Alternative splicing generates two variants of the α1 subunit of the inhibitory glycine receptor

Maria Luisa Malosio, Gabriele Grenningloh, Jochen Kuhse, Volker Schmieden, Bertram Schmitt, Peter Prior, Heinrich Betz

Research output: Contribution to journalArticlepeer-review

Abstract

The inhibitory glycine receptor (GlyR) in mammalian spinal cord displays pharmacological and molecular heterogeneity of its strychnine binding α subunit. Here, cDNAs were isolated which encode a variant (αins 1) of the rat GlyR α1 subunit that contains eight additional amino acids in its putative cytoplasmic domain. Analysis of the corresponding genomic sequence showed that αins 1 transcripts result from alternative splice acceptor site selection. S1 nuclease protection experiments, Northern blot analysis, and RNA amplification by polymerase chain reaction revealed α1 and αins 1 mRNA in postnatal spinal cord, but not in other brain regions. Expression of synthetic αins 1 RNA in Xenopus oocytes generated glycine-gated strychnine-sensitive chloride channels. These data indicate that alternative splicing contributes to GlyR α subunit heterogeneity in the mammalian central nervous system.

Original languageEnglish
Pages (from-to)2048-2053
Number of pages6
JournalJournal of Biological Chemistry
Volume266
Issue number4
Publication statusPublished - Feb 5 1991

ASJC Scopus subject areas

  • Biochemistry

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