Alpha subunit variants of the human glycine receptor: Primary structures, functional expression and chromosomal localization of the corresponding genes

Gabriele Grenningloh, Volker Schmieden, Peter R. Schofield, Peter H. Seeburg, Teepu Siddique, Thuluvancheri K. Mohandas, Cord Michael Becker, Heinrich Betz

Research output: Contribution to journalArticlepeer-review

227 Scopus citations

Abstract

Two cDNAs encoding variants (α1 and α2) of the strychnine binding subunit of the inhibitory glycine receptor (GlyR) were isolated from a human fetal brain cDNA library. The predicted amino acid sequences exhibit ~ 99% and ~ 76% identity to the previously characterized rat 48 kd polypeptide. Heterologous expression of the human α1 and α2 subunits in Xenopous oocytes resulted in the formation of glycine-gated strychnine-sensitive chloride channels, indicating that both polypeptides can form functional GlyRs. Using a panel of rodent-human hybrid cell lines, the gene encoding α2 was mapped to the short arm (Xp21.2-p22.1) of the human X chromosome. In contrast, the α1 subunit gene is autosomally located. These data indicate molecular heterogeneity of the human GlyR at the level of α subunit genes.

Original languageEnglish (US)
Pages (from-to)771-776
Number of pages6
JournalEMBO Journal
Volume9
Issue number3
DOIs
StatePublished - 1990

Keywords

  • X chromosome
  • glycine
  • oocyte expression
  • receptor heterogeneity
  • strychnine
  • synaptic receptor

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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