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Stimulation of cloned human glucagon‐like peptide 1 receptor expressed in HEK 293 cells induces cAMP‐dependent activation of calcium‐induced calcium release
Author(s) -
Gromada Jesper,
Rorsman Patrik,
Dissing Steen,
Wulff Birgitte S.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01070-u
Subject(s) - calcium , hek 293 cells , stimulation , chemistry , receptor , microbiology and biotechnology , glucagon like peptide 1 , glucagon , glucagon like peptide 1 receptor , peptide , biophysics , endocrinology , medicine , biochemistry , biology , agonist , hormone , type 2 diabetes , diabetes mellitus , organic chemistry
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.