A SINGLE AMINO-ACID EXCHANGE ALTERS THE PHARMACOLOGY OF NEONATAL RAT GLYCINE RECEPTOR SUBUNIT

被引:167
作者
KUHSE, J
SCHMIEDEN, V
BETZ, H
机构
[1] Zentrum für Molekulare Biologie Heidelberg Universität Heidelberg Im Neuenheimer Feld 282
关键词
D O I
10.1016/0896-6273(90)90346-H
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
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 alpha subunit cDNA (alpha-2*) that generates chloride channels of low strychnine sensitivity upon expression in Xenopus oocytes. Comparison with the highly homologous human alpha-2 polypeptide and site-directed mutagenesis identified a single amino acid exchange at position 167 that causes the altered pharmacology of alpha2* receptors. Amplification by the polymerase chain reaction revealed a strong decrease in alpha-2* mRNA abundancy during postnatal spinal cord development. These data indicate that alpha-2* represents a ligand binding subunit of the previously identified neonatal GlyR isoform of low strychnine affinity.
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收藏
页码:867 / 873
页数:7
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