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Journal of Ophthalmology
Volume 2010 (2010), Article ID 170393, 12 pages
http://dx.doi.org/10.1155/2010/170393
Review Article

Involvement of TAGE-RAGE System in the Pathogenesis of Diabetic Retinopathy

1Department of Pathophysiological Science, Faculty of Pharmaceutical Sciences, Hokuriku University, Ho-3 Kanagawa-machi, Kanazawa 920-1181, Japan
2Department of Pathophysiology and Therapeutics of Diabetic Vascular Complications, Kurume University School of Medicine, 67 Asahimachi, Kurume 830-0011, Japan

Received 25 November 2009; Accepted 29 March 2010

Academic Editor: Susanne Mohr

Copyright © 2010 Masayoshi Takeuchi 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. M. Laakso, “Hyperglycemia and cardiovascular disease in type 2 diabetes,” Diabetes, vol. 48, no. 5, pp. 937–942, 1999. View at Publisher · View at Google Scholar · View at Scopus
  2. T. Nishikawa, D. Edelstein, X. L. Du, et al., “Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage,” Nature, vol. 404, no. 6779, pp. 787–790, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  3. 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 PubMed · View at Scopus
  4. J. M. Lachin, S. Genuth, P. Cleary, M. D. Davis, and D. M. Nathan, “Retinopathy and nephropathy in patients with type I diabetes four years after a trial of intensive therapy,” The New England Journal of Medicine, vol. 342, no. 6, pp. 381–389, 2000. View at Publisher · View at Google Scholar · View at Scopus
  5. D. M. Nathan, “Sustained effect of intensive treatment of type 1 diabetes mellitus on development and progression of diabetic nephropathy: the Epidemiology of Diabetes Interventions and Complications (EDIC) Study,” Journal of the American Medical Association, vol. 290, no. 16, pp. 2159–2167, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  6. D. M. Nathan, P. A. Cleary, J.-Y. C. Backlund, et al., “Intensive diabetes treatment and cardiovascular disease in patients with type 1 diabetes,” The New England Journal of Medicine, vol. 353, no. 25, pp. 2643–2653, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. R. R. Holman, S. K. Paul, M. A. Bethel, D. R. Matthews, and H. A. W. Neil, “10-year follow-up of intensive glucose control in type 2 diabetes,” The New England Journal of Medicine, vol. 359, no. 15, pp. 1577–1589, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. M. Brownlee, A. Cerami, and H. Vlassara, “Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications,” The New England Journal of Medicine, vol. 318, no. 20, pp. 1315–1321, 1988. View at Scopus
  9. D. G. Dyer, J. A. Blackledge, S. R. Thorpe, and J. W. Baynes, “Formation of pentosidine during nonenzymatic browning of proteins by glucose: identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo,” Journal of Biological Chemistry, vol. 266, no. 18, pp. 11654–11660, 1991. View at Scopus
  10. S.-I. Yamagishi and T. Imaizumi, “Diabetic vascular complications: pathophysiology, biochemical basis and potential therapeutic strategy,” Current Pharmaceutical Design, vol. 11, no. 18, pp. 2279–2299, 2005. View at Publisher · View at Google Scholar · View at Scopus
  11. S. Rahbar and J. L. Figarola, “Novel inhibitors of advanced glycation endproducts,” Archives of Biochemistry and Biophysics, vol. 419, no. 1, pp. 63–79, 2003. View at Publisher · View at Google Scholar · View at Scopus
  12. S.-I. Yamagishi, M. Takeuchi, Y. Inagaki, K. Nakamura, and T. Imaizumi, “Role of advanced glycation end products (AGEs) and their receptor (RAGE) in the pathogenesis of diabetic microangiopathy,” International Journal of Clinical Pharmacology Research, vol. 23, no. 4, pp. 129–134, 2003. View at Scopus
  13. H. Vlassara and M. R. Palace, “Diabetes and advanced glycation endproducts,” Journal of Internal Medicine, vol. 251, no. 2, pp. 87–101, 2002. View at Publisher · View at Google Scholar · View at Scopus
  14. A. Bierhaus, M. A. Hofmann, R. Ziegler, and P. P. Nawroth, “AGEs and their interaction with AGE-receptors in vascular disease and diabetes mellitus. I. The AGE concept,” Cardiovascular Research, vol. 37, no. 3, pp. 586–600, 1998. View at Publisher · View at Google Scholar · View at Scopus
  15. T. Wendt, L. Bucciarelli, W. Qu, et al., “Receptor for advanced glycation endproducts (RAGE) and vascular inflammation: insights into the pathogenesis of macrovascular complications in diabetes,” Current Atherosclerosis Reports, vol. 4, no. 3, pp. 228–237, 2002. View at Scopus
  16. A. M. Schmidt and D. Stern, “Atherosclerosis and diabetes: the RAGE connection,” Current Atherosclerosis Reports, vol. 2, no. 5, pp. 430–436, 2000. View at Scopus
  17. A. W. Stitt, R. Bucala, and H. Vlassara, “Atherogenesis and advanced glycation: promotion, progression, and prevention,” Annals of the New York Academy of Sciences, vol. 811, pp. 115–129, 1997. View at Publisher · View at Google Scholar · View at Scopus
  18. K. Takenaka, S.-I. Yamagishi, T. Matsui, K. Nakamura, and T. Imaizumi, “Role of advanced glycation end products (AGEs) in thrombogenic abnormalities in diabetes,” Current Neurovascular Research, vol. 3, no. 1, pp. 73–77, 2006. View at Publisher · View at Google Scholar · View at Scopus
  19. T. Sato, M. Iwaki, N. Shimogaito, X. Wu, S.-I. Yamagishi, and M. Takeuchi, “TAGE (Toxic AGEs) theory in diabetic complications,” Current Molecular Medicine, vol. 6, no. 3, pp. 351–358, 2006. View at Publisher · View at Google Scholar · View at Scopus
  20. M. Takeuchi and S.-I. Yamagishi, “Involvement of toxic AGEs (TAGE) in the pathogenesis of diabetic vascular complications and Alzheimer's disease,” Journal of Alzheimer's Disease, vol. 16, no. 4, pp. 845–858, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  21. M. Takeuchi and Z. Makita, “Alternative routes for the formation of immunochemically distinct advanced glycation end-products in vivo,” Current Molecular Medicine, vol. 1, no. 3, pp. 305–315, 2001. View at Scopus
  22. R. Bucala and A. Cerami, “Advanced glycosylation: chemistry, biology, and implications for diabetes and aging,” Advances in Pharmacology, vol. 23, pp. 1–34, 1992. View at Scopus
  23. H. Vlassara, R. Bucala, and L. Striker, “Pathogenic effects of advanced glycosylation: biochemical, biologic, and clinical implications for diabetes and aging,” Laboratory Investigation, vol. 70, no. 2, pp. 138–151, 1994. View at Scopus
  24. M. Brownlee, “Advanced protein glycosylation in diabetes and aging,” Annual Review of Medicine, vol. 46, pp. 223–234, 1995. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  25. V. M. Monnier and A. Cerami, “Nonenzymatic browning in vivo: possible process for aging of long-lived proteins,” Science, vol. 211, no. 4481, pp. 491–493, 1981. View at Scopus
  26. K. J. Wells-Knecht, D. V. Zyzak, J. E. Litchfield, S. R. Thorpe, and J. W. Baynes, “Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose,” Biochemistry, vol. 34, no. 11, pp. 3702–3709, 1995. View at Scopus
  27. P. J. Thornalley, “Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification—a role in pathogenesis and antiproliferative chemotherapy,” General Pharmacology, vol. 27, no. 4, pp. 565–573, 1996. View at Publisher · View at Google Scholar · View at Scopus
  28. P. J. Thornalley, A. Langborg, and H. S. Minhas, “Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose,” Biochemical Journal, vol. 344, no. 1, pp. 109–116, 1999. View at Publisher · View at Google Scholar · View at Scopus
  29. M. Takeuchi, Z. Makita, K. Yanagisawa, Y. Kameda, and T. Koike, “Detection of noncarboxymethyllysine and carboxymethyllysine advanced glycation end products (AGE) in serum of diabetic patients,” Molecular Medicine, vol. 5, no. 6, pp. 393–405, 1999. View at Scopus
  30. M. Takeuchi, Z. Makita, R. Bucala, T. Suzuki, T. Koike, and Y. Kameda, “Immunological evidence that non-carboxymethyllysine advanced glycation end-products are produced from short chain sugars and dicarbonyl compounds in vivo,” Molecular Medicine, vol. 6, no. 2, pp. 114–125, 2000. View at Scopus
  31. M. Takeuchi, Y. Yanase, N. Matsuura, et al., “Immunological detection of a novel advanced glycation end-product,” Molecular Medicine, vol. 7, no. 11, pp. 783–791, 2001. View at Scopus
  32. S. D. Yan, X. Chen, J. Fu, et al., “RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease,” Nature, vol. 382, no. 6593, pp. 685–691, 1996. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  33. 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
  34. L. G. Bucciarelli, T. Wendt, L. Rong, et al., “RAGE is a multiligand receptor of the immunoglobulin superfamily: implications for homeostasis and chronic disease,” Cellular and Molecular Life Sciences, vol. 59, no. 7, pp. 1117–1128, 2002. View at Publisher · View at Google Scholar · View at Scopus
  35. B. I. Hudson, L. G. Bucciarelli, T. Wendt, et al., “Blockade of receptor for advanced glycation endproducts: a new target for therapeutic intervention in diabetic complications and inflammatory disorders,” Archives of Biochemistry and Biophysics, vol. 419, no. 1, pp. 80–88, 2003. View at Publisher · View at Google Scholar · View at Scopus
  36. R. Ramasamy, S. J. Vannucci, S. S. D. Yan, K. Herold, S. F. Yan, and A. M. Schmidt, “Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation,” Glycobiology, vol. 15, no. 7, pp. 16R–28R, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  37. Y. M. Li, T. Mitsuhashi, D. Wojciechowicz, et al., “Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80K-H membrane proteins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 20, pp. 11047–11052, 1996. View at Publisher · View at Google Scholar · View at Scopus
  38. H. Vlassara, Y. M. Li, F. Imani, et al., “Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex,” Molecular Medicine, vol. 1, no. 6, pp. 634–646, 1995. View at Scopus
  39. N. Ohgami, R. Nagai, M. Ikemoto, et al., “CD36, serves as a receptor for advanced glycation endproducts (AGE),” Journal of Diabetes and Its Complications, vol. 16, no. 1, pp. 56–59, 2002. View at Publisher · View at Google Scholar · View at Scopus
  40. J. El Khoury, C. A. Thomas, J. D. Loike, S. E. Hickman, L. Cao, and S. C. Silverstein, “Macrophages adhere to glucose-modified basement membrane collagen IV via their scavenger receptors,” Journal of Biological Chemistry, vol. 269, no. 14, pp. 10197–10200, 1994. View at Scopus
  41. Y. Tamura, H. Adachi, J. I. Osuga, et al., “FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end products,” Journal of Biological Chemistry, vol. 278, no. 15, pp. 12613–12617, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  42. B. I. Hudson, E. Harja, B. Moser, and A. M. Schmidt, “Soluble levels of receptor for advanced glycation endproducts (sRAGE) and coronary artery disease: the next C-reactive protein?” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 25, no. 5, pp. 879–882, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  43. H. Yonekura, Y. Yamamoto, S. Sakurai, et al., “Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury,” Biochemical Journal, vol. 370, no. 3, pp. 1097–1109, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  44. Y. Yamamoto, H. Yonekura, T. Watanabe, et al., “Short-chain aldehyde-derived ligands for RAGE and their actions on endothelial cells,” Diabetes Research and Clinical Practice, vol. 77, no. 3, pp. S30–S40, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  45. M. Takeuchi and S.-I. Yamagishi, “Alternative routes for the formation of glyceraldehyde-derived AGEs (TAGE) in vivo,” Medical Hypotheses, vol. 63, no. 3, pp. 453–455, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  46. P. J. Oates, “Polyol pathway and diabetic peripheral neuropathy,” International Review of Neurobiology, vol. 50, pp. 325–392, 2002. View at Scopus
  47. K. Maekawa, T. Tanimoto, and S. Okada, “Gene expression of enzymes comprising the polyol pathway in various rat tissues determined by the competitive RT-PCR method,” Japanese Journal of Pharmacology, vol. 88, no. 1, pp. 123–126, 2002. View at Publisher · View at Google Scholar · View at Scopus
  48. C. G. Schalkwijk, C. D. A. Stehouwer, and V. W. M. van Hinsbergh, “Fructose-mediated non-enzymatic glycation: sweet coupling or bad modification,” Diabetes/Metabolism Research and Reviews, vol. 20, no. 5, pp. 369–382, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  49. A. R. Gaby, “Adverse effects of dietary fructose,” Alternative Medicine Review, vol. 10, no. 4, pp. 294–306, 2005. View at Scopus
  50. J. Hallfrisch, “Metabolic effects of dietary fructose,” The FASEB Journal, vol. 4, no. 9, pp. 2652–2660, 1990. View at Scopus
  51. P. A. Mayes, “Intermediary metabolism of fructose,” American Journal of Clinical Nutrition, vol. 58, no. 5, pp. S754–S765, 1993. View at Scopus
  52. F. A. L'Esperance, W. A. James, and P. H. Judson, Ellenberg and Rifkin's Diabetes Mellitus, Theory and Practice, Elsevier, New York, NY, USA, 1990.
  53. L. J. Mandarino, “Current hypotheses for the biochemical basis of diabetic retinopathy,” Diabetes Care, vol. 15, no. 12, pp. 1892–1901, 1992. View at Scopus
  54. R. N. Frank, “On the pathogenesis of diabetic retinopathy: a 1990 update,” Ophthalmology, vol. 98, no. 5, pp. 586–593, 1991. View at Scopus
  55. D. E. Sims, “Recent advances in pericyte biology—implications for health and disease,” Canadian Journal of Cardiology, vol. 7, no. 10, pp. 431–443, 1991. View at Scopus
  56. I. M. Herman and P. A. D'Amore, “Microvascular pericytes contain muscle and nonmuscle actins,” Journal of Cell Biology, vol. 101, no. 1, pp. 43–52, 1985. View at Scopus
  57. N. C. Joyce, M. F. Haire, and G. E. Palade, “Contractile proteins in pericytes. II. Immunocytochemical evidence for the presence of two isomyosins in graded concentrations,” Journal of Cell Biology, vol. 100, no. 5, pp. 1387–1395, 1985. View at Scopus
  58. A. P. Adamis, J. W. Miller, M. T. Bernal, et al., “Increased vascular endothelial growth factor levels in the vitreous of eyes with proliferative diabetic retinopathy,” American Journal of Ophthalmology, vol. 118, no. 4, pp. 445–450, 1994. View at Scopus
  59. L. P. Aiello, R. L. Avery, P. G. Arrigg, et al., “Vascular endothelial growth factor in ocular fluid of patients with diabetic retinopathy and other retinal disorders,” The New England Journal of Medicine, vol. 331, no. 22, pp. 1480–1487, 1994. View at Publisher · View at Google Scholar · View at Scopus
  60. A. W. Stitt, Y. M. Li, T. A. Gardiner, R. Bucala, D. B. Archer, and H. Vlassara, “Advanced glycation end products (AGEs) co-localize with AGE receptors in the retinal vasculature of diabetic and of AGE-infused rats,” American Journal of Pathology, vol. 150, no. 2, pp. 523–531, 1997. View at Scopus
  61. N. K. Sharma, T. A. Gardiner, and D. B. Archer, “A morphologic and autoradiographic study of cell death and regeneration in the retinal microvasculature of normal and diabetic rats,” American Journal of Ophthalmology, vol. 100, no. 1, pp. 51–60, 1985. View at Scopus
  62. S.-I. Yamagishi, S. Amano, Y. Inagaki, et al., “Advanced glycation end products-induced apoptosis and overexpression of vascular endothelial growth factor in bovine retinal pericytes,” Biochemical and Biophysical Research Communications, vol. 290, no. 3, pp. 973–978, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  63. S.-I. Yamagishi, S. Amano, Y. Inagaki, T. Okamoto, M. Takeuchi, and Z. Makita, “Beraprost sodium, a prostaglandin I2 analogue, protects against advanced glycation end products-induced injury in cultured retinal pericytes,” Molecular Medicine, vol. 8, no. 9, pp. 546–550, 2002. View at Scopus
  64. S.-I. Yamagishi, M. Takeuchi, T. Matsui, K. Nakamura, T. Imaizumi, and H. Inoue, “Angiotensin II augments advanced glycation end product-induced pericyte apoptosis through RAGE overexpression,” FEBS Letters, vol. 579, no. 20, pp. 4265–4270, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  65. T. Okamoto, S.-I. Yamagishi, Y. Inagaki, et al., “Incadronate disodium inhibits advanced glycation end products-induced angiogenesis in vitro,” Biochemical and Biophysical Research Communications, vol. 297, no. 2, pp. 419–424, 2002. View at Publisher · View at Google Scholar · View at Scopus
  66. T. Okamoto, S.-I. Yamagishi, Y. Inagaki, et al., “Angiogenesis induced by advanced glycation end products and its prevention by cerivastatin,” The FASEB Journal, vol. 16, no. 14, pp. 1928–1930, 2002. View at Scopus
  67. S. Schroder, W. Palinski, and G. W. Schmid-Schonbein, “Activated monocytes and granulocytes, capillary nonperfusion, and neovascularization in diabetic retinopathy,” American Journal of Pathology, vol. 139, no. 1, pp. 81–100, 1991. View at Scopus
  68. T. C. B. Moore, J. E. Moore, Y. Kaji, et al., “The role of advanced glycation end products in retinal microvascular leukostasis,” Investigative Ophthalmology and Visual Science, vol. 44, no. 10, pp. 4457–4464, 2003. View at Publisher · View at Google Scholar · View at Scopus
  69. Y. Inagaki, S.-I. Yamagishi, T. Okamoto, M. Takeuchi, and S. Amano, “Pigment epithelium-derived factor prevents advanced glycation end products-induced monocyte chemoattractant protein-1 production in microvascular endothelial cells by suppressing intracellular reactive oxygen species generation,” Diabetologia, vol. 46, no. 2, pp. 284–287, 2003. View at Scopus
  70. Q. Qiao, S. Larsen, K. Borch-Johnsen, et al., “Glucose tolerance and cardiovascular mortality: comparison of fasting and 2-hour diagnostic criteria,” Archives of Internal Medicine, vol. 161, no. 3, pp. 397–405, 2001. View at Scopus
  71. E. B. Levitan, Y. Song, E. S. Ford, and S. Liu, “Is nondiabetic hyperglycemia a risk factor for cardiovascular disease? A meta-analysis of prospective studies,” Archives of Internal Medicine, vol. 164, no. 19, pp. 2147–2155, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  72. T. Shiraiwa, H. Kaneto, T. Miyatsuka, et al., “Post-prandial hyperglycemia is an important predictor of the incidence of diabetic microangiopathy in Japanese type 2 diabetic patients,” Biochemical and Biophysical Research Communications, vol. 336, no. 1, pp. 339–345, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  73. Y. Kitahara, M. Takeuchi, K. Miura, T. Mine, T. Matsui, and S.-I. Yamagishi, “Glyceraldehyde-derived advanced glycation end products (AGEs). A novel biomarker of postprandial hyperglycaemia in diabetic rats,” Clinical and Experimental Medicine, vol. 8, no. 3, pp. 175–177, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  74. X. Du, T. Matsumura, D. Edelstein, et al., “Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells,” Journal of Clinical Investigation, vol. 112, no. 7, pp. 1049–1057, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  75. L. Monnier, H. Lapinski, and C. Colette, “Contributions of fasting and postprandial plasma glucose increments to the overall diurnal hyperglycemia of type 2 diabetic patients: variations with increasing levels of HbA,” Diabetes Care, vol. 26, no. 3, pp. 881–885, 2003. View at Publisher · View at Google Scholar · View at Scopus
  76. K. Koga, S.-I. Yamagishi, T. Okamoto, et al., “Serum levels of glucose-derived advanced glycation end products are associated with the severity of diabetic retinopathy in type 2 diabetic patients without renal dysfunction,” International Journal of Clinical Pharmacology Research, vol. 22, no. 1, pp. 13–17, 2002. View at Scopus
  77. J. Miura, S.-I. Yamagishi, Y. Uchigata, et al., “Serum levels of non-carboxymethyllysine advanced glycation endproducts are correlated to severity of microvascular complications in patients with type 1 diabetes,” Journal of Diabetes and Its Complications, vol. 17, no. 1, pp. 16–21, 2003. View at Publisher · View at Google Scholar · View at Scopus
  78. J. Miura, Y. Uchigata, Y. Yamamoto, et al., “AGE down-regulation of monocyte RAGE expression and its association with diabetic complications in type 1 diabetes,” Journal of Diabetes and Its Complications, vol. 18, no. 1, pp. 53–59, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  79. Y. Jinnouchi, S.-I. Yamagishi, M. Takeuchi, et al., “Atorvastatin decreases serum levels of advanced glycation end products (AGEs) in patients with type 2 diabetes,” Clinical and Experimental Medicine, vol. 6, no. 4, pp. 191–193, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  80. M. Yokoi, S.-I. Yamagishi, M. Takeuchi, et al., “Elevations of AGE and vascular endothelial growth factor with decreased total antioxidant status in the vitreous fluid of diabetic patients with retinopathy,” British Journal of Ophthalmology, vol. 89, no. 6, pp. 673–675, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  81. M. Yokoi, S.-I. Yamagishi, M. Takeuchi, et al., “Positive correlation between vitreous levels of advanced glycation end products and vascular endothelial growth factor in patients with diabetic retinopathy sufficiently treated with photocoagulation,” British Journal of Ophthalmology, vol. 91, no. 3, pp. 397–398, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  82. M. Enomoto, H. Adachi, S.-I. Yamagishi, et al., “Positive association of serum levels of advanced glycation end products with thrombogenic markers in humans,” Metabolism, vol. 55, no. 7, pp. 912–917, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  83. S. Sugiyama, T. Miyata, Y. Ueda, et al., “Plasma levels of pentosidine in diabetic patients: an advanced glycation end product,” Journal of the American Society of Nephrology, vol. 9, no. 9, pp. 1681–1688, 1998. View at Scopus
  84. M. Yamaguchi, N. Nakamura, K. Nakano, et al., “Immunochemical quantification of crossline as a fluorescent advanced glycation endproduct in erythrocyte membrane proteins from diabetic patients with or without retinopathy,” Diabetic Medicine, vol. 15, no. 6, pp. 458–462, 1998. View at Publisher · View at Google Scholar · View at Scopus
  85. Z. Wagner, I. Wittmann, I. Mazak, et al., “Nε-(carboxymethyl)lysine levels in patients with type 2 diabetes: role of renal function,” American Journal of Kidney Diseases, vol. 38, no. 4, pp. 785–791, 2001. View at Scopus
  86. L. Park, K. G. Raman, K. J. Lee, et al., “Suppression of accelerated diabetic atherosclerosis by the soluble receptor for advanced glycation endproducts,” Nature Medicine, vol. 4, no. 9, pp. 1025–1031, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  87. L. G. Bucciarelli, T. Wendt, W. Qu, et al., “RAGE blockade stabilizes established atherosclerosis in diabetic apolipoprotein E-null mice,” Circulation, vol. 106, no. 22, pp. 2827–2835, 2002. View at Publisher · View at Google Scholar · View at Scopus
  88. G. R. Barile, S.-I. Pachydaki, S. R. Tari, et al., “The RAGE axis in early diabetic retinopathy,” Investigative Ophthalmology and Visual Science, vol. 46, no. 8, pp. 2916–2924, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  89. Y. Kaji, T. Usui, S. Ishida, et al., “Inhibition of diabetic leukostasis and blood-retinal barrier breakdown with a soluble form of a receptor for advanced glycation end products,” Investigative Ophthalmology and Visual Science, vol. 48, no. 2, pp. 858–865, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  90. M. Challier, S. Jacqueminet, O. Benabdesselam, A. Grimaldi, and J. L. Beaudeux, “Increased serum concentrations of soluble receptor for advanced glycation endproducts in patients with type 1 diabetes,” Clinical Chemistry, vol. 51, no. 9, pp. 1749–1750, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  91. K. Nakamura, S.-I. Yamagishi, H. Adachi, et al., “Elevation of soluble form of receptor for advanced glycation end products (sRAGE) in diabetic subjects with coronary artery disease,” Diabetes/Metabolism Research and Reviews, vol. 23, no. 5, pp. 368–371, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  92. K. C. Tan, S. W. Shiu, W. S. Chow, L. Leng, R. Bucala, and D. J. Betteridge, “Association between serum levels of soluble receptor for advanced glycation end products and circulating advanced glycation end products in type 2 diabetes,” Diabetologia, vol. 49, no. 11, pp. 2756–2762, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  93. K. Nakamura, S.-I. Yamagishi, T. Matsui, H. Adachi, M. Takeuchi, and T. Imaizumi, “Serum levels of soluble form of receptor for advanced glycation end products (sRAGE) are correlated with AGEs in both diabetic and non-diabetic subjects,” Clinical and Experimental Medicine, vol. 7, no. 4, pp. 188–190, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  94. S.-I. Yamagishi, H. Adachi, K. Nakamura, et al., “Positive association between serum levels of advanced glycation end products and the soluble form of receptor for advanced glycation end products in nondiabetic subjects,” Metabolism, vol. 55, no. 9, pp. 1227–1231, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  95. K. Nakamura, S.-I. Yamagishi, H. Adachi, et al., “Serum levels of sRAGE, the soluble form of receptor for advanced glycation end products, are associated with inflammatory markers in patients with type 2 diabetes,” Molecular Medicine, vol. 13, no. 3-4, pp. 185–189, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  96. K. Nakamura, S.-I. Yamagishi, H. Adachi, et al., “Circulating advanced glycation end products (AGEs) and soluble form of receptor for AGEs (sRAGE) are independent determinants of serum monocyte chemoattractant protein-1 (MCP-1) levels in patients with type 2 diabetes,” Diabetes/Metabolism Research and Reviews, vol. 24, no. 2, pp. 109–114, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  97. S.-I. Yamagishi and T. Imaizumi, “Serum levels of soluble form of receptor for advanced glycation end products (sRAGE) may reflect tissue RAGE expression in diabetes,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 6, p. e32, 2007, author reply e33-e34. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  98. S.-I. Yamagishi, T. Matsui, and K. Nakamura, “Kinetics, role and therapeutic implications of endogenous soluble form of receptor for advanced glycation and products (sRAGE) in diabetes,” Current Drug Targets, vol. 8, no. 10, pp. 1138–1143, 2007. View at Publisher · View at Google Scholar · View at Scopus
  99. J. Miura, Y. Yamamoto, M. Osawa, et al., “Endogenous secretory receptor for advanced glycation endproducts levels are correlated with serum pentosidine and CML in patients with type 1 diabetes,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 1, pp. 253–254, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  100. N. Katakami, M. Matsuhisa, H. Kaneto, et al., “Decreased endogenous secretory advanced glycation end product receptor in type 1 diabetic patients: its possible association with diabetic vascular complications,” Diabetes Care, vol. 28, no. 11, pp. 2716–2721, 2005. View at Publisher · View at Google Scholar · View at Scopus
  101. S. Sakurai, Y. Yamamoto, H. Tamei, et al., “Development of an ELISA for esRAGE and its application to type 1 diabetic patients,” Diabetes Research and Clinical Practice, vol. 73, no. 2, pp. 158–165, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  102. H. Koyama, T. Shoji, H. Yokoyama, et al., “Plasma level of endogenous secretory RAGE is associated with components of the metabolic syndrome and atherosclerosis,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 25, no. 12, pp. 2587–2593, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  103. P. M. Humpert, Z. Djuric, S. Kopf, et al., “Soluble RAGE but not endogenous secretory RAGE is associated with albuminuria in patients with type 2 diabetes,” Cardiovascular Diabetology, vol. 6, article 9, 2007. View at Publisher · View at Google Scholar · View at PubMed
  104. K. Nakamura, S.-I. Yamagishi, Y. Nakamura, et al., “Telmisartan inhibits expression of a receptor for advanced glycation end products (RAGE) in angiotensin-II-exposed endothelial cells and decreases serum levels of soluble RAGE in patients with essential hypertension,” Microvascular Research, vol. 70, no. 3, pp. 137–141, 2005. View at Publisher · View at Google Scholar · View at PubMed
  105. J. C. Mamputu and G. Renier, “Advanced glycation end-products increase monocyte adhesion to retinal endothelial cells through vascular endothelial growth factor-induced ICAM-1 expression: inhibitory effect of antioxidants,” Journal of Leukocyte Biology, vol. 75, no. 6, pp. 1062–1069, 2004. View at Publisher · View at Google Scholar · View at PubMed
  106. K. Miyamoto, S. Khosrof, S. E. Bursell, et al., “Prevention of leukostasis and vascular leakage in streptozotocin-induced diabetic retinopathy via intercellular adhesion molecule-1 inhibition,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 19, pp. 10836–10841, 1999. View at Publisher · View at Google Scholar
  107. Y. Matsumoto, M. Takahashi, and M. Ogata, “Relationship between glycoxidation and cytokines in the vitreous of eyes with diabetic retinopathy,” Japanese Journal of Ophthalmology, vol. 46, no. 4, pp. 406–412, 2002. View at Publisher · View at Google Scholar
  108. S. Okada, K. Shikata, M. Matsuda, et al., “Intercellular adhesion molecule-1-deficient mice are resistant against renal injury after induction of diabetes,” Diabetes, vol. 52, no. 10, pp. 2586–2593, 2003. View at Publisher · View at Google Scholar
  109. F. Y. Chow, D. J. Nikolic-Paterson, E. Ozols, R. C. Atkins, B. J. Rollin, and G. H. Tesch, “Monocyte chemoattractant protein-1 promotes the development of diabetic renal injury in streptozotocin-treated mice,” Kidney International, vol. 69, no. 1, pp. 73–80, 2006. View at Publisher · View at Google Scholar · View at PubMed
  110. A. S. De Vriese, R. G. Tilton, M. Elger, C. C. Stephan, W. Kriz, and N. H. Lameire, “Antibodies against vascular endothelial growth factor improve early renal dysfunction in experimental diabetes,” Journal of the American Society of Nephrology, vol. 12, no. 5, pp. 993–1000, 2001.
  111. A. Flyvbjerg, F. Dagnæs-Hansen, A. S. De Vriese, B. F. Schrijvers, R. G. Tilton, and R. Rasch, “Amelioration of long-term renal changes in obese type 2 diabetic mice by a neutralizing vascular endothelial growth factor antibody,” Diabetes, vol. 51, no. 10, pp. 3090–3094, 2002.
  112. S.-I. Yamagishi, K. Nakamura, K. Takenaka, T. Matsui, and H. Inoue, “Pleiotropic effects of nifedipine on atherosclerosis,” Current Pharmaceutical Design, vol. 12, no. 12, pp. 1543–1547, 2006. View at Publisher · View at Google Scholar
  113. F. L. Celletti, J. M. Waugh, P. G. Amabile, A. Brendolan, P. R. Hilfiker, and M. D. Dake, “Vascular endothelial growth factor enhances atherosclerotic plaque progression,” Nature Medicine, vol. 7, no. 4, pp. 425–429, 2001. View at Publisher · View at Google Scholar · View at PubMed
  114. S.-I. Yamagishi, K. Nakamura, and T. Matsui, “Potential utility of telmisartan, an angiotensin II type 1 receptor blocker with peroxisome proliferator-activated receptor-γ (PPAR-γ)-modulating activity for the treatment of cardiometabolic disorders,” Current Molecular Medicine, vol. 7, no. 5, pp. 463–469, 2007. View at Publisher · View at Google Scholar
  115. T. Matsui, S.-I. Yamagishi, S. Ueda, et al., “Telmisartan, an angiotensin II type 1 receptor blocker, inhibits advanced glycation end-product (AGE)-induced monocyte chemoattractant protein-1 expression in mesangial cells through downregulation of receptor for AGEs via peroxisome proliferator-activated receptor-γ, activation,” Journal of International Medical Research, vol. 35, no. 4, pp. 482–489, 2007.
  116. T. Yoshida, S.-I. Yamagishi, K. Nakamura, et al., “Telmisartan inhibits AGE-induced C-reactive protein production through downregulation of the receptor for AGE via peroxisome proliferator-activated receptor-gamma activation,” Diabetologia, vol. 49, no. 12, pp. 3094–3099, 2006. View at Publisher · View at Google Scholar · View at PubMed
  117. S.-I. Yamagishi, T. Matsui, K. Nakamura, et al., “Olmesartan blocks advanced glycation end products (AGEs)-induced angiogenesis in vitro by suppressing receptor for AGEs (RAGE) expression,” Microvascular Research, vol. 75, no. 1, pp. 130–134, 2008. View at Publisher · View at Google Scholar · View at PubMed
  118. S.-I. Yamagishi, T. Matsui, K. Nakamura, et al., “Olmesartan blocks inflammatory reactions in endothelial cells evoked by advanced glycation end products by suppressing generation of reactive oxygen species,” Ophthalmic Research, vol. 40, no. 1, pp. 10–15, 2007. View at Publisher · View at Google Scholar · View at PubMed
  119. J. Tombran-Tink and C. J. Barnstable, “PEDF: a multifaceted neurotrophic factor,” Nature Reviews Neuroscience, vol. 4, no. 8, pp. 628–636, 2003. View at Publisher · View at Google Scholar · View at PubMed
  120. R. Abe, Y. Fujita, and S.-I. Yamagishi, “Angiogenesis and metastasis inhibitors for the treatment of malignant melanoma,” Mini-Reviews in Medicinal Chemistry, vol. 7, no. 6, pp. 649–661, 2007. View at Publisher · View at Google Scholar
  121. S.-I. Yamagishi, Y. Inagaki, S. Amano, T. Okamoto, M. Takeuchi, and Z. Makita, “Pigment epithelium-derived factor protects cultured retinal pericytes from advanced glycation end product-induced injury through its antioxidative properties,” Biochemical and Biophysical Research Communications, vol. 296, no. 4, pp. 877–882, 2002. View at Publisher · View at Google Scholar
  122. S.-I. Yamagishi, S. Amano, Y. Inagaki, T. Okamoto, M. Takeuchi, and H. Inoue, “Pigment epithelium-derived factor inhibits leptin-induced angiogenesis by suppressing vascular endothelial growth factor gene expression through anti-oxidative properties,” Microvascular Research, vol. 65, no. 3, pp. 186–190, 2003. View at Publisher · View at Google Scholar
  123. S.-I. Yamagishi, Y. Inagaki, K. Nakamura, et al., “Pigment epithelium-derived factor inhibits TNF-α-induced interleukin-6 expression in endothelial cells by suppressing NADPH oxidase-mediated reactive oxygen species generation,” Journal of Molecular and Cellular Cardiology, vol. 37, no. 2, pp. 497–506, 2004. View at Publisher · View at Google Scholar · View at PubMed
  124. S.-I. Yamagishi, K. Nakamura, S. Ueda, S. Kato, and T. Imaizumi, “Pigment epithelium-derived factor (PEDF) blocks angiotensin II signaling in endothelial cells via suppression of NADPH oxidase: a novel anti-oxidative mechanism of PEDF,” Cell and Tissue Research, vol. 320, no. 3, pp. 437–445, 2005. View at Publisher · View at Google Scholar · View at PubMed
  125. S.-I. Yamagishi, T. Matsui, K. Nakamura, et al., “Pigment-epithelium-derived factor (PEDF) inhibits angiotensin-II-induced vascular endothelial growth factor (VEGF) expression in MOLT-3 T cells through anti-oxidative properties,” Microvascular Research, vol. 71, no. 3, pp. 222–226, 2006. View at Publisher · View at Google Scholar · View at PubMed
  126. S.-I. Yamagishi, S. Ueda, T. Matsui, et al., “Pigment epithelium-derived factor (PEDF) prevents advanced glycation end products (AGEs)-elicited endothelial nitric oxide synthase (eNOS) reduction through its anti-oxidative properties,” Protein and Peptide Letters, vol. 14, no. 8, pp. 832–835, 2007. View at Publisher · View at Google Scholar
  127. S.-I. Yamagishi, T. Matsui, K. Nakamura, M. Takeuchi, and T. Imaizumi, “Pigment epithelium-derived factor (PEDF) prevents diabetes- or advanced glycation end products (AGE)-elicited retinal leukostasis,” Microvascular Research, vol. 72, no. 1-2, pp. 86–90, 2006. View at Publisher · View at Google Scholar · View at PubMed
  128. S.-I. Yamagishi, T. Matsui, K. Nakamura, et al., “Pigment-epithelium-derived factor suppresses expression of receptor for advanced glycation end products in the eye of diabetic rats,” Ophthalmic Research, vol. 39, no. 2, pp. 92–97, 2007. View at Publisher · View at Google Scholar · View at PubMed
  129. S.-I. Yamagishi, K. Nakamura, T. Matsui, et al., “Pigment epithelium-derived factor inhibits advanced glycation end product-induced retinal vascular hyperpermeability by blocking reactive oxygen species-mediated vascular endothelial growth factor expression,” Journal of Biological Chemistry, vol. 281, no. 29, pp. 20213–20220, 2006. View at Publisher · View at Google Scholar · View at PubMed
  130. J. Spranger, M. Osterhoff, M. Reimann, et al., “Loss of the antiangiogenic pigment epithelium-derived factor in patients with angiogenic eye disease,” Diabetes, vol. 50, no. 12, pp. 2641–2645, 2001.
  131. B. O. Boehm, G. Lang, O. Volpert, et al., “Low content of the natural ocular anti-angiogenic agent pigment epithelium-derived factor (PEDF) in aqueous humor predicts progression of diabetic retinopathy,” Diabetologia, vol. 46, no. 3, pp. 394–400, 2003.
  132. M. Yokoi, S.-I. Yamagishi, A. Saito, et al., “Positive association of pigment epithelium-derived factor with total antioxidant capacity in the vitreous fluid of patients with proliferative diabetic retinopathy,” British Journal of Ophthalmology, vol. 91, no. 7, pp. 885–887, 2007. View at Publisher · View at Google Scholar · View at PubMed
  133. Y. Yoshida, S.-I. Yamagishi, T. Matsui, et al., “Positive correlation of pigment epithelium-derived factor and total antioxidant capacity in aqueous humour of patients with uveitis and proliferative diabetic retinopathy,” British Journal of Ophthalmology, vol. 91, no. 9, pp. 1133–1134, 2007. View at Publisher · View at Google Scholar · View at PubMed
  134. T. Yoshida, S.-I. Yamagishi, K. Nakamura, et al., “Atorvastatin inhibits advanced glycation end products (AGE)-induced C-reactive expression in hepatoma cells by suppressing reactive oxygen species generation,” Vascular Disease Prevention, vol. 4, no. 3, pp. 213–216, 2007. View at Publisher · View at Google Scholar
  135. S.-I. Yamagishi, T. Matsui, K. Nakamura, and M. Takeuchi, “Minodronate, a nitrogen-containing bisphosphonate, inhibits advanced glycation end product-induced vascular cell adhesion molecule-1 expression in endothelial cells by suppressing reactive oxygen species generation,” International Journal of Tissue Reactions, vol. 27, no. 4, pp. 189–195, 2005.
  136. S.-I. Yamagishi, K. Nakamura, T. Matsui, and M. Takeuchi, “Minodronate, a nitrogen-containing bisphosphonate, is a promising remedy for treating patients with diabetic retinopathy,” Medical Hypotheses, vol. 66, no. 2, pp. 273–275, 2005. View at Publisher · View at Google Scholar · View at PubMed
  137. S.-I. Yamagishi, R. Abe, Y. Inagaki, et al., “Minodronate, a newly developed nitrogen-containing bisphosphonate, suppresses melanoma growth and improves survival in nude mice by blocking vascular endothelial growth factor signaling,” American Journal of Pathology, vol. 165, no. 6, pp. 1865–1874, 2004.
  138. H. Shamoon, H. Duffy, N. Fleischer, et al., “The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus,” The New England Journal of Medicine, vol. 329, no. 14, pp. 977–986, 1993. View at Publisher · View at Google Scholar
  139. R. Turner, “Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33),” The Lancet, vol. 352, no. 9131, pp. 837–853, 1998. View at Publisher · View at Google Scholar