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Berit Svendsen, Ramona Pais, Maja S Engelstoft, Nikolay B Milev, Paul Richards, Charlotte B Christiansen, Kristoffer L Egerod, Signe M Jensen, Abdella M Habib, Fiona M Gribble, Thue W Schwartz, Frank Reimann and Jens J Holst

Introduction The incretin hormones, glucagon-like peptide-1 (GLP1) and glucose-dependent insulinotropic polypeptide (GIP) strongly potentiate postprandial insulin secretion and are therefore important regulators of glucose homeostasis. They are

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Eun Young Lee, Shuji Kaneko, Promsuk Jutabha, Xilin Zhang, Susumu Seino, Takahito Jomori, Naohiko Anzai and Takashi Miki

Introduction Oral ingestion of nutrients triggers the secretion of gut hormones from various enteroendocrine cells ( Ezcurra et al . 2013 , Cho et al . 2014 ). Among these, glucagon-like peptide 1 (GLP1) and glucose-dependent insulinotropic

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J C Parker, K S Lavery, N Irwin, B D Green, B Greer, P Harriott, F P M O’Harte, V A Gault and P R Flatt

Introduction Glucose-dependent insulinotrophic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) are important gastrointestinal-releasing hormones involved in the regulation of postprandial nutrient homeostasis ( Meier et al

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G Üçkaya, P Delagrange, A Chavanieu, G Grassy, M-F Berthault, A Ktorza, E Cerasi, G Leibowitz and N Kaiser

that aim to improve β-cell function and survival. Glucagon-like peptide 1 (GLP-1) is a potent incretin hormone secreted by the intestinal L cells in response to food intake ( Drucker 2001 ). GLP-1 exerts multiple effects on pancreatic β

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Yolanda Diz-Chaves, Manuel Gil-Lozano, Laura Toba, Juan Fandiño, Hugo Ogando, Lucas C González-Matías and Federico Mallo

and GCs impose a trend towards the development of obesity and diabetes in adulthood. Finally, we consider how the agonists of the GLP-1 receptor (GLP-1R) can interfere with these processes, modulating the activity of the HPA axis, the SNS and the

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MA Luque, N Gonzalez, L Marquez, A Acitores, A Redondo, M Morales, I Valverde and ML Villanueva-Penacarrillo

Glucagon-like peptide-1 (GLP-1) has been shown to have insulin-like effects upon the metabolism of glucose in rat liver, muscle and fat, and on that of lipids in rat and human adipocytes. These actions seem to be exerted through specific receptors which, unlike that of the pancreas, are not - at least in liver and muscle - cAMP-associated. Here we have investigated the effect, its characteristics, and possible second messengers of GLP-1 on the glucose metabolism of human skeletal muscle, in tissue strips and primary cultured myocytes. In muscle strips, GLP-1, like insulin, stimulated glycogen synthesis, glycogen synthase a activity, and glucose oxidation and utilization, and inhibited glycogen phosphorylase a activity, all of this at physiological concentrations of the peptide. In cultured myotubes, GLP-1 exerted, from 10(-13) mol/l, a dose-related increase of the D-[U-(14)C]glucose incorporation into glycogen, with the same potency as insulin, together with an activation of glycogen synthase a; the effect of 10(-11) mol/l GLP-1 on both parameters was additive to that induced by the equimolar amount of insulin. Synthase a was still activated in cells after 2 days of exposure to GLP-1, as compared with myotubes maintained in the absence of peptide. In human muscle cells, exendin-4 and its truncated form 9-39 amide (Ex-9) are both agonists of the GLP-1 effect on glycogen synthesis and synthase a activity; but while neither GLP-1 nor exendin-4 affected the cellular cAMP content after 5-min incubation in the absence of 3-isobutyl-1-methylxantine (IBMX), an increase was detected with Ex-9. GLP-1, exendin-4, Ex-9 and insulin all induced the prompt hydrolysis of glycosylphosphatidylinositols (GPIs). This work shows a potent stimulatory effect of GLP-1 on the glucose metabolism of human skeletal muscle, and supports the long-term therapeutic value of the peptide. Further evidence for a GLP-1 receptor in this tissue, different from that of the pancreas, is also illustrated, suggesting a role for an inositolphosphoglycan (IPG) as at least one of the possible second messengers of the GLP-1 action in human muscle.

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Paul Millar, Nupur Pathak, Vadivel Parthsarathy, Anthony J Bjourson, Maurice O’Kane, Varun Pathak, R Charlotte Moffett, Peter R Flatt and Victor A Gault

surge in the number of new drug classes such as glucagon-like peptide-1 (GLP-1) agonists, dipeptidylpeptidase-4 (DPP4) inhibitors and sodium glucose cotransporter-2 (SGLT2) inhibitors ( Bailey et al . 2016 ). Although these agents may be used as

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Yingxin Xian, Zonglan Chen, Hongrong Deng, Mengyin Cai, Hua Liang, Wen Xu, Jianping Weng and Fen Xu

visceral omental fat in subjects with obesity exhibit severely impaired endothelium-dependent vasodilation ( Farb et al. 2012 ). Clinical studies demonstrated that exenatide, a glucagon-like peptide 1 (GLP-1) receptor agonist, improved glycemic control

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Rebecca McGirr, Leonardo Guizzetti and Savita Dhanvantari

al . 1994 , Furuta et al . 2001 ). By contrast, proglucagon is processed to glucagon-like peptide (GLP)-1 and GLP-2 in the intestine and brain by PC1/3 ( Dhanvantari et al . 1996 , Dhanvantari & Brubaker 1998 , Damholt et al . 1999 ). Glucagon

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Alyce M Martin, Emily W Sun and Damien J Keating

-like peptide 1 (GLP-1), peptide YY (PYY) and oxyntomodulin (OXM), and glucose-dependent insulinotropic peptide (GIP) secreting K cells. It is now clear that such a classification system is not accurate given the accumulation of evidence that cross-over in