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Epac2-dependent rap1 activation and the control of islet insulin secretion by glucagon-like peptide-1 Leech CA; Chepurny OG; Holz GGVitam Horm 2010[]; 84 (ä): 279-302Glucagon-like peptide-1 (GLP-1) binds its Class II G protein-coupled receptor to stimulate cyclic adenosine monophosphate (cAMP) production and to potentiate the glucose metabolism-dependent secretion of insulin from pancreatic beta cells located within the islets of Langerhans. Prior clinical studies demonstrate that this cAMP-mediated action of GLP-1 to potentiate glucose-stimulated insulin secretion (GSIS) is of major therapeutic importance when evaluating the abilities of GLP-1 receptor (GLP-1R) agonists to lower levels of blood glucose in type 2 diabetic subjects. Surprisingly, recent in vitro studies of human or rodent islets of Langerhans provide evidence for the existence of a noncanonical mechanism of beta cell cAMP signal transduction, one that may explain how GLP-1R agonists potentiate GSIS. What these studies demonstrate is that a cAMP-regulated guanine nucleotide exchange factor designated as Epac2 couples beta cell cAMP production to the protein kinase A-independent stimulation of insulin exocytosis. Provided here is an overview of the Epac2 signal transduction system in beta cells, with special emphasis on Rap1, a Ras-related GTPase that is an established target of Epac2.|Animals[MESH]|Glucagon-Like Peptide 1/metabolism/*physiology[MESH]|Glucagon-Like Peptide-1 Receptor[MESH]|Guanine Nucleotide Exchange Factors/*metabolism[MESH]|Humans[MESH]|Insulin-Secreting Cells/*metabolism[MESH]|Receptors, Glucagon/*metabolism[MESH]|rap1 GTP-Binding Proteins/*metabolism[MESH] |
