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.
|Number of pages||6|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - Feb 5 1991|
ASJC Scopus subject areas