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B. Beck


The gastrointestinal hormone, gastric inhibitory polypeptide (GIP), has been isolated and characterized because of its enterogastrone-type effects. It is also named glucose-dependent insulinotropic polypeptide and is actually considered to be the main incretin factor of the entero-insular axis. Besides these well-described effects on gastric secretion and pancreatic β cells, it also has direct metabolic effects on other tissues and organs, such as adipose tissue, liver, muscle, gastrointestinal tract and brain. In adipose tissue it is involved in the activation and regulation of lipoprotein lipase (LPL); it also inhibits glucagon-induced lipolysis and potentiates the effect of insulin on incorporation of fatty acids into triglycerides. It may play a role in the development of obesity because of the hypersensitivity of adipose tissue of obese animals to some of these actions. In the liver it does not modify insulin extraction, and its incretin effects are due only to the stimulation of insulin secretion and synthesis. It reduces hepatic glucose output and inhibits glucagon-stimulated glycogenolysis. It might increase glucose utilization in peripheral tissues such as muscle. GIP also has an effect on the volume and/or electrolyte composition of intestinal secretion and saliva. The functional importance of its effect on the hormones of the anterior pituitary lobe remains to be established, as it has never been detected in the brain.

Its links with insulin are very close and the presence of insulin is sometimes necessary for the greater efficiency of both hormones. GIP can be considered as a true metabolic hormone, with most of its functions tending to increase anabolism.

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Yu-Feng Zhao, Damien J Keating, Maria Hernandez, Dan Dan Feng, Yulong Zhu, and Chen Chen

Introduction Normal glucose homeostasis requires finely controlled orchestration of insulin secretion in response to subtle changes in blood glucose levels. Glucose-induced insulin secretion occurs when pancreatic β-cells utilize

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Riccarda Granata, Marco Volante, Fabio Settanni, Carlotta Gauna, Corrado Ghé, Marta Annunziata, Barbara Deidda, Iacopo Gesmundo, Thierry Abribat, Aart-Jan van der Lely, Giampiero Muccioli, Ezio Ghigo, and Mauro Papotti

peptides stimulated glucose-induced insulin secretion by β-cells ( Granata et al . 2007 ). However, data regarding ghrelin influence on insulin secretion are still contradictory; both inhibitory and stimulatory effects having been reported ( Date et al

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Haihua Yang and Linghai Yang

, are regulated by glucose and hormones. cAMP/PKA in pancreatic islets β cell A hallmark of T2D is an early defect in glucose-stimulated insulin secretion from pancreatic β cells ( Nolan et al . 2011 ). Following a meal, glucose

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Yang Mi, Na Guo, Tongqiang He, Jing Ji, Zhibin Li, and Pu Huang

lactate dehydrogenase A (LDHA). LDHA is usually kept in low expression level in insulin-secreting β-cells ( Sekine et al . 1994 ), and its overexpression affects glucose-induced insulin secretion ( Ainscow et al . 2000 ). We then transduced miR-410 into

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Hongjie Zhang, Jing Li, Xiangying Liang, Yun Luo, Ke Zen, and Chen-Yu Zhang

the gut lumen might underlie this L-cell response. It is known that one mechanism for sensing glucose in pancreatic endocrine β-cells is uncoupling protein 2 (UCP2)-mediated insulin secretion. UCP2 is a member of the inner mitochondrial membrane anion

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S Dubois, A M Madec, A Mesnier, M Armanet, K Chikh, T Berney, and Ch Thivolet

analyzed by IRMA to evaluate insulin secretion. Insulin secretion studies were performed using comparable islet numbers. Aliquots of supernatants were stored at −20 °C until insulin concentrations were measured by a highly specific IRMA (BI-insulin IRMA

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Pierre Moulin, Yves Guiot, Jean-Christophe Jonas, Jacques Rahier, Olivier Devuyst, and Jean-Claude Henquin

Introduction Pancreatic β cells adjust insulin secretion to the ambient concentration of glucose and other nutrients through changes in their metabolism ( Newgard 2002 , MacDonald et al. 2005 a , Matschinsky et al. 2006

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Jenny Vikman, Xiaosong Ma, Gregory H Hockerman, Patrik Rorsman, and Lena Eliasson

, Nagamatsu et al. 1999 ) and in insulin-secreting cell lines ( Jacobsson et al. 1994 , Martin et al. 1995 , Oho et al. 1995 , Wheeler et al. 1996 ). The requirement for syntaxin 1 in insulin secretion has previously been demonstrated by inclusion

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Horng-Yih Ou, Hung-Tsung Wu, Feng-Hwa Lu, Yu-Chu Su, Hao-Chang Hung, Jin-Shang Wu, Yi-Ching Yang, Chao-Liang Wu, and Chih-Jen Chang

physiological functions contribute to insulin secretion ( Itoh et al . 2003 ). Activation of FFAR1 increases phospholipase C (PLC) activity through the Gq protein to facilitate insulin secretion ( Feng et al . 2006 ). In addition, results from recent studies