Stimulation of cloned human glucagon-like peptide 1 receptor expressed in HEK 293 cells induces cAMP-dependent activation of calcium-induced calcium release.

Journal article

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 (Kd = 0.76 nM). Binding of GLP-1(7-36)amide stimulated cAMP production in a dose-dependent manner (EC50 = 0.015 nM) and caused an increase in the intracellular free Ca2+ concentration ([Ca2+]i). The latter effect reflected Ca(2+)-induced Ca2+ release and was suppressed by ryanodine. We propose that the ability of GLP-1(7-36)amide to increase [Ca2+]i results from sensitization of the ryanodine receptors by a protein kinase A dependent mechanism.

Authors: Gromada, J; Rorsman, P; Dissing, S; Wulff, B

• Publication status: Published
• Journal: FEBS letters
• Volume: 373
• Issue: 2
• Pages: 182-186
• Publication date: 1995-10-01
• DOI: 10.1016/0014-5793(95)01070-u
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Humans; Thionucleotides; Ryanodine; Glucagon-Like Peptide 1; Embryo, Mammalian; Glucagon; Recombinant Proteins; Peptide Fragments; Calcium Channel Blockers; Glucagon-Like Peptides; Acetylcholine; Receptors, Glucagon; Calcium; Kidney; Cloning, Molecular; Ionomycin; Cyclic AMP; Cell Line