High levels of antioxidant enzymatic defence assure good protection against hypoxic stress in spontaneously diabetic rats

International Journal of Biochemistry and Cell Biology

Volumn 38, Issue 12, 2006, Pages 2196-2208

  Bonfigli, A ^a   Colafarina, S ^a   Falone, S ^a   Di Giulio, C ^b   Di Ilio, C ^b   Amicarelli, F ^a  

^a UNIVERSITY OF L'AQUILA   (Italy)

^b UNIVERSITY OF CHIETI   (Italy)

Author keywords

Antioxidant enzymes; BB rats; Diabetes; Hypoxia; NF B

Indexed keywords

ANTIOXIDANT; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; HYDROXYACYLGLUTATHIONE HYDROLASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LACTOYLGLUTATHIONE LYASE; PROTEIN P53;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; EXPERIMENTAL DIABETES MELLITUS; HYPOTHESIS; HYPOXIA; MALE; NONHUMAN; RAT; RAT STRAIN; STIMULATION; STRESS;

ANIMALS; ANTIOXIDANTS; CASPASE 3; CATALASE; CELL HYPOXIA; DIABETES MELLITUS; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; LACTOYLGLUTATHIONE LYASE; LIVER; LUNG; NF-KAPPA B; RATS; RATS, WISTAR; SUPEROXIDE DISMUTASE; THIOLESTER HYDROLASES; TUMOR SUPPRESSOR PROTEIN P53;

RATTUS NORVEGICUS;

EID: 33748714719     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2006.06.011     Document Type: Article

References (66)

1. Aebi H.E. Catalase. In: Bergmeyer H.U. (Ed). Methods in enzymatic analysis (1974), Academic Press, New York 673-684
2. Amicarelli F., Di Ilio C., Masciocco L., Bonfigli A., Zarivi O., D'Andrea M.R., et al. Aging and detoxifying enzymes responses to hypoxic and hyperoxic treatment. Mech. Ageing Dev. 97 (1997) 215-226
3. Abou-Seif M.A., and Youssef A.A. Evaluation of some biochemical changes in diabetic patients. Clin. Chim. Acta 346 2 (2004) 161-170
4. Arrigo A.P. Gene expression and the thiol redox state. Free Radic. Biol. Med. 27 9-10 (1999) 936-944
5. Baynes J.W. Role of oxidative stress in development of complications in diabetes. Diabetes 40 (1991) 405-412
6. Bekris L.M., Kavanagh T.J., and Lernmark A. Targeting type 1 diabetes before and at the clinical onset of disease. Endocr. Metab. Immune Disord. Drug Targets 6 1 (2006) 103-124
7. Berlanga J., Cibrian D., Guillen I., Freyre F., Alba J.S., Lopez-Saura P., et al. Methylglyoxal administration induces diabetes-like microvascular changes and perturbs the healing process of cutaneous wounds. Clin. Sci. 109 1 (2005) 83-95
8. Bhardwaj S.K., Sharma P., and Kaur G. Alterations in free radical scavenger profile of type I diabetic rat brain. Mol. Chem. Neuropathol. 35 (1999) 187-201
9. Bianciardi P., Fantacci M., Caretti A., Ronchi R., Milano G., Morel S., et al. Chronic in vivo hypoxia in various organs: hypoxia-inducible factor-1alpha and apoptosis. Biochem. Biophys. Res. Commun. 342 3 (2006) 875-880
10. Boirie Y. Insulin regulation of mitochondrial proteins and oxidative phosphorylation in human muscle. Trends Endocrinol. Metab. 14 9 (2003) 393-394
11. Bonnefont-Rousselot D. Glucose and reactive oxygen species. Curr. Opin. Clin. Nutr. Metab. Care 5 5 (2002) 561-568
12. Bourajjaj M., Stehouwer C.D., van Hinsbergh V.W., and Schalkwijk C.G. Role of methylglyoxal adducts in the development of vascular complications in diabetes mellitus. Biochem. Soc. Trans. 31 (2003) 1400-1402
13. Ceriello A. Acute hyperglycaemia and oxidative stress generation. Diabet. Med. 14 Suppl. 3 (1997) S45-S49
14. Chung S.S., Ho E.C., Lam K.S., and Chung S.K. Contribution of polyol pathway to diabetes-induced oxidative stress. J. Am. Soc. Nephrol. 14 8 Suppl. 3 (2003) S233-S236
15. Cojocaru I.M., Cojocaru M., Musuroi C., Botezat M., Lazar L., and Druta A. Lipid peroxidation and catalase in diabetes mellitus with and without ischemic stroke. Rom. J. Intern. Med. 42 2 (2004) 423-429
16. Dandona P., Aljada A., and Bandyopadhyay A. Inflammation: the link between insulin resistance, obesity and diabetes. Trends Immunol. 25 1 (2004) 4-7
17. Demaine A.G. Polymorphisms of the aldose reductase gene and susceptibility to diabetic microvascular complications. Curr. Med. Chem. 10 15 (2003) 1389-1398
18. Di Ilio C., Polidoro G., Arduini A., Muccini A., and Federici G. Glutathione peroxidase, glutathione reductase, glutathione transferase and γ-glutamyl-transpeptidase activities in human early pregnancy placenta. Biochem. Med. 29 (1983) 143-148
19. Di Ilio C., Sacchetta P., Lo Bello M., Caccuri A.M., and Federici G. Selenium independent glutathione peroxidase activity associated with cationic forms of glutathione transferase in human heart. J. Mol. Cell. Cardiol. 18 (1986) 983-991
20. Follak N., Kloting L., Wolf E., and Merk H. Delayed remodeling in the early period of fracture healing in spontaneously diabetic BB/OK rats depending on the diabetic metabolic state. Histol. Histopathol. 19 2 (2004) 473-486
21. Gil-Del Valle L., de la C Milian L., Toledo A., Vilaro N., Tapanes R., and Otero M.A. Altered redox status in patients with diabetes mellitus type I. Pharmacol. Res. 5 4 (2005) 375-380
22. Gomez-Lazaro M., Fernandez-Gomez F.J., and Jordan J. p53: twenty-five years understanding the mechanism of genome protection. J. Physiol. Biochem. 60 4 (2004) 287-307
23. Gugliucci A. Glycation as the glucose link to diabetic complications. J. Am. Osteopath. Assoc. 100 10 (2000) 621-634
24. Guha M.K., Vander Jagt D.L., and Creighton D.J. Diffusion-dependent rates for the hydrolysis reaction catalyzed by glyoxalase II from rat erythrocytes. Biochemistry 27 24 (1988) 8818-8822
25. Habig W.H., and Jakoby W.B. Assay for differentiation of glutathione S-transferases. Meth. Enzymol. 77 (1981) 398-405
26. Haddad J.J. Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors. Cell. Signal. 14 (2002) 879-897
27. Hayes J.D., and Strange R.C. Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress. Free Radic. Res. 22 3 (1995) 193-207
28. Hayes J.D., Flanagan J.U., and Jowsey I.R. Glutathione transferases. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 51-88
29. Ho E., and Bray T.M. Antioxidants, NFkappaB activation, and diabetogenesis. Proc. Soc. Exp. Biol. Med. 222 3 (1999) 205-213
30. Ho E., Quan N., Tsai Y.H., Lai W., and Bray T.M. Dietary zinc supplementation inhibits NFkappaB activation and protects against chemically induced diabetes in CD1 mice. Exp. Biol. Med. (Maywood) 226 2 (2001) 103-111
31. Hotamisligil G.S. Inflammatory pathways and insulin action. Int. J. Obes. Relat. Metab. Disord. 27 Suppl. 3 (2003) S53-S55
32. Hunt J.V., and Wolff S.P. Oxidative glycation and free radical production: a casual mechanism of diabetic complications. Free Radic. Res. Commun. 12-13 Pt (1991) 115-123
33. Hunt J.V., Smith C.C., and Wolff S.P. Autoxidative glycosilation and possible involvement of peroxides and free radicals in LDL modification by glucose. Diabetes 39 11 (1990) 1420-1424
34. Ip S.P., Chan Y.W., Che C.T., and Leung P.S. Effect of chronic hypoxia on glutathione status and membrane integrity in the pancreas. Pancreatology 2 1 (2002) 34-39
35. Ip S.P., Chan Y.W., and Leung P.S. Effects of chronic hypoxia on the circulating and pancreatic renin-angiotensin system. Pancreas 25 3 (2002) 296-300
36. Janssen-Heininger Y.M., Poynter M.E., and Baeuerle P.A. Recent advances towards understanding redox mechanisms in the activation of nuclear factor kappaB. Free Radic. Biol. Med. 28 9 (2000) 1317-1327
37. Jones D.P. The role of oxygen concentration in oxidative stress: hypoxic and hyperoxic models. In: Sies H. (Ed). Oxidative stress (1985), Academic Press, London 151-195
38. Kaneto H., Fujii J., Myint T., Miyazawa N., Islam K.N., Kawasaki Y., et al. Reducing sugar trigger oxidative modification and apoptosis in pancreatic β-cells by provoking oxidative stress through the glycation reaction. Biochem. J. 320 Pt 3 (1996) 855-863
39. Karachalias N., Babaei-Jadidi R., Ahmed N., and Thornalley P.J. Accumulation of fructosyl-lysine and advanced glycation end product in the kidney, retina and peripheral nerve of streptozotocin-induced diabetic rats. Biochem. Soc. Trans. 31 Pt 6 (2003) 1423-1425
40. Kowluru R.A., Koppolu P., Chakrabarti S., and Chen S. Diabetes-induced activation of nuclear transcription factor in the retina, and its inhibition by antioxidants. Free Radic. Res. 37 11 (2003) 1169-1180
41. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277 5259 (1970) 680-685
42. Lamhamedi-Cherradi S.E., Zheng S., Hilliard B.A., Xu L., Sun J., Alsheadat S., et al. Transcriptional regulation of type I diabetes by NF-kappa B. J. Immunol. 171 9 (2003) 4886-4892
43. Leung P.S., and Carlsson P.O. Pancreatic islet rennin angiotensin system: its novel roles in islet function and in diabetes mellitus. Pancreas 30 4 (2005) 293-298
44. Maechler P. Novel regulation of insulin secretion: the role of mitichondria. Curr. Opin. Invest. Drugs 4 10 (2003) 1166-1172
45. Mannervik B., Aronsson A.C., Marmstal E., and Tibbelin G. Glyoxalase I (rat liver). Meth. Enzymol. 77 (1981) 297-301
46. McLellan A.C., Thornalley P.J., Benn J., and Sonksen P.H. Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. (Lond) 87 1 (1994) 21-29
47. Messier C., Awad N., and Gagnon M. The relationships between atherosclerosis, heart disease, type 2 diabetes and dementia. Neurol. Res. 26 5 (2004) 567-572
48. Morel S., Milano G., Ludunge K.M., Corno A.F., Samaja M., Fleury S., et al. Brief reoxygenation episodes during chronic hypoxia enhance posthypoxic recovery of LV function: role of mitogen-activated protein kinase signalling pathways. Basic Res. Cardiol. 101 4 (2006) 336-345
49. Oberley L.W. Free radicals and diabetes. Free Radic. Biol. Med. 5 2 (1988) 113-124
50. Paglia D.E., and Valentine W.N. Studies on the qualitative and quantitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med. 70 1 (1967) 158-169
51. Piconi L., Quagliaro L., and Ceriello A. Oxidative stress in diabetes. Clin. Chem. Lab. Med. 41 9 (2003) 1144-1149
52. Ratliff D.M., Vander Jagt D.J., Eaton R.P., and Vander Jagt D.L. Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II-a clinical research center study. J. Clin. Endocrinol. Metab. 81 2 (1996) 488-492
53. Robertson R.P. Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes. J. Biol. Chem. 279 41 (2004) 42351-42354
54. Santra D., Sawhney H., Aggarwal N., Majumdar S., and Vasishta K. Lipid peroxidation and Vitamin E status in gestational diabetes mellitus. J. Obstet. Gynaecol. Res. 29 5 (2003) 300-304
55. Schenker N., and Gentleman J.F. On judging the significance of differences by examining the overlap between confidence intervals. Am. Stat. 55 (2001) 182-186
56. Schoenhagen P., and Nissen S.E. Coronary atherosclerosis in diabetic subjects: clinical significance, anatomic characteristics, and identification with in vivo imaging. Cardiol. Clin. 22 4 (2004) 527-540
57. Schrauwen P., and Hesselink M.K. Oxidative capacity, lipotoxicity, and mitochondrial damage in type 2 diabetes. Diabetes 53 6 (2004) 1412-1417
58. Shibuya T., Watanabe Y., Nalley K.A., Fusco A., and Salafsky B. The BCA protein determination system: an analysis of several buffers, incubation temperature and protein standards. Tokyo Ika Daigaku Zasshi 47 4 (1989) 677-682
59. Slatter D.A., Bolton C.H., and Bailey A.J. The importance of lipid-derived malondialdehyde in diabetes mellitus. Diabetologia 43 5 (2000) 550-557
60. Somani S.M., Husain K., and Schlorff E.C. Response of antioxidant system to physical and chemical stress. In: Baskin S.I., and Salem H. (Eds). Oxidants, antioxidants and free radicals (1996), Taylor & Francis, Washington, DC 125-141
61. Stitt A.W., Jenkins A.J., and Cooper M.E. Advanced glycation end products and diabetic complications. Expert Opin. Investig. Drugs 11 9 (2002) 1205-1223
62. Sun M., and Zigman S. An improved spectrophotometric assay for superoxide dismutase based on epinephrine autoxidation. Anal. Biochem. 90 1 (1978) 81-89
63. Thornalley P.J. The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269 1 (1990) 1-11
64. Thornalley P.J. Glycation in diabetic neuropathy: characteristics, consequences, causes and therapeutic options. Int. Rev. Neurobiol. 50 (2002) 37-57
65. Towbin H., Staehelin T., and Gordon L. Electrophoretic transfer of proteins from gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76 9 (1979) 4350-4354
66. Wiernsperger N.F. Oxidative stress: the special case of diabetes. Biofactors 19 1-2 (2003) 11-18