Malosio M L, Grenningloh G, Kuhse J, Schmieden V, Schmitt B, Prior P, Betz H
Zentrum für Molekulare Biologie, Universität Heidelberg, Federal Republic of Germany.
J Biol Chem. 1991 Feb 5;266(4):2048-53.
The inhibitory glycine receptor (GlyR) in mammalian spinal cord displays pharmacological and molecular heterogeneity of its strychnine binding alpha subunit. Here, cDNAs were isolated which encode a variant (alpha ins 1) of the rat GlyR alpha 1 subunit that contains eight additional amino acids in its putative cytoplasmic domain. Analysis of the corresponding genomic sequence showed that alpha ins 1 transcripts result from alternative splice acceptor site selection. S1 nuclease protection experiments, Northern blot analysis, and RNA amplification by polymerase chain reaction revealed alpha 1 and alpha ins 1 mRNA in postnatal spinal cord, but not in other brain regions. Expression of synthetic alpha ins 1 RNA in Xenopus oocytes generated glycine-gated strychnine-sensitive chloride channels. These data indicate that alternative splicing contributes to GlyR alpha subunit heterogeneity in the mammalian central nervous system.
哺乳动物脊髓中的抑制性甘氨酸受体（GlyR）在其与士的宁结合的α亚基上表现出药理学和分子异质性。在此，分离出了编码大鼠GlyRα1亚基变体（αins 1）的cDNA，该变体在其假定的胞质结构域中含有另外八个氨基酸。对相应基因组序列的分析表明，αins 1转录本是由选择性剪接受体位点选择产生的。S1核酸酶保护实验、Northern印迹分析以及聚合酶链反应的RNA扩增显示，出生后脊髓中有α1和αins 1 mRNA，但在其他脑区中没有。在非洲爪蟾卵母细胞中合成αins 1 RNA的表达产生了甘氨酸门控的士的宁敏感氯离子通道。这些数据表明，选择性剪接促成了哺乳动物中枢神经系统中GlyRα亚基的异质性。
