Alternative splicing generates two isoforms of the alpha 2 subunit of the inhibitory glycine receptor

The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein which displays developmental heterogeneity in the mammalian central nervous system. Here we describe 2 novel cDNA variants of the rat GlyR alpha 2 subunit and demonstrate that alternative splicing generates these 2 iso...

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Bibliographic Details
Published in:FEBS letters 1991-05, Vol.283 (1), p.73-77
Main Authors: Kuhse, J, Kuryatov, A, Maulet, Y, Malosio, M L, Schmieden, V, Betz, H
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Brain Chemistry
Gene Expression Regulation
glycine
Glycine - metabolism
Mice
Molecular Sequence Data
Nucleic Acid Hybridization
Oligonucleotide Probes
Oligonucleotides, Antisense - genetics
Rats
Receptors, Glycine
Receptors, Neurotransmitter - genetics
Receptors, Neurotransmitter - metabolism
RNA Splicing
Xenopus
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Summary:The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein which displays developmental heterogeneity in the mammalian central nervous system. Here we describe 2 novel cDNA variants of the rat GlyR alpha 2 subunit and demonstrate that alternative splicing generates these 2 isoforms. The deduced protein sequences (alpha 2A and alpha 2B) exhibit 99% identity with the previously characterized human alpha 2 subunit. In situ hybridization revealed expression of both alpha 2A and alpha 2B mRNAs in the prenatal rat brain, suggesting that these variant proteins may have a role in synaptogenesis. Heterologous expression in Xenopus oocytes showed that the more abundantly expressed alpha 2A subunit forms strychnine-sensitive ion channels which resemble human alpha 2 subunit GlyRs in their electrophysiological properties.
ISSN:0014-5793