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

EMBO J. 1990 Mar;9(3):771-6.

Abstract

Two cDNAs encoding variants (alpha 1 and alpha 2) 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 approximately 99% and approximately 76% identity to the previously characterized rat 48 kd polypeptide. Heterologous expression of the human alpha 1 and alpha 2 subunits in Xenopus 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 alpha 2 was mapped to the short arm (Xp21.2-p22.1) of the human X chromosome. In contrast, the alpha 1 subunit gene is autosomally located. These data indicate molecular heterogeneity of the human GlyR at the level of alpha subunit genes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Southern
  • Chromosome Mapping
  • Cloning, Molecular
  • DNA / genetics*
  • Gene Expression
  • Genetic Variation*
  • Glycine / metabolism*
  • Humans
  • Hybrid Cells / metabolism
  • Macromolecular Substances
  • Molecular Sequence Data
  • Nucleic Acid Hybridization
  • Oligonucleotide Probes
  • Rats
  • Receptors, Glycine
  • Receptors, Neurotransmitter / genetics*
  • Sequence Homology, Nucleic Acid
  • X Chromosome*
  • Xenopus

Substances

  • Macromolecular Substances
  • Oligonucleotide Probes
  • Receptors, Glycine
  • Receptors, Neurotransmitter
  • DNA
  • Glycine