Alterations in tissue glutathione antioxidant system in streptozotocin-induced diabetic rats

Molecular and Cellular Biochemistry

Volumn 162, Issue 2, 1996, Pages 153-158

  Mak, Duncan H F ^a   Ip, Siu Po ^a   Li, Pui Chun ^a   Poon, Michel K T ^a   Ko, Kam Ming ^a  

^a HONG KONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Hong Kong)

Author keywords

Glutathione; Glutathione antioxidant enzymes; Oxidative stress; Streptozotocin diabetes

Indexed keywords

ANTIOXIDANT; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; INSULIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; HEART; KIDNEY; LIVER LEVEL; MALE; NONHUMAN; OXIDATIVE STRESS; RAT; STREPTOZOCIN DIABETES;

ANIMALIA;

EID: 0029831258     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00227543     Document Type: Article

References (17)

1. Tomlinson DR, Willars GB, Carrington HL: Aldose reductase inhibitor and diabetic complications. Pharmacol Ther 54: 151-194, 1992
2. Frank RN: On the pathogenesis of diabetic retinopathy. A 1990 update. Ophthalmology 98: 586-593, 1991
3. Osterby R: Glomerular structural changes in type I (insulin-dependent) diabetes mellitus: causes, consequences, and prevention. Diabetologia 35: 803-812, 1992
4. Wolff SP, Dean RT: Glucose auto-oxidation and protein modification. Thepotential role of 'autoxidative glycosylation' in diabetes. Biochem J 245: 243-250, 1987
5. Brownlee M, Vlassara H, Cerami A: Nonenzymatic glycosylation and pathogenesis of diabetic complications. Ann Intern Med 101: 527-537, 1984
6. Gillery P, Monboisse JC, Maquart FX, Borel JP: Glycation of proteins as a source of superoxide. Diabetes Metabol 14: 25-30, 1988
7. Meister A, Anderson ME: Glutathione. Ann Rev Biochem 52: 711-760, 1983
8. Meister A: Glutathione metabolism and its selective modification. J Biol Chem 263: 17205-17208, 1988
9. Anderson ME: Enzymatic and chemical methods for the determination of glutathione. In: D. Dolphin, R. Poulson and O Avramovic (eds). Glutathione: Chemical, Biochemical, and Medical Aspects, Part A. John Wiley & Sons, London, New York, 1989, pp 339- 365
10. Seelig GF, Meister A: Glutathione biosynthesis: γ-glutamylcysteine synthetase from rat kidney. Meth Enzymol 113: 379-390, 1985
11. Warholm M, Gutenberg C, Von Bahr C, Mannervik B: Glutathione transferases from human liver. Meth Enzymol 113: 499-504, 1985
12. Godin DV, Garnett M: Species-related variations in tissue antioxidant status -1. Differences in antioxidant enzyme profiles. Comp Biochem Physiol 103b: 737-742, 1992
13. Monnier VM, Vishwanath V, Frank KE, Elmets GA, Dauchot P, Kohn RR: Relation between complications of type I diabetes mellitus and collagen-linked fluorescence. N Eng J Med 317: 403-408, 1986
14. Woessner JF Jr: Determination of hydroxyproline in connective tissues. In: D.A. Hall (ed). The Methodology of Connective Tissue Research. Joynson-Bruvvers, Oxford, 1976, pp 227-233
15. Hamlin CR, Kohn RR, Luschin JH: Apparent accelerated aging of human collagen in diabetes mellitus. Diabetes 24: 902-904, 1975
16. Sakurai T, Tsuchiya S: Superoxide production from non-enzymatically glycated proteins. FEBS Lett 236: 406-410, 1988
17. Azovedo M, Falcao J, Raposo J, Manso C: Superoxide radical generation by Amadori compound. Free Radic Res Commun 4: 331-335, 1988