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  • Title: Binding specificity and signal transduction of receptors for glucagon-like peptide-1(7-36)amide and gastric inhibitory polypeptide on RINm5F insulinoma cells.
    Author: Gallwitz B, Witt M, Fölsch UR, Creutzfeldt W, Schmidt WE.
    Journal: J Mol Endocrinol; 1993 Jun; 10(3):259-68. PubMed ID: 8396943.
    Abstract:
    Glucagon-like peptide-1(7-36)amide (GLP-1(7-36) amide) and gastric inhibitory polypeptide (GIP), peptides of the glucagon family, stimulate insulin secretion in vitro and in vivo. They possess high N-terminal sequence homology. Binding studies with 125I-labelled GIP and 125I-labelled GLP-1(7-36)amide were performed in RINm5F insulinoma cells to investigate receptor specificity and to compare both receptors directly. Both binding sites were highly ligand-specific: GIP did not bind to the GLP-1(7-36)amide receptor and vice versa. Both peptides increased intracellular cyclic AMP levels; GLP-1(7-36)amide was 100-fold more potent in stimulating cyclic AMP production when compared with GIP. At ranges of 1-10 nmol GLP-1(7-36)amide/l and 0.1-10 nmol GIP/l, corresponding to submaximal binding concentrations, the hormones showed an additive effect on cyclic AMP production. The N-terminal portion of GIP was important for binding, as GIP(1-30) showed almost full binding and biological activity. GIP(17-42) bound in a concentration-dependent manner with approximately 500-fold lower potency than GIP. At concentrations of up to 10 mumol GIP(17-42)/l no stimulation of cyclic AMP was observed.
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