Characterization of high-affinity receptors for truncated glucagon-like peptide-1 in rat gastric glands

FEBS Lett. 1990 Mar 12;262(1):139-41. doi: 10.1016/0014-5793(90)80173-g.


The truncated form of glucagon-like peptide-1 (TGLP-1, or proglucagon 78-108), secreted by the mammalian intestine, has potent pharmacological activities, stimulating insulin release and inhibiting gastric acid secretion. We have characterized high-affinity receptors for this peptide in rat isolated fundic glands. Scatchard analysis of binding studies using mono-125I-TGLP-1(7-36) amide as tracer showed a single class of binding site of Kd (4.4 +/- (SE) .08) x 10(-10) M, with a tissue concentration of 1.0 +/- 0.1 fmol sites/microgram DNA. Whole GLP-1 was approximately 700 times less potent in displacing tracer, while human GLP-2 and pancreatic glucagon produced no significant displacement at concentrations up to 10(-6) M. The data support a physiological role for TGLP-1 in the regulation of gastric acid secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cyclic AMP / biosynthesis
  • Gastric Acid / metabolism
  • Gastric Mucosa / analysis*
  • Glucagon / metabolism*
  • Glucagon / pharmacology
  • Glucagon-Like Peptide 1
  • In Vitro Techniques
  • Male
  • Peptide Fragments / metabolism*
  • Peptide Fragments / pharmacology
  • Protein Precursors / metabolism*
  • Protein Precursors / pharmacology
  • Rats
  • Rats, Inbred Strains
  • Receptors, Cell Surface / analysis*


  • Peptide Fragments
  • Protein Precursors
  • Receptors, Cell Surface
  • Glucagon-Like Peptide 1
  • Glucagon
  • Cyclic AMP