Biochemical studies on peroxidation in ammonium para-tungstate-treated experimental diabetic rats

Medical Science Research

Volumn 26, Issue 11, 1998, Pages 759-762

  Palanivel, R ^a   Ravichandran, P ^a   Govindasamy, S ^a  

^a UNIVERSITY OF MADRAS   (India)

Author keywords

Ammonium para tungstate; Catalase; Ceruloplasmin; Diabetes; Glutathione; Lipid peroxidation; Streptozotocin; Superoxide dismutase

Indexed keywords

AMMONIUM DERIVATIVE; AMMONIUM PARA TUNGSTATE; ANTIOXIDANT; CATALASE; CERULOPLASMIN; FERRITIN; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; HYDROXYL RADICAL; IRON; LIPID; LIPID PEROXIDE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CERULOPLASMIN BLOOD LEVEL; CONTROLLED STUDY; ENZYME ACTIVITY; FERRITIN BLOOD LEVEL; IRON BLOOD LEVEL; LIPID PEROXIDATION; MALE; NONHUMAN; RAT; STREPTOZOCIN DIABETES;

ANIMALIA;

EID: 0031796779     PISSN: 02698951     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (45)

1. Garg MC. Ojha S. Bansal DD. Antioxidant status of streptozotocin diabetic rats. Intl J Exp Biol 1995; 34:264-266.
2. Sandler S. Andersson. The partial protective effect of the hydroxyl radical scavenger dimethyl urea on streptozotocin-induced diabetes in the mouse in vivo and in vitro. Diabeiologiu 1982: 23:374-378.
3. Grankvist K, Marklund SL. Effect of extracellularly generated free radicals on the plasma membrane permeability of isolated pancreatic β-cells. lut J Biochem 1986: 18:109-114.
4. Meister A. Anderson ME. Glutathione. Ann KIT Biochem 1983: 52:711-760.
5. Mak DHF, Ip SP, Li PC. Poon MKT, Ko KM. Alterations in tissue glutathione antioxidant system in streptozotocin-induced diabetic rats. Mol Cell Biochem 1996: 162:153-158.
6. Jinping L, Erberg G. Gefel D, Schechter Y. Permolybdate and pertungstate-potent stimulators of insulin effects in rat adipoeytes. Biochemistry 1995; 34(18):6218-6225.
7. Sasaki J, Matsui S. Effect of acetic acid concentration on the colour reaction in the o-toluidine-boric acid method tor blood glucose determination. Rinshu kegakitin 1972; 1:346-353.
8. Ramsay WNM. Iodine, iron and copper, sulphur, magnesium. In: Sobaka H, Steward LP (editors) Advances in Clinical Chemistry. Vol. 1. New York: Academic Press. 1958. pp. 36914.
9. Drysdale JW, Munro HN. Small scale isolation of ferritin for the assay of the incorporation of C-labelled amino acids. Biochem J 1965: 95:851-858.
10. Herbert AR. An improved colorimetric enzymatic assay for ceruloplasmm. J Lab Clin Med 1961; 58:161-168.
11. Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxide in animal tissue by thiobarbituric acid reaction. Anal Biochem 1979; 95:351-358.
12. Ellamn GL. Tissue sulphydral groups. Arch Biochem Biophvs 1959: 82:70-71.
13. Habig WH, Pabst MJ, Jackoby WBS. Glutathione-S-transierases - the first enzymatic step in mercapturic acid formation. J Biol Chem 1974; 249:7130-7139.
14. Pagila DE. Valentaine WN. Studies on the glutathione and glutathione characterization of erythroeyte glutathione peroxidases. J Lub Clin Med 1967:70:158-169.
15. Misra HP, Fridovich T. The role of Superoxide ion in the auto-oxidation of epinephrine and a simple assay for Superoxide dismutase. J Biol Chem 1972; 247:3170-3175.
16. Takahara S, Hamilton BH, Nell JV, Kobra TY. Ogawa Y. Nichimura ET. Hypocatalasemia. Anew genetic carrier state. J Clin Invest I960: 29:610-619.
17. Parthasarathy S, Wieland E. Steinberg D. A role for endothelial cell lipoxygenase in the oxidative modification of low density lipoprotein. Proc Nail Acad Sci 1989; 86:1046-1050.
18. Woeff SP. Dean RT. Glucose autooxidation and protein modification. The potential role of autooxidative glycosylation in diabetes. Biochem J 1987:245:243-250.
19. Quinlan GJ, Gutteridge JMC. Hydroxy radical generation by the tetracycline antibiotics with free radical damage to DNA, lipids, carbohydrates in the presence of iron and copper salts. Biol Med 1988: 5:341-348.
20. Sekar N, Kanthasamy A, William S, Balasubramaniyan N. Govindasamy S. Antioxidant effect of vanadate on experimental diabetic rats. Ada Diabetoi La! 1990; 27:285-293.
21. Hallwel B, Gutteridge JMC. Oxygen toxicity. oxygen radicals, transition metals and disease. Biochem J 1984; 219:1-14.
22. Gutteridge JMC, Quinlan GJ, Wilkins S. Mitomycin C-induced deoxyribose degradation inhibited by Superoxide dismutase: A reaction involving iron, hydroxyl and semiquinone radicals. FEBS Let: 1984: 167:37-41.
23. Thomas CH, Morehouse LA. Aust SD. Fcrritin and superoxidedepcndent lipid peroxidation. J Riol Cliem 1985: 260:3275-3280.
24. Anne L. Rohen R. An animal model ol' iron overload and ils application to study hepatic ferritin iron mobilization hv chelators. Kiochem Phiirmacol 1986:35:3669-3678.
25. While A. The erythrocytes and iron metabolism. In: Derede J. Macrow A. Labarhera H. Armstrong T (editors) The Principles <>J' Biochemistry. Tokyo: Kosaido Printing Co.. Ltd: 1978. pp. 1006- 1007.
26. West ES. Wilberl T. The metabolism of inorganic elements. In: West ES, Todd WR (editors). The Text Book of Biochemistry. New York: Macmillan Co; 1961. pp. 1252-1253.
27. Barry H. Gutteridgc JMC. Measurement of lipid peroxidation. In: Barry H. (editor) Free Radicals in Biology and Medicine. Oxford: Clarendon Press; 1989. pp. 254-255.
28. Das M. Glutalhione status of some homeothermic vertebrate species and its relation with diabetogenesis. IndJ Exp Biol 1997: 35:661-662.
29. Asplund K. Grankvist K. Marklund S. Teljedal IB. Partial protection against streptoJ.otocin-induced hyperglycemia by Superoxide dismutase linked to polyethlene glyco. Ada Endocrinal 1984; 107:390-394.
30. Burk RF. Glutathione dependent protection by rat liver microsomal protein against lipid peroxidation. Biochim Biophvs Ada 1983; 757:21-28.
31. Younes M, Soegers CP. Mechanistic aspects of enhanced lipid peroxidation following glutathione depletion in vivo. Cheni Biol Interact 1981:34:257-266.
32. Comport! M. Biology of disease: Lipid peroxidation and cellular damage in toxic liver injury. Lab Invest 1985; 53:599-623.
33. Inove M, Saito Y, Hirato E, Morino Y, Nagase S. Regulation of redox status of plasma proteins by metabolism and transport of glutathione and related compounds. J Protein Chem 1987; 6:207-225.
34. Wohaieb SA. Godin DV. Starvation-related alterations in free radical tissue defence mechanisms in rats. Diabetes 1987; 36:169-173.
35. Yoshikawa T. Naito Y, Kishi A, Tomii T. Kaneko T, linuma S et al. Role of active oxygen, lipid peroxidation and antioxidants in the pathogenesis of gastric mucosal injury induced by indomethacin in rats. Gut 1993:34:732-737.
36. Grant MH. Duthie SJ. Conjugation reactions in hepatocyte isolated from streptozotocin-induced diabetic rats. Kiochem Pharmacol 1987: 30:3647-3655.
37. Saito-Yamanaka N, Yamanaka H, Nagasawa S. Glutathione related detoxification functions in streptozotocin-induced diabetic rats. J Vet MedSci 1993; 55:991-994.
38. Thomas H, Schladt, Khehr M. Oesch F. Effect of diabetes and starvation on the activity of rat liver epoxide hydrolases. glutathione-stransferases and peroxisomal -oxidation. Biochem Pharmacol 1989: 38:4291-4297.
39. Aniya Y, Ojiri Y, Sunagawa R, Murakami K. Zhenzhong G, Mimura G et al. Glutathione-s-transferases and chloroform-toxicity in streptozotocin-induced diabetic rats. Jpn J Pharmacol 1989: 50:263-269.
40. De-Mattia G, Laurenti O. Bravi C, Ghiselli A, luliano L. Balsano F. Effect of aldose reductase inhibition on glutathione redox status in erythrocytes of diabetic patients. Metabolism 1994; 43:965-968.
41. Meister A, Glutathione metabolism and its selective modification. J Biol Chem 1988; 263:17205-17208.
42. Ross D. Glutathione, free radicals and chemotherapeutic agents, mechanism of free radical induced toxicity and glutathione dependent protection. Pharmacol The r 1988; 37:231-249.
43. Velykyi AM. The effect of nicotinamide on the enzymatic activity of the antioxidant defense in experimental diabetes. Ukr Biochem Zh 1996: 68(2): 109-114.
44. Mason RP, Chignell CF. Free radicals in pharmacology and toxicology. Pharmacol Rev 1982; 33:189-212.
45. Grankvist K, Marklund S, Taljedal IB. Superoxide dismutase is a prophylactic against alloxan diabetes. Nature 1981; 294:158-160.