Glycosylation of the GLP-1 receptor is a prerequisite for regular receptor function.

@article{Gke1994GlycosylationOT,
  title={Glycosylation of the GLP-1 receptor is a prerequisite for regular receptor function.},
  author={R{\"u}diger G{\"o}ke and Rebecca S. Just and B. Lankat-Buttgereit and Burkhard J. G{\"o}ke},
  journal={Peptides},
  year={1994},
  volume={15 4},
  pages={675-81}
}
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… CONTINUE READING