Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kuhse J,Kuryatov A,Maulet Y,Malosio ML,Schmieden V,Betz Hdoi
10.1016/0014-5793(91)80557-jkeywords:
subject
Has Abstractpub_date
1991-05-20 00:00:00pages
73-7issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(91)80557-Jjournal_volume
283pub_type
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