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

• Published in: FEBS letters Vol. 262; no. 1; pp. 139 - 141
• Main Authors: Uttenthal, L.O., Blázquez, E.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 12.03.1990
• Subjects: Animals; Cyclic AMP - biosynthesis; Fundic gland; Gastric Acid - metabolism; gastric glands; Gastric mucosa; Gastric Mucosa - analysis; Glucagon - metabolism; Glucagon - pharmacology; Glucagon-Like Peptide 1; In Vitro Techniques; Male; Peptide Fragments - metabolism; Peptide Fragments - pharmacology; Proglucagon 78–108; Protein Precursors - metabolism; Protein Precursors - pharmacology; Rats; Rats, Inbred Strains; Receptor; Receptors, Cell Surface - analysis; Fundic gland; Proglucagon 78–108; Receptor; Gastric mucosa
• ISSN: 0014-5793; 1873-3468
• 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-l(7–36) amide as tracer showed a single class of binding site of K d (4.4±(SE) 0.8) × 10 −10 M, with a tissue concentration of 1.0 ± 0.1 fmol sites/μg 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.