the previously identified neonatal GlyR isoform of low strychnine affinity.

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    Present address: Max-Planck-Institut für Hirnforschung Deutschordenstrasse 46, D-6000 Frankfurt 71, Federal Republic of Germany.

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