Table of Contents Author Guidelines Submit a Manuscript
Mediators of Inflammation
Volume 2013, Article ID 591056, 9 pages
http://dx.doi.org/10.1155/2013/591056
Review Article

An Emerging Role of Glucagon-Like Peptide-1 in Preventing Advanced-Glycation-End-Product-Mediated Damages in Diabetes

1Department of Internal Medicine, University of Genoa, Viale Benedetto XV 6, 16132 Genoa, Italy
2Division of Cardiology, Geneva University Hospitals, Faculty of Medicine, Foundation for Medical Researches, Avenue de la Roseraie 64, 1211 Geneva, Switzerland
3First Medical Clinic, Laboratory of Phagocyte Physiopathology and Inflammation, Department of Internal Medicine, University of Genoa, Viale Benedetto XV 6, 16132 Genoa, Italy

Received 8 October 2012; Revised 20 December 2012; Accepted 27 December 2012

Academic Editor: Dennis D. Taub

Copyright © 2013 Alessandra Puddu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. J. Holst, “The physiology of glucagon-like peptide 1,” Physiological Reviews, vol. 87, no. 4, pp. 1409–1439, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. A. J. Garber, “Incretin effects on beta-cell function, replication, and mass: the human perspective,” Diabetes Care, vol. 34, supplement 2, pp. S258–S263, 2011. View at Google Scholar · View at Scopus
  3. S. A. Ross and J. M. Ekoé, “Incretin agents in type 2 diabetes,” Canadian Family Physician, vol. 56, no. 7, pp. 639–648, 2010. View at Google Scholar · View at Scopus
  4. D. J. Drucker and M. A. Nauck, “The incretin system: glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors in type 2 diabetes,” Lancet, vol. 368, no. 9548, pp. 1696–1705, 2006. View at Publisher · View at Google Scholar · View at Scopus
  5. R. Meerwaldt, T. Links, C. Zeebregts, R. Tio, J. L. Hillebrands, and A. Smit, “The clinical relevance of assessing advanced glycation endproducts accumulation in diabetes,” Cardiovascular Diabetology, vol. 7, article no. 29, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. R. Singh, A. Barden, T. Mori, and L. Beilin, “Advanced glycation end-products: A review,” Diabetologia, vol. 44, no. 2, pp. 129–146, 2001. View at Publisher · View at Google Scholar · View at Scopus
  7. S. F. Yan, R. Ramasamy, and A. M. Schmidt, “The RAGE axis a fundamental mechanism signaling danger to the vulnerable vasculature,” Circulation Research, vol. 106, no. 5, pp. 842–853, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. P. K. Lund, R. H. Goodman, and J. F. Habener, “Intestinal glucagon mRNA identified by hybridization to a cloned islet cDNA encoding a precursor,” Biochemical and Biophysical Research Communications, vol. 100, no. 4, pp. 1659–1666, 1981. View at Google Scholar · View at Scopus
  9. P. K. Lund, R. H. Goodman, P. C. Dee, and J. F. Habener, “Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem,” Proceedings of the National Academy of Sciences of the United States of America, vol. 79, no. 2 I, pp. 345–349, 1982. View at Google Scholar · View at Scopus
  10. P. K. Lund, R. H. Goodman, and M. R. Montminy, “Anglerfish islet pre-proglucagon II: Nucleotide and corresponding amino acid sequence of the cDNA,” Journal of Biological Chemistry, vol. 258, no. 5, pp. 3280–3284, 1983. View at Google Scholar · View at Scopus
  11. T. J. Kieffer and J. F. Habener, “The glucagon-like peptides,” Endocrine Reviews, vol. 20, no. 6, pp. 876–913, 1999. View at Google Scholar · View at Scopus
  12. R. Ugleholdt, X. Zhu, C. F. Deacon, C. Ørskov, D. F. Steiner, and J. J. Holst, “Impaired Intestinal Proglucagon Processing in Mice Lacking Prohormone Convertase 1,” Endocrinology, vol. 145, no. 3, pp. 1349–1355, 2004. View at Publisher · View at Google Scholar · View at Scopus
  13. C. Orskov, L. Rabenhoj, A. Wettergren, H. Kofod, and J. J. Holst, “Tissue and plasma concentrations of amidated and glycine-extended glucagon-like peptide I in humans,” Diabetes, vol. 43, no. 4, pp. 535–539, 1994. View at Google Scholar · View at Scopus
  14. C. Orskov, A. Wettergren, and J. J. Holst, “Biological effects and metabolic rates of glucagonlike peptide-1 7-36 amide and glucagonlike peptide-1 7-37 in healthy subjects are indistinguishable,” Diabetes, vol. 42, no. 5, pp. 658–661, 1993. View at Google Scholar · View at Scopus
  15. A. Martinez, M. A. Burrell, M. Kuijk et al., “Localization of amidating enzymes (PAM) in rat gastrointestinal tract,” Journal of Histochemistry and Cytochemistry, vol. 41, no. 11, pp. 1617–1622, 1993. View at Google Scholar · View at Scopus
  16. C. F. Deacon, M. A. Nauck, M. Toft-Nielsen, L. Pridal, B. Willms, and J. J. Holst, “Both subcutaneously and intravenously administered glucagon-like peptide I are rapidly degraded from the NH2-terminus in type II diabetic patients and in healthy subjects,” Diabetes, vol. 44, no. 9, pp. 1126–1131, 1995. View at Google Scholar · View at Scopus
  17. A. M. Lambeir, C. Durinx, S. Scharpé, and I. De Meester, “Dipeptidyl-peptidase IV from bench to bedside: An update on structural properties, functions, and clinical aspects of the enzyme DPP IV,” Critical Reviews in Clinical Laboratory Sciences, vol. 40, no. 3, pp. 209–294, 2003. View at Google Scholar · View at Scopus
  18. C. Herrmann, R. Goke, G. Richter, H. C. Fehmann, R. Arnold, and B. Goke, “Glucagon-like peptide-1 and glucose-dependent insulin releasing polypeptide plasma levels in response to nutrients,” Digestion, vol. 56, no. 2, pp. 117–126, 1995. View at Google Scholar · View at Scopus
  19. R. M. Elliott, L. M. Morgan, J. A. Tredger, S. Deacon, J. Wright, and V. Marks, “Glucagon-like peptide-1 (7-36)amide and glucose-dependent insulinotropic polypeptide secretion in response to nutrient ingestion in man: Acute post-prandial and 24-h secretion patterns,” Journal of Endocrinology, vol. 138, no. 1, pp. 159–166, 1993. View at Google Scholar · View at Scopus
  20. E. Rask, T. Olsson, S. Söderberg et al., “Impaired incretin response after a mixed meal is associated with insulin resistance in nondiabetic men,” Diabetes Care, vol. 24, no. 9, pp. 1640–1645, 2001. View at Google Scholar · View at Scopus
  21. D. J. Drucker, J. Philippe, and S. Mojsov, “Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line,” Proceedings of the National Academy of Sciences of the United States of America, vol. 84, no. 10, pp. 3434–3438, 1987. View at Google Scholar · View at Scopus
  22. J. J. Holst, C. Orskov, O. V. Nielsen, and T. W. Schwartz, “Truncated glucagon-like peptide I, an insulin-releasing hormone from the distal gut,” FEBS Letters, vol. 211, no. 2, pp. 169–174, 1987. View at Google Scholar · View at Scopus
  23. B. Kreymann, G. Williams, M. A. Ghatei, and S. R. Bloom, “Glucagon-like peptide-1 7-36: A physiological incretin in man,” Lancet, vol. 2, no. 8571, pp. 1300–1304, 1987. View at Google Scholar · View at Scopus
  24. S. Mojsov, G. C. Weir, and J. F. Habener, “Insulinotropin: Glucagon-like peptide I (7-37) co-encoded in the glucagon gene is a potent stimulator of insulin release in the perfused rat pancreas,” Journal of Clinical Investigation, vol. 79, no. 2, pp. 616–619, 1987. View at Google Scholar · View at Scopus
  25. D. J. Drucker, “Development of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes,” Current Pharmaceutical Design, vol. 7, no. 14, pp. 1399–1412, 2001. View at Publisher · View at Google Scholar · View at Scopus
  26. D. J. Drucker, “Biological actions and therapeutic potential of the glucagon-like peptides,” Gastroenterology, vol. 122, no. 2, pp. 531–544, 2002. View at Google Scholar · View at Scopus
  27. B. Thorens, “Expression cloning of the pancreatic β cell receptor for the gluco-incretin hormone glucagon-like peptide 1,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 18, pp. 8641–8645, 1992. View at Google Scholar · View at Scopus
  28. D. J. Drucker, “Enhancing incretin action for the treatment of type 2 diabetes,” Diabetes Care, vol. 26, no. 10, pp. 2929–2940, 2003. View at Publisher · View at Google Scholar · View at Scopus
  29. L. Farilla, A. Bulotta, B. Hirshberg et al., “Glucagon-like peptide 1 inhibits cell apoptosis and improves glucose responsiveness of freshly isolated human islets,” Endocrinology, vol. 144, no. 12, pp. 5149–5158, 2003. View at Publisher · View at Google Scholar · View at Scopus
  30. P. E. MacDonald, W. El-kholy, M. J. Riedel, A. M. F. Salapatek, P. E. Light, and M. B. Wheeler, “The multiple actions of GLP-1 on the process of glucose-stimulated insulin secretion,” Diabetes, vol. 51, supplement 3, pp. S434–S442, 2002. View at Google Scholar · View at Scopus
  31. G. Xu, D. A. Stoffers, J. F. Habener, and S. Bonner-Weir, “Exendin-4 stimulates both β-cell replication and neogenesis, resulting in increased β-cell mass and improved glucose tolerance in diabetic rats,” Diabetes, vol. 48, no. 12, pp. 2270–2276, 1999. View at Google Scholar · View at Scopus
  32. J. P. Gutzwiller, B. Göke, J. Drewe et al., “Glucagon-like peptide-1: A potent regulator of food intake in humans,” Gut, vol. 44, no. 1, pp. 81–86, 1999. View at Google Scholar · View at Scopus
  33. S. Delgado-Aros, D. Y. Kim, D. D. Burton et al., “Effect of GLP-1 on gastric volume, emptying, maximum volume ingested, and postprandial symptoms in humans,” American Journal of Physiology, vol. 282, no. 3, pp. G424–G431, 2002. View at Google Scholar · View at Scopus
  34. J. J. Meier, B. Gallwitz, W. E. Schmidt, and M. A. Nauck, “Glucagon-like peptide 1 as a regulator of food intake and body weight: Therapeutic perspectives,” European Journal of Pharmacology, vol. 440, no. 2-3, pp. 269–279, 2002. View at Publisher · View at Google Scholar · View at Scopus
  35. J. M. Egan, C. Montrose-Rafizadeh, Y. Wang, M. Bernier, and J. Roth, “Glucagon-like peptide-1 (7-36) amide (GLP-1) enhances insulin-stimulated glucose metabolism in 3T3-L1 adipocytes: One of several potential extrapancreatic sites of GLP-1 action,” Endocrinology, vol. 135, no. 5, pp. 2070–2075, 1994. View at Publisher · View at Google Scholar · View at Scopus
  36. M. A. Luque, N. González, L. Márquez et al., “Glucagon-like peptide-1 (GLP-1) and glucose metabolism in human myocytes,” Journal of Endocrinology, vol. 173, no. 3, pp. 465–473, 2002. View at Publisher · View at Google Scholar · View at Scopus
  37. A. Perea, C. Viñambres, F. Clemente, M. L. Villanueva-Peñacarrillo, and I. Valverde, “GLP-1 (7-36) amide: Effects on glucose transport and metabolism in rat adipose tissue,” Hormone and Metabolic Research, vol. 29, no. 9, pp. 417–421, 1997. View at Google Scholar · View at Scopus
  38. R. Abu-Hamdah, A. Rabiee, G. S. Meneilly, R. P. Shannon, D. K. Andersen, and D. Elahi, “The extrapancreatic effects of glucagon-like peptide-1 and related peptides,” Journal of Clinical Endocrinology and Metabolism, vol. 94, no. 6, pp. 1843–1852, 2009. View at Publisher · View at Google Scholar · View at Scopus
  39. C. Holscher, “Potential role of glucagon-like peptide-1 (GLP-1) in neuroprotection,” CNS Drugs, vol. 26, no. 10, pp. 871–882, 2012. View at Publisher · View at Google Scholar
  40. K. Vollmer, J. J. Hoist, B. Bailer et al., “Predictors of incretin concentrations in subjects with normal, impaired, and diabetic glucose tolerance,” Diabetes, vol. 57, no. 3, pp. 678–687, 2008. View at Publisher · View at Google Scholar · View at Scopus
  41. M. Nauck, F. Stockmann, R. Ebert, and W. Creutzfeldt, “Reduced incretin effect in Type 2 (non-insulin-dependent) diabetes,” Diabetologia, vol. 29, no. 1, pp. 46–52, 1986. View at Google Scholar · View at Scopus
  42. M. B. Toft-Nielsen, M. B. Damholt, S. Madsbad et al., “Determinants of the impaired secretion of glucagon-like peptide-1 in type 2 diabetic patients,” Journal of Clinical Endocrinology and Metabolism, vol. 86, no. 8, pp. 3717–3723, 2001. View at Publisher · View at Google Scholar · View at Scopus
  43. T. Vilsbøll, T. Krarup, C. F. Deacon, S. Madsbad, and J. J. Holst, “Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in type 2 diabetic patients,” Diabetes, vol. 50, no. 3, pp. 609–613, 2001. View at Google Scholar · View at Scopus
  44. M. A. Nauck, M. M. Heimesaat, C. Orskov, J. J. Holst, R. Ebert, and W. Creutzfeldt, “Preserved incretin activity of glucagon-like peptide 1 [7-36 amide] but not of synthetic human gastric inhibitory polypeptide in patients with type-2 diabetes mellitus,” Journal of Clinical Investigation, vol. 91, no. 1, pp. 301–307, 1993. View at Google Scholar · View at Scopus
  45. D. Elahi, M. McAloon-Dyke, N. K. Fukagawa et al., “The insulinotropic actions of glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (7-37) in normal and diabetic subjects,” Regulatory Peptides, vol. 51, no. 1, pp. 63–74, 1994. View at Publisher · View at Google Scholar · View at Scopus
  46. B. Willms, J. Werner, J. J. Holst, C. Ørskov, W. Creutzfeldt, and M. A. Nauck, “Gastric emptying, glucose responses, and insulin secretion after a liquid test meal: effects of exogenous glucagon-like peptide-1 (GLP-1)-(7-36) amide in type 2 (Noninsulin-Dependent) diabetic patients,” Journal of Clinical Endocrinology and Metabolism, vol. 81, no. 1, pp. 327–332, 1996. View at Google Scholar · View at Scopus
  47. L. K. Phillips and J. B. Prins, “Update on incretin hormones,” Annals of the New York Academy of Sciences, vol. 1243, pp. E55–E74, 2011. View at Publisher · View at Google Scholar
  48. F. K. Knop, T. Vilsbøll, and J. J. Holst, “Incretin-based therapy of type 2 diabetes mellitus,” Current Protein and Peptide Science, vol. 10, no. 1, pp. 46–55, 2009. View at Publisher · View at Google Scholar · View at Scopus
  49. T. Vilsbøll and F. K. Knop, “Long-acting GLP-1 analogs for the treatment of type 2 diabetes mellitus,” BioDrugs, vol. 22, no. 4, pp. 251–257, 2008. View at Publisher · View at Google Scholar · View at Scopus
  50. E. J. Verspohl, “Novel therapeutics for type 2 diabetes: Incretin hormone mimetics (glucagon-like peptide-1 receptor agonists) and dipeptidyl peptidase-4 inhibitors,” Pharmacology and Therapeutics, vol. 124, no. 1, pp. 113–138, 2009. View at Publisher · View at Google Scholar · View at Scopus
  51. B. Ahrén, M. Landin-Olsson, P. A. Jansson, M. Svensson, D. Holmes, and A. Schweizer, “Inhibition of Dipeptidyl Peptidase-4 Reduces Glycemia, Sustains Insulin Levels, and Reduces Glucagon Levels in Type 2 Diabetes,” Journal of Clinical Endocrinology and Metabolism, vol. 89, no. 5, pp. 2078–2084, 2004. View at Publisher · View at Google Scholar · View at Scopus
  52. H. C. Fehmann, J. Jiang, J. Schweinfurth, M. B. Wheeler, A. E. Boyd, and B. Goke, “Stable expression of the rat GLP-I receptor in CHO cells: activation and binding characteristics utilizing GLP-I(7-36)-amide, oxyntomodulin, exendin-4, and exendin(9-39),” Peptides, vol. 15, no. 3, pp. 453–456, 1994. View at Publisher · View at Google Scholar · View at Scopus
  53. G. A. Herman, C. Stevens, K. Van Dyck et al., “Pharmacokinetics and pharmacodynamics of sitagliptin, an inhibitor of dipeptidyl peptidase IV, in healthy subjects: Results from two randomized, double-blind, placebo-controlled studies with single oral doses,” Clinical Pharmacology and Therapeutics, vol. 78, no. 6, pp. 675–688, 2005. View at Publisher · View at Google Scholar · View at Scopus
  54. R. Goke, H. C. Fehmann, T. Linn et al., “Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting β-cells,” Journal of Biological Chemistry, vol. 268, no. 26, pp. 19650–19655, 1993. View at Google Scholar · View at Scopus
  55. L. B. Knudsen, P. F. Nielsen, P. O. Huusfeldt et al., “Potent derivatives of glucagon-like peptide-1 with pharmacokinetic properties suitable for once daily administration,” Journal of Medicinal Chemistry, vol. 43, no. 9, pp. 1664–1669, 2000. View at Publisher · View at Google Scholar · View at Scopus
  56. A. Mari, W. M. Sallas, Y. L. He et al., “Vildagliptin, a dipeptidyl peptidase-IV inhibitor, improves model-assessed β-cell function in patients with type 2 diabetes,” Journal of Clinical Endocrinology and Metabolism, vol. 90, no. 8, pp. 4888–4894, 2005. View at Publisher · View at Google Scholar · View at Scopus
  57. F. J. Tessier, “The Maillard reaction in the human body. The main discoveries and factors that affect glycation,” Pathologie Biologie, vol. 58, no. 3, pp. 214–219, 2010. View at Publisher · View at Google Scholar · View at Scopus
  58. V. M. Monnier, “Nonenzymatic glycosylation, the Maillard reaction and the aging process,” Journals of Gerontology, vol. 45, no. 4, pp. B105–B111, 1990. View at Google Scholar · View at Scopus
  59. D. G. Dyer, J. A. Blackledge, B. M. Katz et al., “The Maillard reaction in vivo,” Zeitschrift fur Ernahrungswissenschaft, vol. 30, no. 1, pp. 29–45, 1991. View at Google Scholar · View at Scopus
  60. C. Cerami, H. Founds, I. Nicholl et al., “Tobacco smoke is a source of toxic reactive glycation products,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 25, pp. 13915–13920, 1997. View at Publisher · View at Google Scholar · View at Scopus
  61. H. Vlassara, W. Cai, J. Crandall et al., “Inflammatory mediators are induced by dietary glycotoxins, a major risk factor for diabetic angiopathy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 24, pp. 15596–15601, 2002. View at Publisher · View at Google Scholar · View at Scopus
  62. J. Uribarri, W. Cai, O. Sandu, M. Peppa, T. Goldberg, and H. Vlassara, “Diet-derived advanced glycation end products are major contributors to the body's AGE pool and induce inflammation in healthy subjects,” Annals of the New York Academy of Sciences, vol. 1043, pp. 461–466, 2005. View at Publisher · View at Google Scholar · View at Scopus
  63. M. Brownlee, “Biochemistry and molecular cell biology of diabetic complications,” Nature, vol. 414, no. 6865, pp. 813–820, 2001. View at Publisher · View at Google Scholar · View at Scopus
  64. A. M. Schmidt, S. D. Yan, S. F. Yan, and D. M. Stern, “The biology of the receptor for advanced glycation end products and its ligands,” Biochimica et Biophysica Acta, vol. 1498, no. 2-3, pp. 99–111, 2000. View at Publisher · View at Google Scholar · View at Scopus
  65. H. Vlassara, “The AGE-receptor in the pathogenesis of diabetic complications,” Diabetes/Metabolism Research and Reviews, vol. 17, no. 6, pp. 436–443, 2001. View at Publisher · View at Google Scholar · View at Scopus
  66. A. Ceriello, “The emerging challenge in diabetes: the ‘metabolic memory’,” Vascular Pharmacology, vol. 57, no. 5-6, pp. 133–138, 2012. View at Publisher · View at Google Scholar
  67. N. Ahmed and P. J. Thornalley, “Advanced glycation endproducts: What is their relevance to diabetic complications?” Diabetes, Obesity and Metabolism, vol. 9, no. 3, pp. 233–245, 2007. View at Publisher · View at Google Scholar · View at Scopus
  68. M. Brownlee, “The pathobiology of diabetic complications: A unifying mechanism,” Diabetes, vol. 54, no. 6, pp. 1615–1625, 2005. View at Publisher · View at Google Scholar · View at Scopus
  69. A. Prasad, P. Bekker, and S. Tsimikas, “Advanced glycation end products and diabetic cardiovascular disease,” Cardiology in Review, vol. 20, no. 4, pp. 177–183, 2012. View at Publisher · View at Google Scholar
  70. R. Ramasamy, S. F. Yan, and A. M. Schmidt, “Receptor for AGE (RAGE): signaling mechanisms in the pathogenesis of diabetes and its complications,” Annals of the New York Academy of Sciences, vol. 1243, pp. 88–102, 2011. View at Publisher · View at Google Scholar
  71. H. Zong, M. Ward, and A. W. Stitt, “AGEs, RAGE, and diabetic retinopathy,” Current Diabetes Reports, vol. 11, no. 4, pp. 244–252, 2011. View at Publisher · View at Google Scholar
  72. A. Puddu, D. Storace, P. Odetti, and G. L. Viviani, “Advanced glycation end-products affect transcription factors regulating insulin gene expression,” Biochemical and biophysical research communications, vol. 395, no. 1, pp. 122–125, 2010. View at Publisher · View at Google Scholar · View at Scopus
  73. G. Luciano Viviani, A. Puddu, G. Sacchi et al., “Glycated fetal calf serum affects the viability of an insulin-secreting cell line in vitro,” Metabolism: Clinical and Experimental, vol. 57, no. 2, pp. 163–169, 2008. View at Publisher · View at Google Scholar · View at Scopus
  74. M. Lim, L. Park, G. Shin, H. Hong, I. Kang, and Y. Park, “Induction of apoptosis of β cells of the pancreas by advanced glycation end-products, important mediators of chronic complications of diabetes mellitus,” Annals of the New York Academy of Sciences, vol. 1150, pp. 311–315, 2008. View at Publisher · View at Google Scholar · View at Scopus
  75. Q. M. Ge, Y. Dong, and Q. Su, “Effects of glucose and advanced glycation end products on oxidative stress in MIN6 cells,” Cellular and Molecular Biology, vol. 56, supplement 1, pp. OL1231–OL1238, 2010. View at Publisher · View at Google Scholar · View at Scopus
  76. Z. Zhao, C. Zhao, H. Z. Xu et al., “Advanced glycation end products inhibit glucose-stimulated insulin secretion through nitric oxide-dependent inhibition of cytochrome c oxidase and adenosine triphosphate synthesis,” Endocrinology, vol. 150, no. 6, pp. 2569–2576, 2009. View at Publisher · View at Google Scholar · View at Scopus
  77. A. Puddu, D. Storace, A. Durante, P. Odetti, and G. L. Viviani, “Glucagon-like peptide-1 counteracts the detrimental effects of Advanced Glycation End-Products in the pancreatic beta cell line HIT-T 15,” Biochemical and Biophysical Research Communications, vol. 398, no. 3, pp. 462–466, 2010. View at Publisher · View at Google Scholar · View at Scopus
  78. M. Minakawa, A. Kawano, Y. Miura, and K. Yagasaki, “Hypoglycemic effect of resveratrol in type 2 diabetic model db/db mice and its actions in cultured L6 myotubes and RIN-5F pancreatic β-cells,” Journal of Clinical Biochemistry and Nutrition, vol. 48, no. 3, pp. 237–244, 2011. View at Publisher · View at Google Scholar · View at Scopus
  79. A. Dhar, I. Dhar, B. Jiang, K. M. Desai, and L. Wu, “Chronic methylglyoxal infusion by minipump causes pancreatic β-cell dysfunction and induces type 2 diabetes in Sprague-Dawley rats,” Diabetes, vol. 60, no. 3, pp. 899–908, 2011. View at Publisher · View at Google Scholar · View at Scopus
  80. Y. Zhu, T. Shu, Y. Lin et al., “Inhibition of the receptor for advanced glycation endproducts (RAGE) protects pancreatic β-cells,” Biochemical and Biophysical Research Communications, vol. 404, no. 1, pp. 159–165, 2011. View at Publisher · View at Google Scholar · View at Scopus
  81. T. Shu, Y. Zhu, H. Wang, Y. Lin, Z. Ma, and X. Han, “Ages decrease insulin synthesis in pancreatic β-cell by repressing pdx-1 protein expression at the post-translational level,” PLoS ONE, vol. 6, no. 4, Article ID e18782, 2011. View at Publisher · View at Google Scholar · View at Scopus
  82. A. M. McKillop, Y. H. A. Abdel-Wahab, M. H. Mooney, F. P. M. O'Harte, and P. R. Flatt, “Secretion of glycated insulin from pancreatic β-cells in diabetes represents a novel aspect of β-cell dysfunction and glucose toxicity,” Diabetes and Metabolism, vol. 28, no. 6, pp. 3–S61, 2002. View at Google Scholar · View at Scopus
  83. A. M. McKillop, J. R. Lindsay, S. Au et al., “Meal-dependent regulation of circulating glycated insulin in type 2 diabetic subjects,” Hormone and Metabolic Research, vol. 38, no. 2, pp. 94–97, 2006. View at Publisher · View at Google Scholar · View at Scopus
  84. Y. H. A. Abdel-Wahab, F. P. M. O'Harte, A. C. Boyd, C. R. Barnett, and P. R. Flatt, “Glycation of insulin results in reduced biological activity in mice,” Acta Diabetologica, vol. 34, no. 4, pp. 265–270, 1997. View at Publisher · View at Google Scholar · View at Scopus
  85. A. C. Boyd, Y. H. A. Abdel-Wahab, A. M. McKillop et al., “Impaired ability of glycated insulin to regulate plasma glucose and stimulate glucose transport and metabolism in mouse abdominal muscle,” Biochimica et Biophysica Acta, vol. 1523, no. 1, pp. 128–134, 2000. View at Publisher · View at Google Scholar · View at Scopus
  86. I. M. Bonapace, R. Addeo, L. Altucci et al., “17β-Estradiol overcomes a G1 block induced by HMG-CoA reductase inhibitors and fosters cell cycle progression without inducing ERK-1 and -2 MAP kinases activation,” Oncogene, vol. 12, no. 4, pp. 753–763, 1996. View at Google Scholar · View at Scopus
  87. B. Corman, M. Duriez, P. Poitevin et al., “Aminoguanidine prevents age-related arterial stiffening and cardiac hypertrophy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 3, pp. 1301–1306, 1998. View at Publisher · View at Google Scholar · View at Scopus
  88. T. S. Kern and R. L. Engerman, “Pharmacological inhibition of diabetic retinopathy: aminoguanidine and aspirin,” Diabetes, vol. 50, no. 7, pp. 1636–1642, 2001. View at Google Scholar · View at Scopus
  89. F. Monacelli, A. Poggi, D. Storace et al., “Effects of valsartan therapy on protein glycoxidation,” Metabolism: Clinical and Experimental, vol. 55, no. 12, pp. 1619–1624, 2006. View at Publisher · View at Google Scholar · View at Scopus
  90. P. Odetti, C. Pesce, N. Traverso et al., “Comparative trial of N-acetyl-cysteine, taurine, and oxerutin on skin and kidney damage in long-term experimental diabetes,” Diabetes, vol. 52, no. 2, pp. 499–505, 2003. View at Publisher · View at Google Scholar · View at Scopus
  91. Y. Ishibashi, T. Matsui, M. Takeuchi, and S. I. Yamagishi, “Glucagon-like peptide-1 (GLP-1) inhibits advanced glycation end product (AGE)-induced up-regulation of VCAM-1 mRNA levels in endothelial cells by suppressing AGE receptor (RAGE) expression,” Biochemical and Biophysical Research Communications, vol. 391, no. 3, pp. 1405–1408, 2010. View at Publisher · View at Google Scholar · View at Scopus
  92. Y. Ishibashi, T. Matsui, M. Takeuchi, and S. Yamagishi, “Sitagliptin augments protective effects of GLP-1 against advanced glycation end product receptor axis in endothelial cells,” Hormone and Metabolic Research, vol. 43, no. 10, pp. 731–734, 2011. View at Publisher · View at Google Scholar
  93. T. Matsui, Y. Nishino, M. Takeuchi, and S. I. Yamagishi, “Vildagliptin blocks vascular injury in thoracic aorta of diabetic rats by suppressing advanced glycation end product-receptor axis,” Pharmacological Research, vol. 63, no. 5, pp. 383–388, 2011. View at Publisher · View at Google Scholar · View at Scopus
  94. Y. Zhan, H. L. Sun, H. Chen et al., “Glucagon-like peptide-1 (GLP-1) protects vascular endothelial cells against advanced glycation end products (AGEs)-induced apoptosis,” Medical Science Monitor, vol. 18, no. 7, pp. BR286–BR291, 2012. View at Google Scholar
  95. R. Kimura, M. Okouchi, H. Fujioka et al., “Glucagon-like peptide-1 (GLP-1) protects against methylglyoxal-induced PC12 cell apoptosis through the PI3K/Akt/mTOR/GCLc/redox signaling pathway,” Neuroscience, vol. 162, no. 4, pp. 1212–1219, 2009. View at Publisher · View at Google Scholar · View at Scopus
  96. Y. Ishibashi, Y. Nishino, T. Matsui, M. Takeuchi, and S. Yamagishi, “Glucagon-like peptide-1 suppresses advanced glycation end product-induced monocyte chemoattractant protein-1 expression in mesangial cells by reducing advanced glycation end product receptor level,” Metabolism, vol. 60, no. 9, pp. 1271–1277, 2011. View at Publisher · View at Google Scholar