Abstract
The actions of glucagon-like peptide-1(7–36)amide (GLP-1(7–36)amide) on cellular signalling were studied in human embryonal kidney 293 (HEK 293) cells stably transfected with the cloned human GLP-1 receptor. The cloned GLP-1 receptor showed a single high-affinity binding site ( K d = 0.76 nM). Binding of GLP-1(7–36)amide stimulated cAMP production in a dose-dependent manner (EC 50 = 0.015 nM) and caused an increase in the intracellular free Ca 2+ concentration ([Ca 2+] i). The latter effect reflected Ca 2+-induced Ca 2+ release and was suppressed by ryanodine. We propose that the ability of GLP-1(7–36)amide to increase [Ca 2+] i results from sensitization of the ryanodine receptors by a protein kinase A dependent mechanism.
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