Glucagon-like peptide-1-(7-36) amide, oxyntomodulin, and glucagon interact with a common receptor in a somatostatin-secreting cell line.

Détails

ID Serval
serval:BIB_B1F5A87AE58B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Glucagon-like peptide-1-(7-36) amide, oxyntomodulin, and glucagon interact with a common receptor in a somatostatin-secreting cell line.
Périodique
Endocrinology
Auteur(s)
Gros L., Thorens B., Bataille D., Kervran A.
ISSN
0013-7227
Statut éditorial
Publié
Date de publication
08/1993
Peer-reviewed
Oui
Volume
133
Numéro
2
Pages
631-638
Langue
anglais
Résumé
Glucagon-like peptide-1(7-36)amide (tGLP-1), oxyntomodulin (OXM), and glucagon are posttranslational end products of the glucagon gene expressed in intestinal L-cells. In vivo, these peptides are potent inhibitors of gastric acid secretion via several pathways, including stimulation of somatostatin release. We have examined the receptors through which these peptides stimulate somatostatin secretion using the somatostatin-secreting cell line RIN T3. tGLP-1, OXM, and glucagon stimulated somatostatin release and cAMP accumulation in RIN T3 cells to similar maximum levels, with ED50 values close to 0.2, 2, and 50 nM and 0.02, 0.3, and 8 nM, respectively. Binding of [125I]tGLP-1, [125I]OXM, and [125I]glucagon to RIN T3 plasma membranes was inhibited by the three peptides, with relative potencies as follows: tGLP-1 > OXM > glucagon. Whatever the tracer used, the IC50 for tGLP-1 was close to 0.15 nM and was shifted rightward for OXM and glucagon by about 1 and 2-3 orders of magnitude, respectively. Scatchard analyses for the three peptides were compatible with a single class of receptor sites displaying a similar maximal binding close to 2 pmol/mg protein. In the hamster lung fibroblast cell line CCL39 transfected with the receptor for tGLP-1, binding of [125I]tGLP-1 was inhibited by tGLP-1, OXM, and glucagon, with relative potencies close to those obtained with RIN T3 membranes. Chemical cross-linking of [125I]tGLP-1, [125I]OXM, and [125I]glucagon revealed a single band at 63,000 mol wt, the intensity of which was dose-dependently reduced by all three peptides. These data suggest that in the somatostatin-secreting cell line RIN T3, OXM and glucagon stimulate somatostatin release through a tGLP-1-preferring receptor. This suggests that some biological effects, previously described for these peptides, might be due to their interaction with this receptor.
Mots-clé
Animals, Binding, Competitive, Blotting, Northern, Cell Line, Cell Membrane, Cricetinae, Cross-Linking Reagents, Cyclic AMP, Fibroblasts, Glucagon, Glucagon-Like Peptide 1, Glucagon-Like Peptides, Oxyntomodulin, Peptide Fragments, Receptors, Cell Surface, Receptors, Glucagon, Somatostatin, Transfection
Pubmed
Web of science
Création de la notice
24/01/2008 13:41
Dernière modification de la notice
20/08/2019 15:20
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