Ligand-specificity of the rat GLP-I receptor recombinantly expressed in Chinese hamster ovary (CHO-) cells

Z Gastroenterol. 1994 Apr;32(4):203-7.


Glucagon-like peptide-I (GLP-I) is a potent incretin hormone and is considered as a new therapeutic tool in the treatment of diabetes mellitus. This study was designed to precisely characterize the binding behavior and activation of the recombinant GLP-I receptor against naturally occurring ligands of the glucagon/VIP/secretin peptide hormone family. CHO-cells were stably transfected with a plasmid containing a cDNA encoding for the rat GLP-I receptor. Northern blot analysis with this cDNA showed a single band of 2.7 kb in CHO cells, while in RINm5F cells, three bands of 2.7, 3.4, and 3.6 kb were specifically labelled. In receptor-binding studies 125I-GLP-I was displaced by GLP-I and weakly by PHI and oxyntomodulin but not by helodermin, helospectin I, helospectin II, secretin, VIP, and PACAP-38. Intracellular cAMP generation was stimulated by GLP-I, PHI, and oxyntomodulin. Helodermin, helospectin I, helospectin II, secretin, VIP, and PACAP-38 were not able to displace 125I-GLP-I from its receptor or to stimulate intracellular cAMP production. This data shows that the GLP-I receptor is characterized by a high ligand specificity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Northern
  • CHO Cells
  • Cricetinae
  • Cyclic AMP / metabolism
  • Glucagon / genetics*
  • Glucagon-Like Peptide 1
  • Glucagon-Like Peptide-1 Receptor
  • Peptide Fragments / genetics*
  • Protein Precursors / genetics*
  • Rats
  • Receptors, Cell Surface / genetics*
  • Receptors, Glucagon*
  • Recombinant Proteins
  • Transfection / genetics*


  • Glp1r protein, rat
  • Glucagon-Like Peptide-1 Receptor
  • Peptide Fragments
  • Protein Precursors
  • Receptors, Cell Surface
  • Receptors, Glucagon
  • Recombinant Proteins
  • Glucagon-Like Peptide 1
  • Glucagon
  • Cyclic AMP