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2009, Number 4

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Bioquimia 2009; 34 (4)

Zinc: relationship with oxidative stress and diabetes

Torres-Domínguez A

Language: Spanish
References: 48
Page: 190-196
PDF size: 85.63 Kb.


ABSTRACT

Zinc is an essential micronutrient for the human organism that plays an important role in the reproduction, growth and development, cellular metabolism, genes expression, the immune response and the neurological function. This element is required as a catalytic cofactor of more than 300 enzymes and it stabilizes the structure of thousands of protein domains. Therefore a great number of biological processes are zinc dependent and an imbalance of its homeostasis has complex implications in a number of organs and can contribute to the onset of chronic pathologies. Recently several studies have been reported a relationship between the zinc functions and the oxidative stress associated to many diseases, such as diabetes mellitus. Diabetes is a serious problem of health at world for its high prevalence and its complications. Its development and complications on various organs have been attributed to increased oxidative stress. This has been associated among other factors to changes in the zinc metabolism that modify the insulin answer and metallothionein antioxidative properties, which is very rich in cysteine and is an excellent scavenger of reactive oxidative species. This review will briefly describe the zinc functions in the organism and its relation with the oxidative stress mechanisms associated with diabetes and its complications with an emphasis on experimental evidence and possible mechanisms.


REFERENCES

  1. Walsh T, Sandstead H, Prasad AS, Newberne P, Fraker PJ. Zinc: health effects and research priorities for the 1990s. Environ Health Perspect. 1994; 102(Suppl 2): 5-46.

  2. Kambea T, Yamaguchi-Iwai Y, Sasakib R, Nagaoa M. Overview of mammalian zinc transporters. Cell Mol Life Sci. 2004; 61: 49-68.

  3. Fischer CW, Black RE. Zinc and the risk for infectious disease. Annu Rev Nutr. 2004; 24: 255-75.

  4. Prasad AS. Recognition of zinc-deficiency syndrome. Nutrition. 2001; 17: 67-9.

  5. Hambidge KM, Krebs N. Zinc deficiency: a special challenge. J Nutr. 2007; 137: 1101-5.

  6. Valko M, Morris H, Cronin MTD. Metals, toxicity and oxidative stress. Curr Med Chem. 2005; 12: 1161-208.

  7. Prasad AS, Bin B, Beck FW, Kucuk O, Sarkar FH. Antioxidant effect of zinc in humans. Free Radic Biol Med. 2004; 37: 1182-90.

  8. Yousef MI, Hendy HAE, Demerdash FM, Elagamy E. Dietary zinc deficiency induced-changes in the activity of enzymes and the levels of free radicals, lipids and protein electrophoretic behaviour in growing rats. Toxicology. 2002; 14: 223-34.

  9. Kroncke KD. Cellular stress and intracellular zinc dyshomeostasis. Arch Biochem Biophys. 2007; 463: 183-7.

  10. Davis CD, Klevay LM, Milne DB, Nielsen FH. Extracellular superoxide dismutase activity: a promising indicator of zinc status in humans. FASEB J. 1998; 12: A346.

  11. Cousins R. Absorption, transport and hepatic metabolism of copperand zinc: special reference to metallothionein and ceruloplasmin. Phys Rev. 1985; 65: 238-309.

  12. Islam MS, Loots du T. Diabetes, metallothionein, and zinc interactions: a review Biofactors. 2007; 29: 203-12.

  13. Li X, Cai L, Feng W. Diabetes and metallothionein. Mini Rev Med Chem. 2007; 7: 761-8.

  14. Bray T, Bettger W. The physiological role of zinc as an antioxidant. Free Radic Biol Med. 1990; 8: 281-91.

  15. Noh S, Koo S. Feeding of a marginally low level of dietary zinc lowers the concentration of a-tocopherol (a-P) in selected organs. FASEB J. 1998; 12: A217.

  16. Shankar AH, Prasad AS. Zinc and immune function: the biological basis of altered resistance to infection. Am J Clin Nutr. 1998; 68(Suppl): 447S-463S.

  17. Stein JH. Medicina interna. Ciudad de La Habana: Revolucionaria. 1988; Tomo II (II): 2321-2, 2077-8.

  18. Kruston L. Endocrinology and diabetes. New York: Grune and Stratton; 1975.

  19. Organización Mundial de la Salud. Informes y estadísticas de Salud. 2006-2008. Disponible en: http://www.who.int/whr/2007/es/index.html

  20. Knight JA. Diseases related to oxygen-derived free radicals. Ann Clin Lab Sci. 1995; 25: 111-21.

  21. Halliwell B, Cross CE. Oxygen-derived species: their relation to human disease and environmental stress. Environ Health Presp. 1994; 102(Suppl. 10): 5-12.

  22. Favier A. Oxidative stress in human diseases. Ann Pharm Fr. 2006; 64: 390-6.

  23. Sinclair AJ, Lunce J. Free radicals, oxidative stress and diabetes mellitus. In: Immunopharmacology of free radical species. D Wingard PG. [Eds] Ciudad: Academic Press; 1995. p. 183-98.

  24. Wulf D. Free radicals in the physiological control of cell function. Physiol Rev. 2002; 82: 47-95.

  25. Jarjour N, Callhouh WJ. Enhanced production of oxygen radicals in asthma. J Lab Clin Med. 1994; 123: 131-6.

  26. Maxwell SR. Prospects for the use of antioxidant therapies. Drugs. 1995; 49: 345-61.

  27. León OS, Menéndez S, Merino N. Ozone oxidative preconditioning: a protection against cellular damage by free radicals. Mediators Inflamm. 1998; 7: 289-94.

  28. Coppola L. Influence of ozone on hemoglobin oxygen affinity in type 2 diabetic patients with peripheral vascular disease: in vitro studies. Diabetes Metabol. 1995; 21: 252-5.

  29. Sadaivudu B, Sasikala M, Sailaja V, Reddy S. Serum malondialdehyde, insulin, glucose and lipid profile in hypertension. Med Sci Res. 1997; 25: 631-3.

  30. Rakesh K, Jawahar K, Subrahmanyam V M, Kailash P. Lipid peroxidation and activity of antioxidant enzymes in diabetic rats. Mol Cell Biochem. 1995; 15: 113-9.

  31. Ceriello A. Acute hyperglycemia and oxidative stress generation. Diabet Med. 1997; 14 (Suppl. 3): S45-49.

  32. Ceriello A, Mercuri F, Quagliano L, Assaloni R, Motz E. Detection of nitrotyrosine in the diabetic plasma: evidence of oxidative stress. Diabetología. 2001; 44: 834-8.

  33. Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature. 2001; 44: 813-20.

  34. Bruno G, Constantiro L, Curinga C. Synthesis and aldose reductase inhibitory activity of 5-aryldene-2,4-thiazolinediones. Bioorg Med Chem. 2002; 10: 1077-84.

  35. Rastelli G, Ferrari AM, Constantino L. Discovery of new inhibitors of aldose reductase from molecular docking and database screening. Bioorg Med Chem. 2002; 10: 1437-50.

  36. Iwata Y, Naito S, Itai A, Miyamoto S. Protein structure-based de novo design and synthesis of aldose reductase inhibitors. Drug Des Discov. 2001; 17: 349-59.

  37. Chen YQ. Sp1 sites mediated activation of the plasminogen activator inhibitor-1 promoter by glucose to vascular smooth muscle cells. J Biol Chem. 1998; 273: 8225-31.

  38. Duzguner V, Kay S. Effect of zinc on the lipid peroxidation and the antioxidant defense systems of the alloxan-induced diabetic rabbits. Free Radic Biol Med. 2007; 42: 1481-6.

  39. Devirgiliis C, Zalewski PD, Perozzi G, Murgia C. Zinc fluxes and zinc transporter genes in chronic diseases. Mutat Res. 2007; 622: 84-93.

  40. Prasad AS. Zinc deficiency in patients with sickle cell disease. Am J Clin Nutr. 2002; 75: 181-2.

  41. Bhatnagar S. Effects of zinc supplementation on child mortality. Lancet. 2007; 369: 885-6.

  42. Prasad AS, Beck FWJ, Bao B, Fitzgerald JT, Snell DC, Steinberg JD, Cardozo LJ. Zinc supplementation decreases incidence of infections in the elderly: effect of zinc on generation of cytokines and oxidative stress. Am J Clin Nutr. 2007; 85: 837-44.

  43. Franklin RB, Costello LC. Zinc as an anti-tumor agent in prostate cancer and in other cancers. Arch Biochem Biophys. 2007; 463: 211-7.

  44. Cai L. Diabetic cardiomyopathy and its prevention by metallothionein: experimental evidence, possible mechanisms and clinical implications. Curr Med Chem. 2007; 14: 2193-203.

  45. Partida-Hernández G, Arreola F, Fenton B, Cabeza M, Román-Ramos R, Revilla-Monsalve MC. Effect of zinc replacement on lipids and lipoproteins in type 2-diabetic patients. Biomed Pharmacother. 2006; 60: 161-8.

  46. Chimienti F, Devergnas S, Favier A, Seve M. Identification and cloning of a beta-cell-specific zinc transporter, ZnT-8, localized into insulin secretory granules. Diabetes. 2004; 53: 2330-7.

  47. Chimienti F, Devergnas S, Pattou F, Schuit F, Garcia-Cuenca R, Vandewalle B, et al. In vivo expression and functional characterization of the zinc transporter ZnT8 in glucose-induced insulin secretion. J Cell Sci. 2006; 119: 4199-206.

  48. Haase H, Maret W. Protein tyrosine phosphatases as targets of the combined insulinomimetic effects of zinc and oxidants. Biometals. 2005; 18: 333-8.




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