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Studies on the effect of monosodium glutamate (MSG) administration on the activity of xanthine oxidase, superoxide dismutase and catalase in hepatic tissue of adult male mice

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Abstract

Subcutaneous administration of monosodium glutamate (MSG), to normal adult male mice, for six consecutive days at dose levels of 4 and 8 mg/g body weight, significantly increased the level of free radical initiating enzyme, xanthine oxidase, whereas the activity of free radical scavenging enzymes, like catalase and superoxide dismutase was significantly decreased in hepatic tissue. These observations suggested that ingestion of MSG at dose level of 4 mg/g body weight and above, induced oxidative stress in the hepatic tissue of adult male mice.

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References

  1. Walkar, R. and Lupien, J. (2000) The safety evolution of monosodium glutamate. J. Nutr, 130, 1049S-1052S.

    Google Scholar 

  2. Nakashima, K., Katsukawa, H., Sasmoto, K. and Ninomiya, Y. (2001) Behavioral taste stamulates and differences among monosodium glutamate and glutamate receptor agonists in C57BL mice J. Nutr. Sci. Vitaminol. 47, 161–166.

    PubMed  CAS  Google Scholar 

  3. Geha, R.S., Beiser, A., Ren, C., Patterson, R., Greenberger, P.A., Grammer, L.C., Ditto, A.M., Harris, K.E., Shaughnessy, M., Yarnold, P.R., Corren, J. and Saxon, A. (2000) Review of alleged reaction to monosodium glutamate and out come of a multicenter double-blind placebo-controlled study. J. Nutr, 130, 1058S-1062S.

    PubMed  CAS  Google Scholar 

  4. Choudhary, P., Malik, V.B.T., Puri, S. and Ahluwalia, P. (1996). Studies on the effect of monosodium glutamate on hepatic microsomal lipid peroxidation, calcium, ascorbic acid and glutathione and its dependent enzymes in adult male mice. Toxicol. Lett, 89, 71–76.

    Article  PubMed  CAS  Google Scholar 

  5. Ahluwalia, P. and Malik, V.B.T. (1989) Effect of monosodium glutamate (MSG) on serum lipids, blood glucose and cholesterol in adult male mice. Toxicol. Lett, 45 195–198.

    Article  PubMed  CAS  Google Scholar 

  6. Ahluwalia, P., Tewari, K. and Choudhary, P. (1996) Studies on the effect of monosodium glutamate (MSG) on oxidative stress in erythrocyte of adult male mice. Toxicol. Lett. 84, 161–165.

    Article  PubMed  CAS  Google Scholar 

  7. Malik, V.B.T. and Ahluwalia, P. (1994) Studies on the effect of monosodium glutamate (MSG) on various fractions of lipids and carbohydrate metabolic enzymes in liver and blood of adult male mice. Toxicol. Lett. 74, 69–77.

    Article  PubMed  CAS  Google Scholar 

  8. Baskaran, S., Lakshmi, S. and Prasad, P.R. (1999). Effect of cigarette smoke on lipid peroxidation and antioxidant enzymes in albino rat. Ind. J. Exp. Biol. 37, 1196–1200.

    CAS  Google Scholar 

  9. Hamaoka, K. and Kusunok, T. (1986) Morphological and cell proliferative study on the growth of visceral organ in monosodium L-glutamate-treated obese mice. J. Nutr. Sci. Vitaminol. 32, 395–411.

    PubMed  CAS  Google Scholar 

  10. Ochi, M., Furukawa, H., Yoshioka, H., Sawada, T., Kusuoki, T. and Hattori, T. (1991) Adipocyte dynamics in hypothalamic obese mice during food deprivation and refeeding. J. Nutr. Sci. Vitaminol. 37, 479–491.

    PubMed  CAS  Google Scholar 

  11. Luck, H. (1971) Catalase. Methods of enzymatic analysis, Ed. Bergmeyer, H.O. Academic Press, New York, London, p. 855–893.

    Google Scholar 

  12. Kono, Y. (1978) Generation of superoxide radical during autoxidation of hydroxylamine and an assay for superoxide dismutase. Arch. Biochem. Biophys. 186 189–195.

    Article  PubMed  CAS  Google Scholar 

  13. Fried, R. and Fried, L.W. (1974) Xanthine oxidase (Xanthine dehydrogenase). Method of enzymatic analysis, Ed. Bergmeyer, H.U. Academic Press, New York, London, vol 2, p. 644–649.

    Google Scholar 

  14. Lowry, O.H., Rosenbrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265.

    PubMed  CAS  Google Scholar 

  15. Adachi, T., Fukshima, T., Usami, Y. and Hirano, K. (1993) Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endothelial cell surface. Biochem. J. 289, 523–527.

    PubMed  CAS  Google Scholar 

  16. Sharma, O.P., Makkar, H.P.S., Pal, R.N. and Negi, S.S. (1980) Lantadene a content and toxicity of the lantana plant (Lantana camara, Linn.) to guinea pigs. Toxicon 18, 485–488.

    Article  PubMed  CAS  Google Scholar 

  17. McCord, J.M. (1979) Superoxide dismutase in Isozyme: Current topics in biological and medical research Eds. Tattazzi M.C., Scanalios J.G., Whitt, G.S. and Alan, R. Liss Inc, New York, section 1.

    Google Scholar 

  18. Marklund, S.L. (1984) Properties of extracellular superoxide dismutase from human lung. Biochem. J. 220, 269–272.

    PubMed  CAS  Google Scholar 

  19. Fridovich, I. (1975) Superoxide dismutase. Annu. Rev. Biochem. 44, 147–159.

    Article  PubMed  CAS  Google Scholar 

  20. Smith, P. and Health, D. (1986) Paraquat, C.R.C. Crit. Rev. Toxicol. 4, 411–445.

    Google Scholar 

  21. Karalsson, K. and Marklund, S.L. (1988) Extracelullar-superoxide dismutase association with cell surface-bound sulfated glucosaminoglycans. In: Oxygen radical in biology and medicine, Eds. Simic, M.G., Taylor, K.A., Ward, J.F. and Von Sonntag, C. Plenum Press, New York, London, p. 647–649.

    Google Scholar 

  22. Oshino, N., Jamieson, D. and Chance, B. (1975) The properties of hydrogen peroxide production under hyperoxic and hypoxic conditions of perfused rat liver. Biochem. J. 146 53–56.

    PubMed  CAS  Google Scholar 

  23. Krikman, H.N. and Gaetani, G.F. (1984) Catalase, a tetrameric enzyme with four tightly bound molecules of NADPH. Proc. Natl. Acad. Sci. USA. 81, 4343–4347.

    Article  Google Scholar 

  24. Gaetani, G.F., Galliano, S., Canepa, L., Ferraris, A.M. and Kirkman, J.N. (1989) Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes. Blood 73, 334–339.

    PubMed  CAS  Google Scholar 

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Singh, K., Ahluwalia, P. Studies on the effect of monosodium glutamate (MSG) administration on the activity of xanthine oxidase, superoxide dismutase and catalase in hepatic tissue of adult male mice. Indian J Clin Biochem 17, 29–33 (2002). https://doi.org/10.1007/BF02867938

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