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

Peptides. 1994;15(4):675-81. doi: 10.1016/0196-9781(94)90095-7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / pharmacology
  • Glucagon / metabolism*
  • Glucagon-Like Peptide 1
  • Glucagon-Like Peptide-1 Receptor
  • Glucagon-Like Peptides
  • Glycosylation
  • Insulin / metabolism*
  • Insulin Secretion
  • Islets of Langerhans / cytology
  • Islets of Langerhans / drug effects
  • Islets of Langerhans / metabolism*
  • Molecular Weight
  • Peptide Fragments / drug effects
  • Peptide Fragments / metabolism*
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Receptors, Cell Surface / drug effects
  • Receptors, Cell Surface / metabolism*
  • Receptors, Glucagon*
  • Tumor Cells, Cultured
  • Tunicamycin / pharmacology

Substances

  • Glucagon-Like Peptide-1 Receptor
  • Insulin
  • Peptide Fragments
  • Receptors, Cell Surface
  • Receptors, Glucagon
  • Tunicamycin
  • glucagon-like peptide 1 (7-36)amide
  • Glucagon-Like Peptides
  • Glucagon-Like Peptide 1
  • Glucagon
  • Amidohydrolases
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase