The role of oxidative stress in diabetic complications

Cell Biochemistry and Biophysics

Volumn 43, Issue 2, 2005, Pages 289-330

  Niedowicz, Dana M ^a   Daleke, David L ^a  

^a INDIANA UNIVERSITY   (United States)

Author keywords

Antioxidants; Diabetes mellitus; Free radicals; Glucose autoxidation; Lipid asymmetry; Lipid oxidation; NADPH oxidase; Oxidative phosphorylation; Protein kinase C

Indexed keywords

CYTOKINE; NITRIC OXIDE; REACTIVE OXYGEN METABOLITE;

ANIMAL; ARTICLE; DIABETES MELLITUS; HUMAN; LIPID PEROXIDATION; METABOLISM; OXIDATIVE STRESS;

ANIMALS; CYTOKINES; DIABETES COMPLICATIONS; HUMANS; LIPID PEROXIDATION; NITRIC OXIDE; OXIDATIVE STRESS; REACTIVE OXYGEN SPECIES;

EID: 23244451614     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:43:2:289     Document Type: Article

References (385)

1. National Diabetes Information Clearinghouse. National Diabetes Statistics. Available from: http://diabetes.niddk.nih.gov/dm/pubs/statistics/ index.htm. Accessed September 8, 2004.
2. Brownlee, M. and Cerami, A. (1981) The biochemistry of the complications of diabetes mellitus. Annu. Rev. Biochem. 50, 385-432.
3. Kuusisto, J., Mykkanen, L., Pyorala, K., and Laakso, M. (1994) NIDDM and its metabolic control predict coronary heart disease in elderly subjects. Diabetes 43, 960-967.
4. Luscher, T. F., Creager, M. A., Beckman, J. A., and Cosentino, F. (2003) Diabetes and vascular disease: pathophysiology, clinical consequences, and medical therapy: part II. Circulation 108, 1655-1661.
5. Resnick, H. E. and Howard, B. V. (2002) Diabetes and cardiovascular disease. Annu. Rev. Med. 53, 245-267.
6. Giugliano, D., Ceriello, A., and Paolisso, G. (1996) Oxidative stress and diabetic vascular complications. Diabetes Care 19, 257-267.
7. Creager, M. A., Luscher, T. F., Cosentino, F., and Beckman, J. A. (2003) Diabetes and vascular disease: pathophysiology, clinical consequences, and medical therapy: part I. Circulation 108, 1527-1532.
8. Brownlee, M. (2001) Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813-820.
9. Rosen, P., Du, X., and Tschope, D. (1998) Role of oxygen derived radicals for vascular dysfunction in the diabetic heart: prevention by alpha-tocopherol? Mol. Cell. Biochem. 188, 103-111.
10. Sheetz, M. J. and King, G. L. (2002) Molecular understanding of hyperglycemia's adverse effects for diabetic complications. JAMA. 288, 2579-2588.
11. Roberts, L. J. and Morrow, J. D. (2000) Measurement of F(2)-isoprostanes as an index of oxidative stress in vivo. Free Radic. Biol. Med. 28, 505-513.
12. Pratico, D. (1999) F(2)-isoprostanes: sensitive and specific non-invasive indices of lipid peroxidation in vivo. Atherosclerosis 147, 1-10.
13. Hyun, D. H., Lee, M., Hattori, N., Kubo, S., Mizuno, Y., Halliwell, B., et al. (2002) Effect of wild-type or mutant Parkin on oxidative damage, nitric oxide, antioxidant defenses, and the proteasome. J. Biol. Chem. 277, 28572-28577.
14. 2alpha-III, an index of oxidant stress. Am. J. Respir. Crit. Care Med. 158, 1709-1714.
15. Kwong, L. K. and Sohal, R. S. (1998) Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria. Arch. Biochem. Biophys. 350, 118-126.
16. Yamagishi, S. I., Edelstein, D., Du, X. L., and Brownlee, M. (2001) Hyperglycemia potentiates collagen-induced platelet activation through mitochondrial superoxide overproduction. Diabetes 50, 1491-1494.
17. Nishikawa, T., Edelstein, D., Du, X. L., Yamagishi, S., Matsumura, T., Kaneda, Y., et al. (2000) Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic- damage. Nature 404, 787-790.
18. Du, Y., Miller, C. M., and Kern, T. S. (2003) Hyperglycemia increases mitochondrial superoxide in retina and retinal cells. Free Radic. Biol. Med. 35, 1491-1499.
19. Du, X. L., Edelstein, D., Rossetti, L., Fantus, I. G., Goldberg, H., Ziyadeh, F., et al. (2000) Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. Proc. Natl. Acad. Sci. USA 97, 12222-12226.
20. Nedergaard, J. and Cannon, B. (2003) The 'novel' 'uncoupling' proteins UCP2 and UCP3: what do they really do? Pros and cons for suggested functions. Exp. Physiol. 88, 65-84.
21. Korshunov, S. S., Skulachev, V. P., and Starkov, A. A. (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416, 15-18.
22. Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., et al. (2002) Superoxide activates mitochondrial uncoupling proteins. Nature 415, 96-99.
23. Murphy, M. P., Echtay, K. S., Blaikie, F. H., Asin-Cayuela, J., Cocheme, H. M., Green, K., et al. (2003) Superoxide activates uncoupling proteins by generating carbon-centered radicals and initiating lipid peroxidation: studies using a mitochondria-targeted spin trap derived from alpha-phenyl-N-tert- butylnitrone. J. Biol. Chem. 278, 48534-48545.
24. Pecqueur, C., Alves-Guerra, M. C., Gelly, C., Levi-Meyrueis, C., Couplan, E., Collins, S., et al. (2001) Uncoupling protein 2, in vivo distribution, induction upon oxidative stress, and evidence for translational regulation. J. Biol. Chem. 276, 8705-8512.
25. Zhou, Y. T., Shimabukuro, M., Koyama, K., Lee, Y., Wang, M. Y., Trieu, F., et al. (1997) Induction by leptin of uncoupling protein-2 and enzymes of fatty acid oxidation. Proc. Natl. Acad. Sci. U. S. A. 94, 6386-6390.
26. Bindokas, V. P., Kuznetsov, A., Sreenan, S., Polonsky, K. S., Roe, M. W., and Philipson, L. H. (2003) Visualizing superoxide production in normal and diabetic rat islets of Langerhans. J. Biol. Chem. 278, 9796-9801.
27. Vincent, A. M., Olzmann, J. A., Brownlee, M., Sivitz, W. I., and Russell, J. W. (2004) Uncoupling proteins prevent glucose-induced neuronal oxidative stress and programmed cell death. Diabetes 53, 726-734.
28. Krook, A., Digby, J., O'rahilly, S., Zierath, J. R., and Wallberg-Henriksson, H. (1998) Uncoupling protein 3 is reduced in skeletal muscle of NIDDM patients. Diabetes 47, 1528-1531.
29. Blanc, J., Alves-Guerra, M. C., Esposito, B., Rousset, S., Gourdy, P., Ricquier, D., et al. (2003) Protective role of uncoupling protein 2 in atherosclerosis. Circulation 107, 388-390.
30. Berman, R. S. and Martin, W. (1993) Arterial endothelial barrier dysfunction: actions of homocysteine and the hypoxanthine-xanthine oxidase free radical generating system. Br. J. Pharmacol. 108, 920-926.
31. 2-isoprostanes to plaque instability in human carotid atherosclerosis. J. Clin. Invest. 103, 421-427.
32. Mattiasson, G., Shamloo, M., Gido, G., Mathi, K., Tomasevic, G., Yi, S., et al. (2003) Uncoupling protein-2 prevents neuronal death and diminishes brain dysfunction after stroke and brain trauma. Nat. Med. 9, 1062-1068.
33. Teshima, Y., Akao, M., Jones, S. P., and Marban, E. (2003) Uncoupling protein-2 overexpression inhibits mitochondrial death pathway in cardiomyocytes. Circ. Res. 93, 192-200.
34. Henderson, L. M. and Chappel, J. B. (1996) NADPH oxidase of neutrophils. Biochim. Biophys. Acta 1273, 87-107.
35. Lassegue, B. and Clempus, R. E. (2003) Vascular NAD(P)H oxidases: specific features, expression, and regulation. Am. J. Physiol. Regul. Integr. Comp. Physiol. 285, R277-R297.
36. Inoguchi, T., Li, P., Umeda, F., Yu, H. Y., Kakimoto, M., Imamura, M., Aoki, T., Etoh, T., Hashimoto, T., Naruse, M., Sano, H., Utsumi, H., and Nawata, H. (2000) High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells. Diabetes 49, 1939-1945.
37. Quagliaro, L., Piconi, L., Assaloni, R., Martinelli, L., Motz, E., and Ceriello, A. (2003) Intermittent high glucose enhances apoptosis related- to oxidative stress in human umbilical vein endothelial cells: the role of protein kinase C and NAD(P)H-oxidase activation. Diabetes 52, 2795-2804.
38. Cosentino, F., Eto, M., De Paolis, P., Van Der Loo, B., Bachschmid, M., Ullrich, V., et al. (2003) High glucose causes upregulation of cyclooxygenase-2 and alters prostanoid profile in human endothelial cells: role of protein kinase C and reactive oxygen species. Circulation 107, 1017-1023.
39. Perner, A., Andresen, L., Pedersen, G., and Rask-Madsen, J. (2003) Superoxide production and expression of NAD(P)H oxidases by transformed and primary human colonic epithelial cells. Gut 52, 231-236.
40. Kitada, M., Koya, D., Sugimoto, T., Isono, M., Araki, S., Kashiwagi, A., et al. (2003) Translocation of glomerular p47phox and p67phox by protein kinase C-beta activation is required for oxidative stress in diabetic nephropathy. Diabetes 52, 2603-2614.
41. Hua, H., Munk, S., Goldberg, H., Fantus, I. G., and Whiteside, C. I. (2003) High glucose-suppressed endothelin-1 Ca2+ signaling via NADPH oxidase and diacylglycerol-sensitive protein kinase C isozymes in mesangial cells. J. Biol. Chem. 278, 33951-33962.
42. Seno, T., Inoue, N., Gao, D., Okuda, M., Sumi, Y., Matsui, K., et al. (2001) Involvement of NADH/NADPH oxidase in human platelet ROS production. Thromb. Res. 103, 399-409.
43. Dupuy, C., Virion, A., Ohayon, R., Kaniewski, J., Deme, D., and Pommier, J. (1991) Mechanism of hydrogen peroxide formation catalyzed by NADPH oxidase in thyroid plasma membrane. J. Biol. Chem. 266, 3739-3743.
44. Mohanty, P., Hamouda, W., Garg, R., Aljada, A., Ghanim, H., and Dandona, P. (2000) Glucose challenge stimulates reactive oxygen species (ROS) generation by leucocytes. J. Clin. Endocrinol. Metab. 85, 2970-2973.
45. Babior, B. M. (1999) NADPH oxidase: an update. Blood 93, 1464-1476.
46. Griendling, K. K., Sorescu, D., Lassegue, B., and Ushio-Fukai, M. (2000) Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology. Arterioscler. Thromb. Vasc. Biol. 20, 2175-2183.
47. Inoguchi, T., Sonta, T., Tsubouchi, H., Etoh, T., Kakimoto, M., Sonoda, N., et al. (2003) Protein kinase C-dependent increase in reactive oxygen species (ROS) production in vascular tissues of diabetes: role of vascular NAD(P)H oxidase. J. Am. Soc. Nephrol. 14, S227-S232.
48. Li, J. M. and Shah, A. M. (2003) ROS generation by nonphagocytic NADPH oxidase: potential relevance in diabetic nephropathy. J. Am. Soc. Nephrol. 14, S221-S226.
49. Lee, H. S., Son, S. M., Kim, Y. K., Hong, K. W., and Kim, C. D. (2003) NAD(P)H oxidase participates in the signaling events in high glucose-induced proliferation of vascular smooth muscle cells. Life Sci. 72, 2719-2730.
50. Obrosova, I. G., Minchenko, A. G., Vasupuram, R., White, L., Abatan, O. I., Kumagai, A. K., et al. (2003) Aldose reductase inhibitor fidarestat prevents retinal oxidative stress and vascular endothelial growth factor overexpression in streptozotocin-diabetic rats. Diabetes 52, 864-871.
51. Llorente, L., De La Fuente, H., Richaud-Patin, Y., Alvarado-De La Barrera, C., Diaz-Borjon, A., Lopez-Ponce, A., et al. (2000) Innate immune response mechanisms in non-insulin dependent diabetes mellitus patients assessed by flow cytoenzymology. Immunol. Lett. 74, 239-244.
52. Christ, M., Bauersachs, J., Liebetrau, C., Heck, M., Gunther, A., and Wehling, M. (2002) Glucose increases endothelial-dependent superoxide formation in coronary arteries by NAD(P)H oxidase activation: attenuation by the 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor atorvastatin. Diabetes 51, 2648-2652.
53. Fukui, T., Ishizaka, N., Rajagopalan, S., Laursen, J. B., Capers, Q. T., Taylor, W. R., et al. (1997) p22phox mRNA expression and NADPH oxidase activity are increased in aortas from hypertensive rats. Circ. Res. 80, 45-51.
54. Landmesser, U., Cai, H., Dikalov, S., Mccann, L., Hwang, J., Jo, H., et al. (2002) Role of p47(phox) in vascular oxidative stress and hypertension caused by angiotensin II. Hypertension 40, 511-515.
55. Frustaci, A., Kajstura, J., Chimenti, C., Jakoniuk, I., Leri, A., Maseri, A., et al. (2000) Myocardial cell death in human diabetes. Circ. Res. 87, 1123-1132.
56. Ye, G., Metreveli, N. S., Ren, J., and Epstein, P. N. (2003) Metallothionein prevents diabetes-induced deficits in cardiomyocytes by inhibiting reactive oxygen species production. Diabetes 52, 777-783.
57. Privratsky, J. R., Wold, L. E., Sowers, J. R., Quinn, M. T., and Ren, J. (2003) AT1 blockade prevents glucose-induced cardiac dysfunction in ventricular myocytes: role of the AT1 receptor and NADPH oxidase. Hypertension 42, 206-212.
58. Onozato, M. L., Tojo, A., Goto, A., Fujita, T., and Wilcox, C. S. (2002) Oxidative stress and nitric oxide synthase in rat diabetic nephropathy: effects of ACEI and ARB. Kidney Int. 61, 186-194.
59. Kajstura, J., Fiordaliso, F., Andreoli, A. M., Li, B., Chimenti, S., Medow, M. S., et al. (2001) IGF-1 overexpression inhibits the development of diabetic cardiomyopathy and angiotensin II-mediated oxidative stress. Diabetes 50, 1414-1424.
60. Hink, U., Li, H., Mollnau, H., Oelze, M., Matheis, E., Hartmann, M., et al. (2001) Mechanisms underlying endothelial dysfunction in diabetes mellitus. Circ. Res. 88, E14-E22.
61. Jain, S. K. (1989) Hyperglycemia can cause membrane lipid peroxidation and osmotic fragility in human red blood cells. J. Biol. Chem. 264, 21340-21345.
62. Robertson, R. P., Harmon, J., Tran, P. O., Tanaka, Y., and Takahashi, H. (2003) Glucose toxicity in beta-cells: type 2 diabetes, good radicals gone bad, and the glutathione connection. Diabetes 52, 581-587.
63. Wolff, S. P., Jiang, Z. Y., and Hunt, J. V. (1991) Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Radic. Biol. Med. 10, 339-352.
64. Hunt, J. V., Dean, R. T., and Wolff, S. P. (1988) Hydroxyl radical production and autoxidative glycosylation. Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and ageing. Biochem. J. 256, 205-212.
65. Hunt, J. V. and Wolff, S. P. (1991) Oxidative glycation and free radical production: a causal mechanism of diabetic complications. Free Radic. Res. Commun. 12-13, 115-123.
66. Chace, K. V., Carubelli, R., and Nordquist, R. E. (1991) The role of nonenzymatic glycosylation, transition metals, and free radicals in the formation of collagen aggregates. Arch. Biochem. Biophys. 288, 473-480.
67. Hicks, M., Delbridge, L., Yue, D. K., and Reeve, T. S. (1988) Catalysis of lipid peroxidation by glucose and glycosylated collagen. Biochem. Biophys. Res. Commun. 151, 649-655.
68. Ou, P. and Wolff, S. P. (1994) Erythrocyte catalase inactivation (H2O2 production) by ascorbic acid and glucose in the presence of aminotriazole: role of transition metals and relevance to diabetes. Biochem. J. 303, 935-939.
69. Lomonosova, E. E., Kirsch, M., and De Groot, H. (1998) Calcium vs. iron-mediated processes in hydrogen peroxide toxicity to L929 cells: effects of glucose. Free Radic. Biol. Med. 25, 493-503.
70. Graier, W. F., Simecek, S., Kukovetz, W. R., and Kostner, G. M. (1996) High D-glucose-induced changes in endothelial Ca2+/EDRF signaling are due to generation of superoxide anions. Diabetes 45, 1386-1395.
71. Wolff, S. P. and Dean, R. T. (1987) Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes. Biochem. J. 245, 243-250.
72. Massion, P. B., Feron, O., Dessy, C., and Balligand, J. L. (2003) Nitric oxide and cardiac function: ten years after, and continuing. Circ. Res. 93, 388-398.
73. Zou, M. H., Shi, C., and Cohen, R. A. (2002) Oxidation of the zinc-thiolate complex and uncoupling of endothelial nitric oxide synthase by peroxynitrite. J. Clin. Invest. 109, 817-826.
74. Rosen, G. M., Tsai, P., and Pou, S. (2002) Mechanism of free-radical generation by nitric oxide synthase. Chem. Rev. 102, 1191-1200.
75. Harrison, D. G. (1997) Cellular and molecular mechanisms of endothelial cell dysfunction. J. Clin. Invest. 100, 2153-2157.
76. Wever, R. M., Luscher, T. F., Cosentino, F., and Rabelink, T. J. (1998) Atherosclerosis and the two faces of endothelial nitric oxide synthase. Circulation 97, 108-112.
77. Ceriello, A. (2003) New insights on oxidative stress and diabetic complications may lead to a "causal" antioxidant therapy. Diabetes Care 26, 1589-1596.
78. Shinozaki, K., Kashiwagi, A., Nishio, Y., Okamura, T., Yoshida, Y., Masada, M., et al. (1999) Abnormal biopterin metabolism is a major cause of impaired endothelium-dependent relaxation through nitric oxide/O2-imbalance in insulin-resistant rat aorta. Diabetes 48, 2437-2445.
79. Cosentino, F., Hishikawa, K., Katusic, Z. S., and Luscher, T. F. (1997) High glucose increases nitric oxide synthase expression and superoxide anion generation in human aortic endothelial cells. Circulation 96, 25-28.
80. El-Remessy, A. B., Behzadian, M. A., Abou-Mohamed, G., Franklin, T., Caldwell, R. W., and Caldwell, R. B. (2003) Experimental diabetes causes breakdown of the blood-retina barrier by a mechanism involving tyrosine nitration and increases in expression of vascular endothelial growth factor and urokinase plasminogen activator receptor. Am. J. Pathol. 162, 1995-2004.
81. Kowluru, R. A. (2003) Effect of reinstitution of good glycemic control on retinal oxidative stress and nitrative stress in diabetic rats. Diabetes 52, 818-823.
82. Shinozaki, K., Nishio, Y., Okamura, T., Yoshida, Y., Maegawa, H., Kojima, H., et al. (2000) Oral administration of tetrahydrobiopterin prevents endothelial dysfunction and vascular oxidative stress in the aortas of insulin-resistant rats. Circ. Res. 87, 566-573.
83. Reif, A., Frohlich, L. G., Kotsonis, P., Frey, A., Bommel, H. M., Wink, D. A., et al. (1999) Tetrahydrobiopterin inhibits monomerization and is consumed during catalysis in neuronal NO synthase. J. Biol. Chem. 274, 24921-24929.
84. Kwon, N. S., Nathan, C. F., and Stuehr, D. J. (1989) Reduced biopterin as a cofactor in the generation of nitrogen oxides by murine macrophages. J. Biol. Chem. 264, 20496-20501.
85. Heitzer, T., Krohn, K., Albers, S., and Meinertz, T. (2000) Tetrahydrobiopterin improves endothelium-dependent vasodilation by increasing nitric oxide activity in patients with type II diabetes mellirus. Diabetologia 43, 1435-1438.
86. Szabo, C., Mabley, J. G., Moeller, S. M., Shimanovich, R., Pacher, P., Virag, L., et al. (2002) Part I: pathogenetic role of peroxynitrite in the development of diabetes and diabetic vascular complications: studies with FP15, a novel potent peroxynitrite decomposition catalyst. Mol. Med. 8, 571-580.
87. Turko, I. V., Li, L., Aulak, K. S., Stuehr, D. J., Chang, J. Y., and Murad, F. (2003) Protein tyrosine nitration in the mitochondria from diabetic mouse heart. Implications to dysfunctional mitochondria in diabetes. J. Biol. Chem. 278, 33972-33977.
88. Hoeldtke, R. D., Bryner, K. D., Mcneill, D. R., Hobbs, G. R., and Baylis, C. (2003) Peroxynitrite versus nitric oxide in early diabetes. Am. J. Hypertens. 16, 761-766.
89. Hoeldtke, R. D., Bryner, K. D., Mcneill, D. R., Hobbs, G. R., Riggs, J. E., Warehime, S. S., et al. (2002) Nitrosative stress, uric acid, and peripheral nerve function in early type 1 diabetes. Diabetes 51, 2817-2825.
90. Kossenjans, W., Eis, A., Sahay, R., Brockman, D., and Myatt, L. (2000) Role of peroxynitrite in altered fetal-placental vascular reactivity in diabetes or preeclampsia. Am. J. Physiol. Heart Circ. Physiol. 278, H1311-H1319.
91. Pritsos, C. A. (2000) Cellular distribution, metabolism and regulation of the xanthine oxidoreductase enzyme system. Chem. Biol. Interact. 129, 195-208.
92. Harrison, R. (2002) Structure and function of xanthine oxidoreductase: where are we now? Free Radic. Biol. Med. 33, 774-797.
93. Garattini, E., Mendel, R., Romao, M. J., Wright, R., and Terao, M. (2003) Mammalian molybdoflavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem. J. 372, 15-32.
94. Paler-Martinez, A., Panus, P. C., Chumley, P. H., Ryan, U., Hardy, M. M., and Freeman, B. A. (1994) Endogenous xanthine oxidase does not significantly contribute to vascular endothelial production of reactive oxygen species. Arch. Biochem. Biophys. 311, 79-85.
95. Friedl, H. P., Smith, D. J., Till, G. O., Thomson, P. D., Louis, D. S., and Ward, P. A. (1990) Ischemia-reperfusion in humans. Appearance of xanthine oxidase activity. Am. J. Pathol. 136, 491-495.
96. Salas, A., Panes, J., Elizalde, J. I., Granger, D. N., and Pique, J. M. (1999) Reperfusion-induced oxidative stress in diabetes: cellular and enzymatic sources. J. Leukoc. Biol. 66, 59-66.
97. Desco, M. C., Asensi, M., Marquez, R., Martinez-Valls, J., Vento, M., Pallardo, F. V., et al. (2002) Xanthine oxidase is involved in free radical production in type 1 diabetes: protection by allopurinol. Diabetes 51, 1118-1124.
98. Butler, R., Morris, A. D., Belch, J. J., Hill, A., and Struthers, A. D. (2000) Allopurinol normalizes endothelial dysfunction in type 2 diabetics with mild hypertension. Hypertension 35, 746-751.
99. White, C. R., Darley-Usmar, V., Berrington, W. R., Mcadams, M., Gore, J. Z., Thompson, J. A., et al. (1996) Circulating plasma xanthine oxidase contributes to vascular dysfunction in hypercholesterolemic rabbits. Proc. Natl. Acad. Sci U. S. A. 93, 8745-8749.
100. Aliciguzel, Y., Ozen, I., Asian, M., and Karayalcin, U. (2003) Activities of xanthine oxidoreductase and antioxidant enzymes in different tissues of diabetic rats. J. Lab. Clin. Med. 142, 172-177.
101. Coon, M. J. (2003) Multiple oxidants and multiple mechanisms in cytochrome P450 catalysis. Biochem. Biophys. Res. Commun. 312, 163-168.
102. Guengerich, F. P. (2003) Cytochrome P450 oxidations in the generation of reactive electrophiles: epoxidation and related reactions. Arch. Biochem. Biophys. 409, 59-71.
103. Caro, A. A. and Cederbaum, A. I. (2004) Oxidative stress, toxicology, and pharmacology of CYP2E1. Annu. Rev. Pharmacol. Toxicol. 44, 27-42.
104. Loida, P. J. and Sligar, S. G. (1993) Molecular recognition in cytochrome P-450: mechanism for the control of uncoupling, reactions. Biochemistry 32, 11530-11538.
105. Leclercq, I. A., Farrell, G. C., Field, J., Bell, D. R., Gonzalez, F. J., and Robertson, G. R. (2000) CYP2E1 and CYP4A as microsomal catalysts of lipid peroxides in murine nonalcoholic steatohepatitis. J. Clin. Invest. 105, 1067-1075.
106. Wang, Z., Hall, S. D., Maya, J. F., Li, L., Asghar, A., and Gorski, J. C. (2003) Diabetes mellitus increases the in vivo activity of cytochrome P450 2E1 in humans. Br. J. Clin. Pharmacol. 55, 77-85.
107. Hannon-Fletcher, M. P., O'kane, M. J., Moles, K. W., Barnett, Y. A., and Barnett, C. R. (2001) Lymphocyte cytochrome P450-CYP2E1 expression in human IDDM subjects. Food Chem. Toxicol. 39, 125-132.
108. Haufroid, V., Ligocka, D., Buysschaert, M., Horsmans, Y., and Lison, D. (2003) Cytochrome P4502E1 (CYP2E1) expression in peripheral blood lymphocytes: evaluation in hepatitis C and diabetes. Eur. J. Clin. Pharmacol. 59, 29-33.
109. Leclercq, I. A., Field, J., Enriquez, A., Farrell, G. C., and Robertson, G. R. (2000) Constitutive and inducible expression of hepatic CYP2E1 in leptin-deficient ob/ob mice. Biochem. Biophys. Res. Commun. 268, 337-344.
110. Favreau, L. V., Malchoff, D. M., Mole, J. E., and Schenkman, J. B. (1987) Responses to insulin by two forms of rat hepatic microsomal cytochrome P-450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes. J. Biol. Chem. 262, 14319-14326.
111. Takatori, A., Akahori, M., Kawamura, S., Itagaki, S., and Yoshikawa, Y. (2002) The effects of diabetes with hyperlipidemia on P450 expression in APA hamster livers. J. Biochem. Mol. Toxicol. 16, 174-181.
112. Enriquez, A., Leclercq, I., Farrell, G. C., and Robertson, G. (1999) Altered expression of hepatic CYP2E1 and CYP4A in obese, diabetic ob/ob mice, and fa/fa Zucker rats. Biochem. Biophys. Res. Commun. 255, 300-306.
113. Zangar, R. C. and Novak, R. F. (1997) Effects of fatty acids and ketone bodies on cytochromes P450 2B, 4A, and 2E1 expression in primary cultured rat hepatocytes. Arch. Biochem. Biophys. 337, 217-224.
114. Iber, H., Li-Masters, T., Chen, Q., Yu, S., and Morgan, E. T. (2001) Regulation of hepatic cytochrome P450 2C11 via cAMP: implications for down-regulation in diabetes, fasting, and inflammation. J. Pharmacol. Exp. Ther. 297, 174-180.
115. Pass, G. J., Becker, W., Kluge, R., Linnartz, K., Plum, L., Giesen, K, et al. (2002) Effect of hyperinsulinemia and type 2 diabetes-like hyperglycemia on expression of hepatic cytochrome p450 and glutathione S-transferase isoforms in a New Zealand obese-derived mouse backcross population. J. Pharmacol. Exp. Ther. 302, 442-450.
116. Chanez, P., Bonnans, C., Chavis, C., and Vachier, I. (2002) 15-lipoxygenase: a Janus enzyme? Am. J. Respir. Cell. Mol. Biol. 27, 655-658.
117. Brash, A. R. (1999) Lipoxygenases: occurrence, functions, catalysis, and acquisition of substrate. J. Biol. Chem. 274, 23679-23682.
118. Furstenberger, G., Marks, F., and Krieg, P. (2002) Arachidonate 8(S)-lipoxygenase. Prostaglandins Other Lipid Mediat. 68-69, 235-243.
119. Yoshimoto, T. and Takahashi, Y. (2002) Arachidonate 12-lipoxygenases. Prostaglandins Other Lipid Mediat. 68-69, 245-262.
120. Kuhn, H., Walther, M., and Kuban, R. J. (2002) Mammalian arachidonate 15-lipoxygenases structure, function, and biological implications. Prostaglandins Other Lipid Mediat. 68-69, 263-290.
121. Schewe, T. (2002) 15-lipoxygenase-1: a prooxidant enzyme. Biol. Chem. 383, 365-374.
122. Conrad, D. J. (1999) The arachidonate 12/15 lipoxygenases. A review of tissue expression and biologic function. Clin. Rev. Allergy Immunol. 17, 71-89.
123. Funk, C. D. and Cyrus, T. (2001) 12/15-lipoxygenase, oxidative modification of LDL and atherogenesis. Trends Cardiovasc. Med. 11, 116-124.
124. Natarajan, R. and Nadler, J. L. (2003) Lipoxygenases and lipid signaling in vascular cells in diabetes. Front Biosci. 8, s783-s795.
125. Dandona, P. and Aljada, A. (2002) A rational approach to pathogenesis and treatment of type 2 diabetes mellitus, insulin resistance, inflammation, and atherosclerosis. Am. J. Cardiol. 90, 27G-33G.
126. Hatley, M. E., Srinivasan, S., Reilly, K. B., Bolick, D. T., and Hedrick, C. C. (2003) Increased production of 12/15 lipoxygenase eicosanoids accelerates monocyte/endothelial interactions in diabetic db/db mice. J. Biol. Chem. 278, 25369-25375.
127. Patricia, M. K., Natarajan, R., Dooley, A. N., Hernandez, F., Gu, J. L., Berliner, J. A., et al. (2001) Adenoviral delivery of a leukocyte-type 12 lipoxygenase ribozyme inhibits effects of glucose and platelet-derived growth factor in vascular endothelial and smooth muscle cells. Circ. Res. 88, 659-665.
128. Bleich, D., Chen, S., Zipser, B., Sun, D., Funk, C. D., and Nadler, J. L. (1999) Resistance to type 1 diabetes induction in 12-lipoxygenase knockout mice. J. Clin. Invest. 103, 1431-1436.
129. Maritim, A. C., Sanders, R. A., and Watkins, J. B., 3rd (2003) Diabetes, oxidative stress, and antioxidants: a review. J. Biochem. Mol. Toxicol. 17, 24-38.
130. Sundaram, R. K., Bhaskar, A., Vijayalingam, S., Viswanathan, M., Mohan, R., and Shanmugasundaram, K. R. (1996) Antioxidant status and lipid peroxidation in type II diabetes mellitus with and without complications. Clin. Sci. (Lond). 90, 255-260.
131. Nourooz-Zadeh, J., Rahimi, A., Tajaddini-Sarmadi, J., Tritschler, H., Rosen, P., Halliwell, B., et al. (1997) Relationships between plasma measures of oxidative stress and metabolic control in NIDDM. Diabetologia 40, 647-653.
132. Martin-Gallan, P., Carrascosa, A., Gussinye, M., and Dominguez, C. (2003) Biomarkers of diabetes-associated oxidative stress and antioxidant status in young diabetic patients with or without subclinical complications. Free Radic. Biol. Med. 34, 1563-1574.
133. Davison, G. W., George, L., Jackson, S. K., Young, I. S., Davies, B., Bailey, D. M., et al. (2002) Exercise, free radicals, and lipid peroxidation in type 1 diabetes mellitus. Free Radic. Biol. Med. 33, 1543-1551.
134. Wilson, M. (1998) The Effect of Hyperglycemia on Erythrocyte Phospholipid Organization. Indiana University: Bloomington, IN.
135. Jain, S. K., Palmer, M., and Chen, Y. (1999) Effect of vitamin E and N-acetylcysteine on phosphatidylserine externalization and induction of coagulation by high-glucose-treated human erythrocytes. Metabolism 48, 957-959.
136. Trachtman, H. (1994) Vitamin E prevents glucose-induced lipid peroxidation and increased collagen production in cultured rat mesangial cells. Microvasc. Res. 47, 232-239.
137. Sharpe, P. C., Yue, K. K., Catherwood, M. A., Mcmaster, D., and Trimble, E. R. (1998) The effects of glucose-induced oxidative stress on growth and extracellular matrix gene expression of vascular smooth muscle cells. Diabetologia 41, 1210-1219.
138. Jachec, W., Tomasik, A., Tarnawski, R., and Chwalinska, E. (2002) Evidence of oxidative stress in the renal cortex of diabetic rats: favourable effect of vitamin E. Scand. J. Clin. Lab. Invest. 62, 81-88.
139. Jain, S. K., Mcvie, R., Jaramillo, J. J., Palmer, M., Smith, T., Meachum, Z. D., et al. (1996) The effect of modest vitamin E supplementation on lipid peroxidation products and other cardiovascular risk factors in diabetic patients. Lipids 31 Suppl, S87-S90.
140. Jain, S. K., Krueger, K. S., Mcvie, R., Jaramillo, J. J., Palmer, M., and Smith, T. (1998) Relationship of blood thromboxane-B2 (TxB2) with lipid peroxides and effect of vitamin E and placebo supplementation on TxB2 and lipid peroxide levels in type 1 diabetic patients. Diabetes Care 21, 1511-1516.
141. May, J. M., Qu, Z. C., and Morrow, J. D. (1996) Interaction of ascorbate and alpha-tocopherol in resealed human erythrocyte ghosts. Transmembrane electron transfer and protection from lipid peroxidation. J. Biol. Chem. 271, 10577-10582.
142. Ford, E. S., Mokdad, A. H., Giles, W. H., and Brown, D. W. (2003) The metabolic syndrome and antioxidant concentrations: findings from the Third National Health and Nutrition Examination Survey. Diabetes 52, 2346-2352.
143. Vanderjagt, D. J., Harrison, J. M., Ratliff, D. M., Hunsaker, L. A., and Vander Jagt, D. L. (2001) Oxidative stress indices in IDDM subjects with and without long-term diabetic complications. Clin. Biochem. 34, 265-270.
144. Obrosova, I. G., Fathallah, L., Liu, E., and Nourooz-Zadeh, J. (2003) Early oxidative stress in the diabetic kidney: effect of DL-alpha-lipoic acid. Free Radic. Biol. Med. 34, 186-195.
145. Kashiba, M., Oka, J., Ichikawa, R., Kasahara, E., Inayama, T., Kageyama, A., et al. (2002) Impaired ascorbic acid metabolism in streptozotocin-induced diabetic rats. Free Radic. Biol. Med. 33, 1221-1230.
146. Catherwood, M. A., Powell, L. A., Anderson, P., Mcmaster, D., Sharpe, P. C., and Trimble, E. R. (2002) Glucose-induced oxidative stress in mesangial cells. Kidney Int. 61, 599-608.
147. Hamilton, J. S., Powell, L. A., Mcmaster, C., Mcmaster, D., and Trimble, E. R. (2003) Interaction of glucose and long chain fatty acids (C18) on antioxidant defences and free radical damage in porcine vascular smooth muscle cells in vitro. Diabetologia 46, 106-114.
148. Van Dam, P. S., Van Asbeck, B. S., Van Oirschot, J. F., Biessels, G. J., Hamers, F. P., and Marx, J. J. (2001) Glutathione and alpha-lipoate in diabetic rats: nerve function, blood flow and oxidative state. Eur. J. Clin. Invest. 31, 417-424.
149. Yilmaz, O., Ozkan, Y., Yildirim, M., Ozturk, A. I., and Ersan, Y. (2002) Effects of alpha lipoic acid, ascorbic acid-6-palmitate, and fish oil on the glutathione, malonaldehyde, and fatty acids levels in erythrocytes of streptozotocin induced diabetic male rats. J. Cell. Biochem. 86, 530-539.
150. Aragno, M., Parola, S., Brignardello, E., Manti, R., Betteto, S., Tamagino, E., et al. (2001) Oxidative stress and eicosanoids in the kidneys of hyperglycemic rats treated with dehydroepiandrosterone. Free Rad. Biol. Med. 31, 935-942.
151. Tagami, S., Kondo, T., Yoshida, K., Hirokawa, J., Ohtsuka, Y., and Kawakami, Y. (1992) Effect of insulin on impaired antioxidant activities in aortic endothelial cells from diabetic rabbits. Metabolism 41, 1053-1058.
152. Sailaja, Y. R., Baskar, R., and Saralakumari, D. (2003) The antioxidant status during maturation of reticulocytes to erythrocytes in type 2 diabetics. Free Radic. Biol. Med. 35, 133-139.
153. Murakami, K., Kondo, T., Ohtsuka, Y., Fujiwara, Y., Shimada, M., and Kawakami, Y. (1989) Impairment of glutathione metabolism in erythrocytes from patients with diabetes mellitus. Metabolism 38, 753-758.
154. Thomas, G., Skrinska, V., Lucas, F. V., and Schumacher, O. P. (1985) Platelet glutathione and thromboxane synthesis in diabetes. Diabetes 34, 951-954.
155. Chari, S. N., Nath, N., and Rathi, A. B. (1984) Glutathione and its redox system in diabetic polymorphonuclear leukocytes. Am. J. Med. Sci. 287, 14-15.
156. Liang, Q., Carlson, E. C., Donthi, R. V., Kralik, P. M., Shen, X., and Epstein, P. N. (2002) Overexpression of metallothionein reduces diabetic cardiomyopathy. Diabetes 51, 174-181.
157. Thornalley, P. J., Mclellan, A. C., Lo, T. W., Benn, J., and Sonksen, P. H. (1996) Negative association between erythrocyte reduced glutathione concentration and diabetic complications. Clin. Sci. (Lond). 91, 575-582.
158. Packer, L., Kraemer, K., and Rimbach, G. (2001) Molecular aspects of lipoic acid in the prevention of diabetes complications. Nutrition 17, 888-895.
159. Coppey, L. J., Gellett, J. S., Davidson, E. P., Dunlap, J. A., Lund, D. D., and Yorek, M. A. (2001) Effect of antioxidant treatment of streptozotocin-induced diabetic rats on endoneurial blood flow, motor nerve conduction velocity, and vascular reactivity of epineurial arterioles of the sciatic nerve. Diabetes 50, 1927-1937.
160. Obrosova, I. G., Fathallah, L., and Greene, D. A. (2000) Early changes in lipid peroxidation and antioxidative defense in diabetic rat retina: effect of DL-alpha-lipoic acid. Eur. J. Pharmacol. 398, 139-146.
161. Bojunga, J., Dresar-Mayert, B., Usadel, K. H., Kusterer, K., and Zeuzem, S. (2004) Antioxidative treatment reverses imbalances of nitric oxide synthase
162. Stevens, M. J., Obrosova, I., Cao, X., Van Huysen, C., and Greene, D. A. (2000) Effects of DL-alpha-lipoic acid on peripheral nerve conduction, blood flow, energy metabolism, and oxidative stress in experimental diabetic neuropathy. Diabetes 49, 1006-1015.
163. Heitzer, T., Finckh, B., Albers, S., Krohn, K., Kohlschutter, A., and Meinertz, T. (2001) Beneficial effects of alpha-lipoic acid and ascorbic acid on endothelium-dependent, nitric oxide-mediated vasodilation in diabetic patients: relation to parameters of oxidative stress. Free Radic. Biol. Med. 31, 53-61.
164. Ametov, A. S., Barinov, A., Dyck, P. J., Hermann, R., Kozlova, N., Litchy, W. J., et al. (2003) The sensory symptoms of diabetic polyneuropathy are improved with alpha-lipoic acid: the SYD-NEY trial. Diabetes Care 26, 770-776.
165. Midaoui, A. E., Elimadi, A., Wu, L., Haddad, P. S., and De Champlain, J. (2003) Lipoic acid prevents hypertension, hyperglycemia, and the increase in heart mitochondrial superoxide production. Am. J. Hypertens. 16, 173-179.
166. Arthur, J. R. (2000) The glutathione peroxidases. Cell. Mol. Life Sci. 57, 1825-1835.
167. Hodgkinson, A. D., Bartlett, T., Oates, P. J., Millward, B. A., and Demaine, A. G. (2003) The response of antioxidant genes to hyperglycemia is abnormal in patients with type 1 diabetes and diabetic nephropathy. Diabetes 52, 846-851.
168. Salvemini, F., Franze, A., lervolino, A., Filosa, S., Salzano, S., and Ursini, M. V. (1999) Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression. J. Biol. Chem. 274, 2750-2757.
169. Pandolfi, P. P., Sonati, F., Rivi, R., Mason, P., Grosveld, F., and Luzzatto, L. (1995) Targeted disruption of the housekeeping gene encoding glucose-6-phosphate dehydrogenase:(G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J. 14, 5209-5215.
170. Leopold, J. A., Cap, A., Scribner, A. W., Stanton, R. C., and Loscalzo, J. (2001) Glucose-6-phosphate dehydrogenase deficiency promotes endothelial oxidant stress and decreases endothelial nitric oxide bioavailability. FASEB J. 15, 1771-1773.
171. Ingrosso, D., Cimmino, A., D'angelo, S., Alfinito, F., Zappia, V., and Galletti, P. (2002) Protein methylation as a marker of aspartate damage in glucose-6-phosphate dehydrogenase-deficient erythrocytes: role of oxidative stress. Eur. J. Biochem. 269, 2032-2039.
172. Ho, H. Y., Cheng, M. L., Lu, F. J., Chou, Y. H., Stern, A., Liang, C. M., et al. (2000) Enhanced oxidative stress and accelerated cellular senescence in glucose-6-phosphate dehydrogenase (G6PD)-deficient human fibroblasts. Free Radic. Biol. Med. 29, 156-169.
173. Zhang, Z., Apse, K., Pang, J., and Stanton, R. C. (2000) High glucose inhibits glucose-6-phosphate dehydrogenase via cAMP in aortic endothelial cells. J. Biol. Chem. 275, 40042-40047.
174. Donma, O., Yorulmaz, E., Pekel, H., and Suyugul, N. (2002) Blood and lens lipid peroxidation and antioxidant status in normal individuals, senile and diabetic cataractous patients. Curr. Eye Res. 25, 9-16.
175. Otton, R., Mendonca, J. R., and Curi, R. (2002) Diabetes causes marked changes in lymphocyte metabolism. J. Endocrinol. 174, 55-61.
176. Sochor, M., Kunjara, S., Greenbaum, L., and Mclean, P. (1986) Renal hypertrophy in experimental diabetes: effect of diabetes on the pathways of glucose metabolism: differential response in adult and immature rats. Biochem. J. 234, 573-577.
177. Asahina, T., Kashiwagi, A., Nishio, Y., Ikebuchi, M., Harada, N., Tanaka, Y., et al. (1995) Impaired activation of glucose oxidation and NADPH supply in human endothelial cells exposed to H2O2 in high-glucose medium. Diabetes 44, 520-526.
178. Zelko, I. N., Mariani, T. J., and Folz, R. J. (2002) Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic. Biol. Med. 33, 337-349.
179. Derubertis, F. R., Craven, P. A., Melhem, M. F., and Salah, E. M. (2004) Attenuation of renal injury in db/db mice overexpressing superoxide dismutase: evidence for reduced superoxide-nitric oxide interaction. Diabetes 53, 762-868.
180. Karasu, C. (1999) Increased activity of H2O2 in aorta isolated from chronically streptozotocin-diabetic rats: effects of antioxidant enzymes and enzymes inhibitors. Free Radic. Biol. Med. 27, 16-27.
181. Kirkman, H. N., Rolfo, M., Ferraris, A. M., and Gaetani, G. F. (1999) Mechanisms of protection of catalase by NADPH. J. Biol. Chem. 274, 13908-13914.
182. Goth, L. and Eaton, J. W. (2000) Hereditary catalase deficiencies and increased risk of diabetes. Lancet 356, 1820-1821.
183. Goth, L., Lenkey, A., and Bigler, W. N. (2001) Blood catalase deficiency and diabetes in Hungary. Diabetes Care 24, 1839-1840.
184. Srivastava, S., Dixit, B. L., Cai, J., Sharma, S., Hurst, H. E., Bhatnagar, Aet al. (2000) Metabolism of lipid peroxidation product, 4-hydroxynonenal (HNE) in rat erythrocytes: role of aldose reductase. Free Radic. Biol. Med. 29, 642-651.
185. Chandra, D., Jackson, E. B., Ramana, K. V., Kelley, R., Srivastava, S. K., and Bhatnagar, A. (2002) Nitric oxide prevents aldose reductase activation and sorbitol accumulation during diabetes. Diabetes 51, 3095-3101.
186. Lee, A. Y., Chung, S. K., and Chung, S. S. (1995) Demonstration that polyol accumulation is responsible for diabetic cataract by the use of transgenic mice expressing the aldose reductase gene in the lens. Proc. Natl. Acad. Sci. U. S. A. 92, 2780-2784.
187. Nishimura, C., Hotta, Y., Gui, T., Seko, A., Fujimaki, T., Ishikawa, T., et al. (1997) The level of erythrocyte aldose reductase is associated with the severity of diabetic retinopathy. Diabetes Res. Clin. Pract. 37, 173-177.
188. Malone, J. I., Knox, G., Benford, S., and Tedesco, T. A. (1980) Red cell sorbitol: an indicator of diabetic control. Diabetes 29, 861-864.
189. Oishi, N., Kubo, E., Takamura, Y., Maekawa, K., Tanimoto, T., and Akagi, Y. (2002) Correlation between erythrocyte aldose reductase level and human diabetic retinopathy. Br. J. Ophthalmol. 86, 1363-1366.
190. Nakamura, J., Koh, N., Sakakibara, F., Hamada, Y., Wakao, T., Hara, T., et al. (1995) Polyol pathway, 2,3-diphosphoglycerate in erythrocytes and diabetic neuropathy in rats. Eur. J. Pharmacol. 294, 207-214.
191. Takahashi, Y., Tachikawa, T., Ito, T., Takayama, S., Omori, Y., and Iwamoto, Y. (1998) Erythrocyte aldose reductase protein: a clue to elucidate risk factors for diabetic neuropathies independent of glycemic control. Diabetes Res. Clin. Pract. 42, 101-107.
192. Maeda, S., Haneda, M., Yasuda, H., Tachikawa, T., Isshiki, K., Koya, D., et al. (1999) Diabetic nephropathy is not associated with the dinucleotide repeat polymorphism upstream of the aldose reductase (ALR2) gene but with erythrocyte aldose reductase content in Japanese subjects with type 2 diabetes. Diabetes 48, 420-422.
193. Raccah, D., Coste, T., Cameron, N. E., Dufayet, D., Vague, P., and Hohman, T. C. (1998) Effect of the aldose reductase inhibitor tolrestat on nerve conduction velocity, Na/K ATPase activity, and polyols in red blood cells, sciatic nerve, kidney cortex, and kidney medulla of diabetic rats. J. Diabetes Complications 12, 154-162.
194. Ito, T., Nishimura, C., Takahashi, Y., Saito, T., and Omori, Y. (1997) The level of erythrocyte aldose reductase: a risk factor for diabetic neuropathy? Diabetes Res. Clin. Pract. 36, 161-167.
195. Asano, T., Saito, Y., Kawakami, M., and Yamada, N. (2002) Fidarestat (SNK-860), a potent aldose reductase inhibitor, normalizes the elevated sorbitol accumulation in erythrocytes of diabetic patients. J. Diabetes Complications 16, 133-138.
196. Hamada, Y., Nishimura, C., Koh, N., Sakakibara, F., Nakamura, J., Tanimoto, T., et al. (1998) Influence of interindividual variability of aldose reductase protein content on polyolpathway metabolites and redox state in erythrocytes in diabetic patients. Diabetes Care 21, 1014-1018.
197. Bravi, M. C., Pietrangeli, P., Laurenti, O., Basili, S., Cassone-Faldetta, M., Ferri, C., et al. (1997) Polyol pathway activation and glutathione redox status in non-insulin-dependent diabetic patients. Metabolism 46, 1194-1198.
198. Hamada, Y., Odagaki, Y., Sakakibara, F., Naruse, K., Koh, N., and Hotta, N. (1995) Effects of an aldose reductase inhibitor on erythrocyte fructose 3-phosphate and sorbitol 3-phosphate levels in diabetic patients. Life Sci. 57, 23-29.
199. Hamada, Y., Nakamura, J., Naruse, K., Komori, T., Kato, K., Kasuya, Y., et al. (2000) Epalrestat, an aldose reductase ihibitor, reduces the levels of Nepsilon-(carboxymethyl)lysine protein adducts and their precursors in erythrocytes from diabetic patients. Diabetes Care 23, 1539-1544.
200. Vincent, T. E., Mendiratta, S., and May, J. M. (1999) Inhibition of aldose reductase in human erythrocytes by vitamin C. Diabetes Res. Clin. Pract. 43, 1-8.
201. Wang, H., Zhang, Z. B., Wen, R. R., and Chen, J. W. (1995) Experimental and clinical studies on the reduction of erythrocyte sorbitol-glucose ratios by ascorbic acid in diabetes mellitus. Diabetes Res. Clin. Pract. 28, 1-8.
202. Slatter, D. A., Bolton, C. H., and Bailey, A. J. (2000) The importance of lipid-derived malondialdehyde in diabetes mellitus. Diabetologia 43, 550-557.
203. Jain, S. K. (1985) In vivo externalization of phosphatidylserine and phosphatidylethanolamine in the membrane bilayer and hypercoagulability by the lipid peroxidation of erythrocytes in rats. J. Clin. Invest. 76, 281-286.
204. Romero, M. J., Bosch-Morell, F., Romero, B., Rodrigo, J. M., Serra, M. A., and Romero, F. J. (1998) Serum malondialdehyde: possible use for the clinical management of chronic hepatitis C patients. Free Radic. Biol. Med. 25, 993-997.
205. Muchova, J., Sustrova, M., Garaiova, I., Liptakova, A., Blazicek, P., Kvasnicka, P., et al Z. (2001) Influence of age on activities of antioxidant enzymes and lipid peroxidation products in erythrocytes and neutrophils of Down syndrome patients. Free Radic. Biol. Med. 31, 499-508.
206. Marnett, L. J. (2002) Oxy radicals, lipid peroxidation and DNA damage. Toxicology 181-182, 219-222.
207. Tuma, D. J. (2002) Role of malondialdehydeacetaldehyde adducts in liver injury. Free Radic. Biol. Med. 32, 303-308.
208. Dib, M., Garrel, C., Favier, A., Robin, V., and Desnuelle, C. (2002) Can malondialdehyde be used as a biological marker of progression in neurodegenerative disease? J. Neurol. 249, 367-374.
209. Jain, S. K., Morshed, K. M., Kannan, K., Mcmartin, K. E., and Bocchini, J. A., Jr. (1996) Effect of elevated glucose concentrations on cellular lipid peroxidation and growth of cultured human kidney proximal tubule cells. Mol. Cell. Biochem. 162, 11-16.
210. Rajeswari, P., Natarajan, R., Nadler, J. L., Kumar, D., and Kalra, V. K. (1991) Glucose induces lipid peroxidation and inactivation of membrane-associated ion-transport enzymes in human erythrocytes in vivo and in vitro. J. Cell. Physiol. 149, 100-109.
211. Wittenstein, B., Klein, M., Finckh, B., Ullrich, K., and Kohlschutter, A. (2002) Plasma antioxidants in pediatric patients with glycogen storage disease, diabetes mellitus, and hypercholesterolemia. Free Radic. Biol. Med. 33, 103-110.
212. Olusi, S. O. (2002) Obesity is an independent risk factor for plasma lipid peroxidation and depletion of erythrocyte cytoprotectic enzymes in humans. Int. J. Obes. Relat. Metab. Disord. 26, 1159-1164.
213. Jain, S. K. and Mcvie, R. (1999) Hyperketonemia can increase lipid peroxidation and lower glutathione levels in human erythrocytes in vitro and in type 1 diabetic patients. Diabetes 48, 1850-1855.
214. Jain, S. K., Mcvie, R., Jackson, R., Levine, S. N., and Lim, G. (1999) Effect of hyperketonemia on plasma lipid peroxidation levels in diabetic patients. Diabetes Care 22, 1171-1175.
215. Jain, S. K., Kannan, K., and Lim, G. (1998) Ketosis (acetoacetate) can generate oxygen radicals and cause increased lipid peroxidation and growth inhibition in human endothelial cells. Free Radic. Biol. Med. 25, 1083-1088.
216. Schneider, C., Tallman, K. A., Porter, N. A., and Brash, A. R. (2001) Two distinct pathways of formation of 4-hydroxynonenal. Mechanisms of nonenzymatic transformation of the 9- and 13-hydroperoxides of linoleic acid to 4-hydroxyalkenals. J. Biol. Chem. 276, 20831-20838.
217. Hoff, H. F., O'Neil, J., Wu, Z., Hoppe, G., and Salomon, R. L. (2003) Phospholipid hydroxyalkenals: biological and chemical properties of specific oxidized lipids present in atherosclerotic lesions. Arterioscler. Thromb. Vasc. Biol. 23, 275-282.
218. Friguet, B. and Szweda, L. I. (1997) Inhibition of the mulitcatalytic proteinase by 4-hydroxy-2-nonenal cross-linked protein. FEBS Lett. 405, 21-25.
219. Uchida, K., Shiraishi, M., Naito, Y., Torii, Y., Nakamura, Y., and Osawa, T. (1999) Activation of stress signaling pathways by the end product of lipid peroxidation. 4-hydroxy-2-nonenal is a potential inducer of intracellular peroxide production. J. Biol. Chem. 274, 2234-2242.
220. Traverse, N., Menini, S., Odetti, P., Pronzato, M. A., Cottalasso, D., and Marinari, U. M. (2002) Diabetes impairs the enzymatic disposal of 4-hydroxynonenal in rat liver. Free Radic. Biol. Med. 32, 350-359.
221. Yla-Herttuala, S., Palinski, W., Rosenfeld, M. E., Parthasarathy, S., Carew, T. E., Butler, S., Witztum, J. L., and Steinberg, D. (1989) Evidence for the presence of oxidatively modified low density lipoprotein in atherosclerotic lesions of rabbit and man. J. Clin. Invest. 84, 1086-1095.
222. Jurgens, G., Chen, Q., Esterbauer, H., Mair, S., Ledinski, G., and Dinges, H. P. (1993) Immunostaining of human autopsy aortas with antibodies to modified apolipoprotein B and apoprotein(a). Arterioscler. Thromb. 13, 1689-1699.
223. Heinecke, J. W. (1998) Oxidants and antioxidants in the pathogenesis of atherosclerosis: implications for the oxidized low density lipoprotein hypothesis. Atherosclerosis. 141, 1-15.
224. Seeds, M. C. and Bass, D. A. (1999) Regulation and metabolism of arachidonic acid. Clin. Rev. Allergy Immunol. 17, 5-26.
225. Kalyankrishna, S., Parmentier, J. H., and Malik, K. U. (2002) Arachidonic acid-derived oxidation products initiate apoptosis in vascular smooth muscle cells. Prostaglandins Other Lipid Mediat. 70, 13-29.
226. Nourooz-Zadeh, J., Tajaddini-Sarmadi, J., Mccarhty, S., Betteridge, D. J., and Wolff, S. P. (1995) Elevated levels of authentic plasma hydroperoxides in NIDDM. Diabetes 44, 1054-1058.
227. Santini, S. A., Marra, G., Giardina, B., Cotroneo, P., Mordente, A., Martorana, G. E., et al. (1997) Defective plasma antioxidant defenses and enhanced susceptibility to lipid peroxidation in uncomplicated IDDM. Diabetes 46, 1853-1858.
228. Berg, T. J., Nourooz-Zadeh, J., Wolff, S. P., Tritschler, H. J., Bangstad, H. J., and Hanssen, K. F. (1998) Hydroperoxides in plasma are reduced by intensified insulin treatment: a randomized controlled study of IDDM patients with microalbuminuria. Diabetes Care 21, 1295-1300.
229. Patricia, M. K., Kim, J. A., Harper, C. M., Shih, P. T., Berliner, J. A., Natarajan, R., et al. (1999) Lipoxy-genase products increase monocyte adhesion to human aortic endothelial cells. Arterioscler. Thromb. Vasc. Biol. 19, 2615-2622.
230. Cyrus, T., Witztum, J. L., Rader, D. J., Tangirala, R., Fazio, S., Linton, M. F., et al. (1999) Disruption of the 12/15-lipoxygenase gene diminishes atherosclerosis in apo E-deficient mice. J. Clin. Invest. 103, 1597-1604.
231. George, J., Afek, A., Shaish, A., Levkovitz, H., Bloom, N., Cyrus, T., et al. (2001) 12/15-Lipoxygenase gene disruption attenuates atherogenesis in LDL receptor-deficient mice. Circulation 104, 1646-1650.
232. Harats, D., Shaish, A., George, J., Mulkins, M., Kurihara, H., Levkovitz, H., et al. (2000) Overexpression of 15-lipoxygenase in vascular endothelium accelerates early atherosclerosis in LDL receptor-deficient mice. Arterioscler. Thromb. Vasc. Biol. 20, 2100-2105.
233. Shen, J., Herderick, E., Cornhill, J. F., Zsigmond, E., Kim, H. S., Kuhn, H., et al. (1996) Macrophage-mediated 15-lipoxygenase expression protects against atherosclerosis development. J. Clin. Invest. 98, 2201-2208.
234. Honda, H. M., Leitinger, N., Frankel, M., Goldhaber, J. I., Natarajan, R., Nadler, J. L., et al. (1999) Induction of monocyte binding to endothelial cells by MM-LDL: role of lipoxygenase metabolites. Arterioscler. Thromb. Vasc. Biol. 19, 680-686.
235. Morrow, J. D., Hill, K. E., Burk, R. F., Nammour, T. M., Badr, K. F., and Roberts, L. J. (1990) A series of prostaglandin p2-like compounds are produced in vivo in humans by a non-cyclooxygenase, free radical mechanism. Proc. Natl. Acad. Sci. U. S. A. 87, 9383-9387.
236. 2-isoprostanes, prostaglandin-like products of lipid peroxidation, in Free Radicals: A Pratical Approach (Punchard, N. A. and Kelly, F. J., ed.). Oxford University Press: New York, pp. 147-157.
237. Morrow, J. D. and Roberts, L. J., II (1996) The isoprostanes. Current knowledge and directions for future research. Biochem. Pharmacol. 51, 1-9.
238. Morrow, J. D. and Roberts, L. J. (1997) The isoprostanes: unique bioactive products of lipid peroxidation. Prog. Lipid Res. 36, 1-21.
239. Roberts, L. J., II and Morrow, J. D. (1997) The generation and actions of isoprostanes. Biochim. Biophys. Acta 1345, 121-135.
240. 2alpha-III induce cardiomyocyte hypertrophy. J. Biol. Chem. 273, 22442-22452.
241. 2alpha-III). Prostaglandins Other Lipid Mediat. 57, 319-331.
242. 2-isoprostane stimulates cell proliferation and endothelin-1 expression on endothelial cells. Kidney Int. 56, 471-478.
243. 2 receptors in human platelets. J. Pharmacol Exp Therapeutics 270, 1192-1196.
244. 2alpha is not mediated by thromboxane receptor isoforms. J. Biol. Chem. 271, 14916-14924.
245. 2alpha, a potent agonist of the vascular thromboxane/endoperoxide receptor, is a platelet thromboxane/ endoperoxide receptor antagonist. Prostaglandins 44, 155-163.
246. Leitinger, N., Blazek, I., and Sinzinger, H. (1997) The influence of isoprostanes on ADP-induced platelet aggregation and cyclic AMP-generation in human platelets. Thromb. Res. 86, 337-342.
247. 2alpha and platelet activation in diabetes mellitus. Circulation 99, 224-229.
248. Morrow, J. D., Minton, T. A., Mukundan, C. R., Campbell, M. D., Zackert, W. E., Daniel, V. C., et al. (1994) Free radical-induced generation of isoprostanes in vivo. J. Biol. Chem. 269, 4317-4326.
249. 2alpha on retinal circulation in diabetic and non-diabetic rats. Prostaglandins Leuko. Essent. Fatty Acids 59, 349-355.
250. Subbanagounder, G., Wong, J. W., Lee, H., Faull, K. F., Miller, E., Witztum, J. L., et al. (2002) Epoxyisoprostane and epoxycyclopentenone phospholipids regulate monocyte chemotactic protein-1 and interleukin-8 synthesis. Formation of these oxidized phospholipids in response to interleukin-1beta. J. Biol. Chem. 277, 7271-7281.
251. Salomon, R. G., Batyreva, E., Kaur, K., Sprecher, D. L., Schreiber, M. J., Crabb, J. W., et al. (2000) Isolevuglandin-protein adducts in humans: products of free radical-induced lipid oxidation through the isoprostane pathway. Biochim. Biophys. Acta 1485, 225-235.
252. 2, a product of the isoprostane pathway, in oxidized low density lipoprotein. J. Biol. Chem. 274, 20271-20280.
253. Roberts, L. J. I., Salomon, R. G., Morrow, J. D., and Brame, C. J. (1999) New developments in the isoprostane pathway: identification of novel highly reactive gamma-ketoaldehydes (isolevuglandins) and characterization of their protein adducts. FASEB J. 13, 1157-1168.
254. Brame, C. J., Salomon, R. G., Morrow, J. D., and Roberts, L. G. I. (1999) Identification of extremely reactive gamma-ketoaldehydes (isolevuglandins) as products of the isoprostane pathway and characterization of their lysyl protein adducts. J. Biol. Chem. 274, 13139-13146.
255. 2alpha, a novel index of lipid peroxidation in vivo, by immunoaffinity extraction/gas chromatography-mass spoectrometry. Basal levels in smokers and non-smokers. Free Radic. Biol. Med. 20, 619-624.
256. 2-isoprostanes) are formed in situ on phospholipids. Proc. Natl. Acad. Sci. USA 89, 10721-10725.
257. Patrono, C. and Fitzgerald, G. A. (1997) Isoprostanes: potential markers of oxidant stress in atherothrombotic disease. Arterioscler. Thromb. Vasc. Biol. 17, 2309-2315.
258. 2alpha is accumulated in coronary arteries isolated from patients with coronary heart disease. Cardiovasc. Res. 43, 492-499.
259. Kauffman, L. D., Sokol, R. J., Jones, R. H., Awad, J. A., Rewers, M. J., and Norris, J. M. (2003) Urinary F2-isoprostanes in young healthy children at risk for type 1 diabetes mellitus. Free Radic. Biol. Med. 35, 551-557.
260. 2alpha levels are elevated in individuals with non-insulin dependent diabetes mellitus. FEBS Lett. 368, 225-229.
261. Palmer, A. M., Thomas, C. R., Gopaul, N., Dhir, S., Anggard, E. E., Poston, L., et al. (1998) Dietary antioxidant supplementation reduces lipid peroxidation but impairs vascular function in small mesenteric arteries of the streptozotocin-diabetic rat. Diabetologia 41, 148-156.
262. Devaraj, S., Hirany, S. V., Burk, R. F., and Jialal, I. (2001) Divergence between LDL oxidative susceptibility and urinary F(2)-isoprostanes as measures of oxidative stress in type 2 diabetes. Clin. Chem. 47, 1974-1979.
263. Voutilainen, S., Morrow, J. D., Roberts, L. J. I., Alfthan, G., Alho, H., Nyyssonen, K., et al. (1999) Enhanced in vivo lipid peroxidation at elevated plasma total homocysteine levels. Arterioscler. Thromb. Vasc. Biol. 19, 1263-1266.
264. Refsum, H., Smith, A. D., Ueland, P. M., Nexo, E., Clarke, R., Mcpartlin, J., et al. (2004) Facts and recommendations about total homocysteine determinations: an expert opinion. Clin. Chem. 50, 3-32.
265. Suzuki, D. and Miyata, T. (1999) Carbonyl stress in the pathogenesis of diabetic nephropathy. Intern. Med. 38, 309-314.
266. Jain, A. K., Lim, G., Langford, M., and Jain, S. K. (2002) Effect of high-glucose levels on protein oxidation in cultured lens cells, and in crystalline and albumin solution and its inhibition by vitamin B(6) and N-acetylcysteine: its possible relevance to cataract formation in diabetes. Free Radic. Biol. Med. 33, 1615-1621.
267. Portero-Otin, M., Pamplona, R., Ruiz, M. C., Cabiscol, E., Prat, J., and Bellmunt, M. J. (1999) Diabetes induces an impairment in the proteolytic activity against oxidized proteins an a hetergeneous effect in nonenzymatic protein modifications in the cytosol of rat liver and kidney. Diabetes 48, 2215-2220.
268. Oh-Ishi, M., Ueno, T., and Maeda, T. (2003) Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-Evans Tokushima Fatty (OLETF) rat. Free Radic. Biol. Med. 34, 11-22.
269. Shringarpure, R. and Davies, K. J. A. (2002) Protein turnover by the proteasome in aging and disease. Free Radic. Biol. Med. 32, 1084-89.
270. Friguet, B., Szweda, L. I., and Stadtman, E. R. (1994) Susceptibility of glucose-6-phosphate dehydrogenase modified by 4-hydroxy-2-nonenal and metal-catalyzed oxidation to proteolysis by the multicatalytic protease. Arch. Biochem. Biophys. 311, 168-173.
271. Brownlee, M. (1995) Advanced protein glycosylation in diabetes and aging. Annu. Rev. Med. 46, 223-234.
272. Bolli, G., Compagnucci, P., Cartechini, M. G., Santeusanio, F., Cirotto, C., Scionti, L., et al. (1980) HbA1 in subjects with abnormal glucose tolerance but normal fasting plasma glucose. Diabetes 29, 272-277.
273. Sensi, M., Pricci, F., Andreani, D., and Di Mario, U. (1991) Advanced nonenzymatic glycation endproducts (AGE): their relevance to aging and the pathogenesis of late diabetic complications. Diabetes Res. 16, 1-9.
274. Bucala, R., Makita, Z., Koschinsky, T., Cerami, A., and Vlassara, H. (1993) Lipid advanced glycosylation: pathway for lipid oxidation in vivo. Proc. Natl. Acad. Sci. U. S. A. 90, 6434-6438.
275. Reddy, S., Bichler, J., Wells-Knecht, K. J., Thorpe, S. R., and Baynes, J. W. (1995) N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. Biochemistry 34, 10872-10878.
276. Singh, R., Barden, A., Mori, T., and Beilin, L. (2001) Advanced glycation end-products: a review. Diabetologia 44, 129-146.
277. Ghitescu, L. D., Gugliucci, A., and Dumas, F. (2001) Actin and annexins I and II are among the main endothelial plasmalemma-associated proteins forming early glucose adducts in experimental diabetes. Diabetes 50, 1666-1674.
278. Uchimura, T., Nakano, K., Hashiguchi, T., Iwamoto, H., Miura, K., Yoshimura, Y., et al. (2001) Elevation of N-(carboxymethyl)valine residue in hemoglobin of diabetic patients. Its role in the development of diabetic nephropathy. Diabetes Care 24, 891-896.
279. Wolffenbuttel, B. H., Giordano, D., Founds, H. W., and Bucala, R. (1996) Long-term assessment of glucose control by haemoglobin-AGE measurement. Lancet 347, 513-515.
280. Yan, H. and Harding, J. J. (1997) Glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase. Biochem. J. 328, 599-605.
281. Ando, K., Beppu, M., Kikugawa, K., Nagai, R., and Horiuchi, S. (1999) Membrane proteins of human erythrocytes are modified by advanced glycation end products during aging in the circulation. Biochem. Biophys. Res. Commun. 258, 123-127.
282. Gonzalez Flecha, F. L., Castello, P. R., Caride, A. J., Gagliardino, J. J., and Rossi, J. P. (1993) The erythrocyte calcium pump is inhibited by non-enzymic glycation: studies in situ and with the purified enzyme. Biochem. J. 29, 369-375.
283. Chellan, P. and Nagaraj, R. H. (2001) Early glycation products produce pentosidine cross-links on native proteins, novel mechanism of pentosidine formation and propagation of glycation. J. Biol. Chem. 276, 3895-3903.
284. Jain, S. K. and Palmer, M. (1997) The effect of oxygen radicals metabolites and vitamin E on glycosylation of proteins. Free Radic. Biol. Med. 22, 593-596.
285. Ortwerth, B. J., James, H., Simpson, G., and Linetsky, M. (1998) The generation of superoxide anions in glycation reactions with sugars, osones, and 3-deoxyosones. Biochem. Biophys. Res. Commun. 245, 161-165.
286. Akagawa, M., Sasaki, T., and Suyama, K. (2002) Oxidative deamination of lysine residue in plasma protein of diabetic rats. Novel mechanism via the Maillard reaction. Eur. J. Biochem. 269, 5451-5458.
287. Qian, M. and Eaton, J. W. (2000) Glycochelates and the etiology of diabetic peripheral neuropathy. Free Radic. Biol. Med. 28, 652-656.
288. Bulteau, A.-L., Verbeke, P., Petropoulos, I., Chaffotte, A.-F., and Frigue, B. (2001) Proteasome inhibition in glyoxal-treated fibroblasts an resistance of glycated glucose-6-phosphate dehydrogenase to 20 S proteasome degradation in vitro. J. Biol. Chem. 276, 45662-45668.
289. Ling, X., Nagai, R., Sakashita, N., Takeya, M., Horiuchi, S., and Takahashi, K. (2001) Immunohistochemical distribution and quantitative biochemical detection of advanced glycation end products in fetal to adult rats and in rats with streptozotocin-induced diabetes. Lab. Invest. 81, 845-861.
290. Candiloros, H., Muller, S., Ziegler, O., Donner, M., and Drouin, P. (1996) Role of albumin glycation on the erythrocyte aggregation: an in vitro study. Diabetes Med. 13, 646-650.
291. Niwa, T., Katsuzaki, T., Miyazaki, S., Miyazaki, T., Ishizaki, Y., Hayase, F., et al. (1997) Immunohistochemical detection of imidazolone, a novel advanced glycation end product, in kidneys and aortas of diabetic patients. J. Clin. Invest. 99, 1272-1280.
292. Booth, A. A., Khalifah, R. G., and Hudson, B. G. (1996) Thiamine pyrophosphate and pyridoxamine inhibit the formation of antigenic advanced glycation end-products: comparison with aminoguanidine. Biochem. Biophys. Res. Commun. 220, 113-119.
293. Metz, T. O., Alderson, N. L., Chachich, M. E., Thorpe, S. R., and Baynes, J. W. (2003) Pyridoxamine traps intermediates in lipid peroxidation reactions in vivo: evidence on the role of lipids in chemical modification of protein and development of diabetic complications. J. Biol. Chem. 278, 42012-42019.
294. Stitt, A., Gardiner, T. A., Anderson, N. L., Canning, P., Frizzell, N., Duffy, N., et al. (2002) The AGE inhibitor pyridoxamine inhibits development of retinopathy in experimental diabetes. Diabetes 51, 2826-2832.
295. Nagaraj, R. H., Sarkar, P., Mally, A., Biemel, K. M., Lederer, M. O., and Padayatti, P. S. (2002) Effect of pyridoxamine on chemical modification of proteins by carbonyls in diabetic rats: characterization of a major product from the reaction of pyridoxamine and methylglyoxal. Arch. Biochem. Biophys. 402, 110-119.
296. Voziyan, P. A., Metz, T. O., Baynes, J. W., and Hudson, B. G. (2002) A post-Amadori inhibitor pyridoxamine also inhibits chemical modification of proteins by scavenging carbonyl intermediates of carbohydrate and lipid degradation. J. Biol. Chem. 277, 3397-3403.
297. Giardino, I., Fard, A. K., Hatchell, D. L., and Brownlee, M. (1998) Aminoguanidine inhibits reactive oxygen species formation, lipid peroxidation, and oxidant-induced apoptosis. Diabetes 47, 1114-1120.
298. Ihm, S. H., Yoo, H. J., Park, S. W., and Ihm, J. (1999) Effect of aminoguanidine on lipid peroxidation in streptozotocin-induced diabetic rats. Metabolism 48, 1141-1145.
299. Jakus, V., Hrnciarova, M., Carsky, J., Krahulec, B., and Rietbrock, N. (1999) Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidant activity. Life Sci. 65, 1991-1993.
300. Kedziora-Kornatowska, K. Z., Luciak, M., Blaszczyk, J., and Pawlak, W. (1998) Effect of aminoguanidine on erythrocyte lipid peroxidation and activities of antioxidant enzymes in experimental diabetes. Clin. Chem. Lab. Med. 36, 771-775.
301. Ha, H. and Lee, H. B. (2000) Reactive oxygen species as glucose signaling molecules in mesangial cells cultured under high glucose. Kidney Int. Suppl. 77, S19-S25.
302. Salahudeen, A. K., Kanji, V., Reckelhoff, J. F., and Schmidt, A. M. (1997) Pathogenesis of diabetic nephropathy: a radical approach. Nephrol. Dial. Transplant. 12, 664-668.
303. Wautier, J. L., Wautier, M. P., Schmidt, A. M., Anderson, G. M., Hori, O., Zoukourian, C., Capron, L., Chappey, O., Yan, S. D., Brett, J., et al. (1994) Advanced glycation end products (AGEs) on the surface of diabetic erythrocytes bind to the vessel wall via a specific receptor inducing oxidant stress in the vasculature: a link between surface-associated AGEs and diabetic complications. Proc. Natl. Acad. Sci. USA 91, 7742-7746.
304. Schmidt, A. M., Hori, O., Brett, J., Yan, S. D., Wautier, J. L., and Stern, D. (1994) Cellular receptors for advanced glycation end products. Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions. Arterioscler. Thromb. 14, 1521-1528.
305. Assero, G., Lupo, G., Anfuso, C. D., Ragusa, N., and Alberghina, M. (2001) High glucose and advanced glycation end products induce phospholipid hydrolysis and phospholipid enzyme inhibition in bovine retinal pericytes. Biochim. Biophys. Acta 1533, 128-140.
306. Wautier, M. P., Chappey, O., Corda, S., Stern, D. M., Schmidt, A. M., and Wautier, J. L. (2001) Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE. Am. J. Physiol. Endocrinol. Metab. 280, E685-E6894.
307. Yan, S. D., Schmidt, A. M., Anderson, G. M., Zhang, J., Brett, J., Zou, Y. S., et al. (1994) Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. J. Biol. Chem. 269, 9889-9897.
308. Schmidt, A. M., Yan, S. D., Tan, S. F., and Stern, D. M. (2000) The biology of the receptor for advanced glycation end products and its ligands. Biochim. Biophys. Acta 1498, 99-111.
309. Bierhaus, A., Chevion, S., Chevion, M., Hofmann, M., Quehenberger, P., Illmer, T., et al. (1997) Advanced glycation end product-induced activation of NF-kappaB is suppressed by alpha-lipoic acid in cultured endothelial cells. Diabetes 46, 1481-1490.
310. Valencia, J. V., Mone, M., Zhang, J., Weetall, M., Buxton, F. P., and Hughes, T. E. (2004) Divergent pathways of gene expression are activated by the RAGE ligands S100b and AGE-BSA. Diabetes 53, 743-751.
311. Park, L., Raman, K. G., Lee, K. J., Lu, Y., Ferran, L. J., Jr., Chow, W. S., et al. (1998) Suppression of accelerated diabetic atherosclerosis by the soluble receptor for advanced glycation end-products. Nat. Med. 4, 1025-1031.
312. Ramstrom, S., Ranby, M., and Lindahl, T. L. (2003) Platelet phosphatidylserine exposure and procoagulant activity in clotting whole blood - different effects of collagen, TRAP and calcium ionophore A23187. Thromb. Haemost. 89, 132-141.
313. Schlegel, R. A., Prendergast, T. W., and Williamson, P. (1985) Membrane phospholipid asymmetry as a factor in erythrocyte-endothelial cell interactions. J. Cell. Physiol. 123, 215-218.
314. Manodori, A. B., Barabino, G. A., Lubin, B. H., and Kuypers, F. A. (2000) Adherence of phosphatidylserine-exposing erythrocytes to endothelial matrix thrombospondin. Blood 95, 1293-1300.
315. Fadok, V. A., Bratton, D. L., Rose, D. M., Pearson, A., Ezekewitz, R. A., and Henson, P. M. (2000) A receptor for phosphatidylserine-specific clearance of apoptotic cells. Nature 405, 85-90.
316. Wali, R. K., Jaffe, S., Kumar, D., and Kalra, V. K. (1988) Alterations in organization of phospholipids in erythrocytes as factor in adherence to endothelial cells in diabetes mellitus. Diabetes 37, 104-111.
317. Wilson, M. J., Richter-Lowney, K., and Daleke, D. L. (1993) Hyperglycemia induces a loss of phospholipid asymmetry in human erythrocytes. Biochemistry 32, 11302-11310.
318. Wautier, J. L., Paton, R. C., Wautier, M. P., Pintigny, D., Abadie, E., Passa, P., et al. (1981) Increased adhesion of erythrocytes to endothelial cells in diabetes mellitus and its relation to vascular complications. N. Engl. J. Med. 305, 237-242.
319. Ceriello, A., Giacomello, R., Stel, G., Motz, E., Taboga, C., Tonutti, L., et al. (1995) Hyperglycemia-induced thrombin formation in diabetes. The possible role of oxidative stress. Diabetes 44, 924-928.
320. Tyurina, Y. Y., Serinkan, F. B., Tyurin, V. A., Kini, V., Yalowich, J. C., Schroit, A. J., et al. (2004) Lipid antioxidant, etoposide, inhibits phosphatidylserine externalization and macrophage clearance of apoptotic cells by preventing phosphatidylserine oxidation. J. Biol. Chem. 279, 6056-6064.
321. Weinstein, E. A., Li, H., Lawson, J. A., Rokach, J., Fitzgerald, G. A., and Axelsen, P. H. (2000) Prothrombinase acceleration by oxidatively damaged phospholipids. J. Biol. Chem. 275, 22925-22930.
322. Balasubramanian, K., Bevers, E. M., Willems, G. M., and Schroit, A. J. (2001) Binding of annexin V to membrane products of lipid peroxidation. Biochemistry 40, 8672-8676.
323. Middlekoop, E., Van Der Hoek, E. E., Bevers, E. M., Comfurius, P., Slotboom, A. J., Op Den Kamp, J. A., et al. (1989) Involvement of ATP-dependent aminophospholipid translocation in maintaining phospholipid asymmetry in diamide-treated human erythrocytes. Biochim. Biophys. Acta 981, 151-160.
324. Kamp, D., Sieberg, T., and Haest, C. W. (2001) Inhibition and stimulation of phospholipid scrambling activity. Consequences for lipid asymmetry, echinocytosis, and microvesiculation of erythrocytes. Biochemistry 40, 9438-9446.
325. Newton, A. C. (1995) Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270, 28495-28498.
326. Newton, A. C. (1996) Protein kinase C: ports of anchor in the cell. Curr. Biol. 6, 806-809.
327. Koya, D. and King, G. L. (1998) Protein kinase C activation and the development of diabetic complications. Diabetes 47, 859-866.
328. Lynch, J. J., Ferro, T. J., Blumenstock, F. A., Brockenauer, A. M., and Malik, A. B. (1990) Increased endothelial albumin permeability mediated by protein kinase C activation. J. Clin. Invest. 85, 1991-1998.
329. Rasmussen, H., Forder, J., Kojima, I., and Scriabine, A. (1984) TPA-induced contraction of isolated rabbit vascular smooth muscle. Biochem. Biophys. Res. Commun. 122, 776-784.
330. Inoguchi, T., Battan, R., Handler, E., Sportsman, J. R., Heath, W., and King, G. L. (1992) Preferential elevation of protein kinase C isoform beta II and diacylglycerol levels in the aorta and heart of diabetic rats: differential reversibility to glycemic control by islet cell transplantation. Proc. Natl. Acad. Sci. USA 89, 11059-11063.
331. Abiko, T., Abiko, A., Clermont, A. C., Shoelson, B., Horio, N., Takahashi, J., et al. (2003) Characterization of retinal leukostasis and hemodynamics in insulin resistance and diabetes: role of oxidants and protein kinase-C activation. Diabetes 52, 829-837.
332. Venugopal, S. K., Devaraj, S., Yang, T., and Jialal, I. (2002) α-Tocopherol decreases superoxide anion release in human monocytes under hyperglycemic conditions via inhibition of protein kinase C-alpha. Diabetes 51, 3049-3054.
333. Craven, P. A., Davidson, C. M., and Derubertis, F. R. (1990) Increase in diacylglycerol mass in isolated glomeruli by glucose from de novo synthesis of glycerolipids. Diabetes 39, 667-674.
334. Craven, P. A. and Derubertis, F. R. (1989) Protein kinase C is activated in glomeruli from streptozotocin diabetic rats. Possible mediation by glucose. J. Clin. Invest. 83, 1667-1675.
335. Koya, D., Lee, I. K., Ishii, H., Kanoh, H., and King, G. L. (1997) Prevention of glomerular dysfunction in diabetic rats by treatment with d-alpha-tocopherol. J. Am. Soc. Nephrol.. 8, 426-435.
336. Kunisaki, M., Bursell, S. E., Clermont, A. C., Ishii, H., Ballas, L. M., Jirousek, M. R., et al. (1995) Vitamin E prevents diabetes-induced abnormal retinal blood flow via the diacylglycerol-protein kinase C pathway. Am. J. Physiol. 269, E239-E246.
337. Shiba, T., Inoguchi, T., Sportsman, J. R., Heath, W. F., Bursell, S., and King, G. L. (1993) Correlation of diacylglycerol level and protein kinase C activity in rat retina to retinal circulation. Am. J. Physiol. 265, E783-E793.
338. Ishii, H., Jirousek, M. R., Koya, D., Takagi, C., Xia, P., Clermont, A., et al. (1996) Amelioration of vascular dysfunctions in diabetic rats by an oral PKC beta inhibitor. Science 272, 728-731.
339. Igarashi, M., Wakasaki, H., Takahara, N., Ishii, H., Jiang, Z. Y., Yamauchi, T., et al. (1999) Glucose or diabetes activates p38 mitogen-activated protein kinase via different pathways. J. Clin. Invest. 103, 185-195.
340. Pricci, F., Leto, G., Amadio, L., Iacobini, C., Cordone, S., Catalano, S., et al. (2003) Oxidative stress in diabetes-induced endothelial dysfunction involvement of nitric oxide and protein kinase C. Free Radic. Biol. Med. 35, 683-694.
341. Morigi, M., Angioletti, S., Imberti, B., Donadelli, R., Micheletti, G., Figliuzzi, M., et al. (1998) Leukocyte-endothelial interaction is augmented by high glucose concentrations and hyperglycemia in a NF-kB-dependent fashion. J. Clin. Invest. 101, 1905-1915.
342. Lenardo, M. J. and Baltimore, D. (1989) NF-kappa B: a pleiotropic mediator of inducible and tissue-specific gene control. Cell 58, 227-229.
343. Beyaert, R. (2003) Nuclear Factor kB: Regulation and Role in Disease. Kluwer Academic Publishers, Dordrecht.
344. Evans, J. L., Goldfine, I. D., Maddux, B. A., and Grodsky, G. M. (2002) Oxidative stress and stress-activated signaling pathways: a unifying hypothesis of type 2 diabetes. Endocr. Rev. 23, 599-622.
345. Pieper, G. M. and Riaz UI, H. (1997) Activation of nuclear factor-kappaB in cultured endothelial cells by increased glucose concentration: prevention by calphostin C. J. Cardiovasc. Pharmacol. 30, 528-532.
346. Du, X., Stocklauser-Farber, K., and Rosen, P. (1999) Generation of reactive oxygen intermediates, activation of NF-kappaB, and induction of apoptosis in human endothelial cells by glucose: role of nitric oxide synthase? Free Radic. Biol. Med. 27, 752-763.
347. Brand, K., Page, S., Rogler, G., Bartsch, A., Brandi, R., Knuechel, R., et al. (1996) Activated transcription factor nuclear factor-kappa B is present in the atherosclerotic lesion. J. Clin. Invest. 97, 1715-1722.
348. Chen, Z., Gibson, T. B., Robinson, F., Silvestro, L., Pearson, G., Xu, B., et al. (2001) MAP kinases. Chem. Rev. 101, 2449-2476.
349. Davis, R. J. (2000) Signal transduction by the JNK group of MAP kinases. Cell 103, 239-252.
350. Minden, A. and Karin, M. (1997) Regulation and function of the JNK subgroup of MAP kinases. Biochim. Biophys. Acta 1333, F85-F104.
351. Nebreda, A. R. and Porras, A. (2000) p38 MAP kinases: beyond the stress response. Trends Biochem. Sci. 25, 257-260.
352. Kumar, S., Boehm, J., and Lee, J. C. (2003) p38 MAP kinases: key signalling molecules as therapeutic targets for inflammatory diseases. Nat. Rev. Drug Discov. 2, 717-726.
353. Fujita, H., Omori, S., Ishikura, K., Hida, M., and Awazu, M. (2004) ERK and p38 mediate high-glucose-induced hypertrophy and TGF-beta expression in renal tubular cells. Am. J. Physiol. Renal Physiol. 286, F120-F126.
354. Liu, B. F., Miyata, S., Hirota, Y., Higo, S., Miyazaki, H., Fukunaga, M., et al. (2003) Methylglyoxal induces apoptosis through activation of p38 mitogen-activated protein kinase in rat mesangial cells. Kidney Int. 63, 947-957.
355. Price, S. A., Agthong, S., Middlemas, A. B., and Tomlinson, D. R. (2004) Mitogen-activated protein kinase p38 mediates reduced nerve conduction velocity in experimental diabetic neuropathy: interactions with aldose reductase. Diabetes 53, 1851-1856.
356. Koistinen, H. A., Chibalin, A. V., and Zierath, J. R. (2003) Aberrant p38 mitogen-activated protein kinase signalling in skeletal muscle from type 2 diabetic patients. Diabetologia 46, 1324-1328.
357. Carlson, C. J., Koterski, S., Sciotti, R. J., Poccard, G. B., and Rondinone, C. M. (2003) Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: potential role of p38 in the downregulation of GLUT4 expression. Diabetes 52, 634-641.
358. Coulon, L., Calzada, C., Moulin, P., Vericel, E., and Lagarde, M. (2003) Activation of p38 mitogen-activated protein kinase/cytosolic phospholipase A2 cascade in hydroperoxide-stressed platelets. Free Radic. Biol. Med. 35, 616-625.
359. Gum, R. J., Gaede, L. L., Heindel, M. A., Waring, J. F., Trevillyan, J. M., Zinker, B. A., et al. (2003) Antisense protein tyrosine phosphatase 1B reverses activation of p38 mitogen-activated protein kinase in liver of ob/ob mice. Mol. Endocrinol. 17, 1131-1143.
360. Agthong, S. and Tomlinson, D. R. (2002) Inhibition of p38 MAP kinase corrects biochemical and neurological deficits in experimental diabetic neuropathy. Ann. N. Y. Acad. Sci. 973, 359-362.
361. Hirosumi, J., Tuncman, G., Chang, L., Gorgun, C. Z., Uysal, K. T., Maeda, K., et al. (2002) A central role for JNK in obesity and insulin resistance. Nature 420, 333-336.
362. Li, M., Mossman, B. T., Kolpa, E., Timblin, C. R., Shukla, A., Taatjes, D. J., et al. (2003) Age-related differences in MAP kinase activity in VSMC in response to glucose or TNF-alpha. J. Cell. Physiol. 197, 418-425.
363. Green, D. R. (1998) Apoptotic pathways: the roads to ruin. Cell 94, 695-698.
364. Cohen, G. M. (1997) Caspases: the executioners of apoptosis. Biochem. J. 326, 1-16.
365. Nagata, S. (1997) Apoptosis by death factor. Cell 88, 355-365.
366. Thornberry, N. A. and Lazebnik, Y. (1998) Caspases: enemies within. Science 281, 1312-1316.
367. Vincent, A. M., Brownlee, M., and Russell, J. W. (2002) Oxidative stress and programmed cell death in diabetic neuropathy. Ann. N. Y. Acad. Sci. 959, 368-383.
368. Greene, D. A., Stevens, M. J., Obrosova, I., and Feldman, E. L. (1999) Glucose-induced oxidative stress and programmed cell death in diabetic neuropathy. Eur. J. Pharmacol. 375, 217-223.
369. Sima, A. A. (2003) New insights into the metabolic and molecular basis for diabetic neuropathy. Cell. Mol. Life Sci. 60, 2445-2464.
370. Cai, L., Li, W., Wang, G., Guo, L., Jiang, Y., and Kang, Y. J. (2002) Hyperglycemia-induced apoptosis in mouse myocardium: mitochondrial cytochrome C-mediated caspase-3 activation pathway. Diabetes 51, 1938-1948.
371. Srinivasan, S., Stevens, M., and Wiley, J. W. (2000) Diabetic peripheral neuropathy: evidence for apoptosis and associated mitochondrial dysfunction. Diabetes 49, 1932-1938.
372. Cheng, C. and Zochodne, D. W. (2003) Sensory neurons with activated caspase-3 survive long-term experimental diabetes. Diabetes 52, 2363-2371.
373. Ido, Y., Carling, D., and Ruderman, N. (2002) Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: inhibition by the AMP-activated protein kinase activation. Diabetes 51, 159-167.
374. Russell, J. W., Sullivan, K. A., Windebank, A. J., Herrmann, D. N., and Feldman, E. L. (1999) Neurons undergo apoptosis in animal and cell culture models of diabetes. Neurobiol. Dis. 6, 347-363.
375. Schmeichel, A. M., Schmelzer, J. D., and Low, P. A. (2003) Oxidative injury and apoptosis of dorsal root ganglion neurons in chronic experimental diabetic neuropathy. Diabetes 52, 165-171.
376. Wu, Q. D., Wang, J. H., Fennessy, F., Redmond, H. P., and Bouchier-Hayes, D. (1999) Taurine prevents high-glucose-induced human vascular endothelial cell apoptosis. Am. J. Physiol. 277, C1229-C1238.
377. Dubois, R. N., Abramson, S. B., Crofford, L., Gupta, R. A., Simon, L. S., Van De Putte, L. B., et al. (1998) Cyclooxygenase in biology and disease. FASEB J. 12, 1063-1073.
378. Feng, L., Xia, Y., Garcia, G. E., Hwang, D., and Wilson, C. B. (1995) Involvement of reactive oxygen intermediates in cyclooxygenase-2 expression induced by interleukin-1, tumor necrosis factor-alpha, and lipopolysaccharide. J. Clin. Invest. 95, 1669-1675.
379. Pop-Busui, R., Marinescu, V., Van Huysen, C., Li, F., Sullivan, K., Greene, D. A., et al. (2002) Dissection of metabolic, vascular, and nerve conduction interrelationships in experimental diabetic neuropathy by cyclooxygenase inhibition and acetyl-L-carnitine administration. Diabetes 51, 2619-2628.
380. Quilley, J. and Chen, Y. J. (2003) Role of COX-2 in the enhanced vasoconstrictor effect of arachidonic acid in the diabetic rat kidney. Hypertension 42, 837-843.
381. Nasrallah, R., Landry, A., Singh, S., Sklepowicz, M., and Hebert, R. L. (2003) Increased expression of cyclooxygenase-1 and -2 in the diabetic rat renal medulla. Am. J. Physiol. Renal Physiol. 285, F1068-F1077.
382. Shanmugam, N., Gaw Gonzalo, I. T., and Natarajan, R. (2004) Molecular mechanisms of high glucose-induced cyclooxygenase-2 expression in monocytes. Diabetes 53, 795-802.
383. Kiritoshi, S., Nishikawa, T., Sonoda, K., Kukidome, D., Senokuchi, T., Matsuo, T., et al. (2003) Reactive oxygen species from mitochondria induce cyclooxygenase-2 gene expression in human mesangial cells: potential role in diabetic nephropathy. Diabetes 52, 2570-2577.
384. Cipollone, F., Iezzi, A., Fazia, M., Zucchelli, M., Pini, B., Cuccurullo, C., et al. (2003) The receptor RAGE as a progression factor amplifying arachidonate-dependent inflammatory and proteolytic response in human atherosclerotic plaques: role of glycemic control. Circulation 108, 1070-1077.
385. Sennlaub, F., Valamanesh, F., Vazquez-Tello, A., El-Asrar, A. M., Checchin, D., Brault, S., et al. (2003) Cyclooxygenase-2 in human and experimental ischemic proliferative retinopathy. Circulation 108, 198-204.