Göke R, Just R, Lankat-Buttgereit B, Göke B
Department of Internal Medicine, Philipps-University of Marburg, Germany.
Peptides. 1994;15(4):675-81. doi: 10.1016/0196-9781(94)90095-7.
The GLP-1 receptor on RINm5F cells is a glycoprotein with a M(r) of 63,000. Treatment of the receptor with glycopeptidase F generated a protein with a M(r) of 51,000, indicating that the GLP-1 receptor contains N-linked glycans. Tunicamycin pretreatment concentration-dependently decreased GLP-1 binding to RINm5F cells due to a decreased receptor number without change of receptor affinity. Tunicamycin exerted no effect on the GLP-1 receptor mRNA expression. The stimulation of cAMP production was decreased in tunicamycin-treated cells. Our data show that glycosylation of the GLP-1 receptor is a precondition for regular receptor function.
RINm5F细胞上的GLP-1受体是一种糖蛋白，相对分子质量为63,000。用糖肽酶F处理该受体可产生一种相对分子质量为51,000的蛋白质，这表明GLP-1受体含有N-连接聚糖。衣霉素预处理由于受体数量减少而浓度依赖性地降低了GLP-1与RINm5F细胞的结合，而受体亲和力没有变化。衣霉素对GLP-1受体mRNA表达没有影响。在衣霉素处理的细胞中，cAMP生成的刺激作用减弱。我们的数据表明，GLP-1受体的糖基化是受体正常功能的前提条件。
