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PMID:2155780
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| Citation |
Grenningloh, G, Schmieden, V, Schofield, PR, Seeburg, PH, Siddique, T, Mohandas, TK, Becker, CM and Betz, H (1990) Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes. EMBO J. 9:771-6 |
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| 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. |
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| Keywords |
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 |
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