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An insect model for assessing mercury toxicity: Effect of mercury on antioxidant enzyme activities of the housefly (Musca domestica) and the cabbage looper moth (Trichoplusia ni)

  • K. Zaman
  • R. S. MacGill
  • J. E. Johnson
  • S. Ahmad
  • R. S. Pardini
Article

Abstract

The effect of mercury as Hg2Cl2 and HgCl2 on the antioxidant enzyme levels and its toxicity was investigated in an insect model comprised of adult females of the common housefly, Musca domestica, and fourth-instar larvae of the cabbage looper moth, Trichoplusia ni. HgCl2 was found to be more toxic than Hg2Cl2 to both M. domestica and T. ni. The LC50s for M. domestica were 1.17% and 0.38% w/v concentration for Hg2Cl2 and HgCl2, respectively. For the more tolerant T. ni, the LC50s were 5.15% for Hg2Cl2 and 0.96% w/w concentration for HgCl2. The minimally acute LC5 dose of both oxidation states of Hg was approximately 0.005% for both insects (w/v for M. domestica and w/w for T. ni). At the LC5, both forms of Hg significantly induced the activity of superoxide dismutase in both insect species. Catalase was induced by both Hg2Cl2 and HgCl2 in M. domestica but was only induced by HgCl2 in T. ni. Glutathione-S-transferase, its peroxidase activity, and glutathione reductase activites were also significantly altered in most cases by Hg in both insects although the pattern of alteration was different between the two insects. It is evident that mercury induces oxidative stress in insects as it does in vertebrates. Our findings suggest that insects may serve as a valuable, non-mammalian model species to assess Hg-induced oxidative stress as a component of environmental toxicity.

Keywords

Mercury Antioxidant Enzyme Catalase Superoxide Dismutase Glutathione Reductase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Aebi H (1984) Catalase in vitro. Meth Enzymol 105:121–126Google Scholar
  2. Ahmad S (1992) Biochemical defence of pro-oxidant plant allelochemicals by herbivorous insects. Biochem Syst Ecol 20:269–296Google Scholar
  3. Ahmad S, Pardini RS (1988) Evidence for the presence of glutathione peroxidase activity toward an organic hydroperoxide in larvae of the cabbage looper moth, Trichoplusia ni. Insect Biochem 18:861–866Google Scholar
  4. —, — (1989) Corrigendum. Insect Biochem 19:109Google Scholar
  5. —, — (1990) Mechanisms for regulating of oxygen toxicity in phytophagous insects. Free Rad Biol Med 8:401–413Google Scholar
  6. Ahmad S, Pritsos CA, Bowen SM, Heisler CR, Blomquist GJ, Pardini RS (1988) Antioxidant enzymes of larvae of the cabbage looper moth, Trichoplusia ni: Subcellular distribution and activities of superoxide dismutase, catalase, and glutathione reductase. Free Rad Res Commun 4:403–408Google Scholar
  7. Ahmad S, Pritsos CA, Bowen SM, Kirkland KE, Blomquist GJ, Pardini RS (1987) Activities of the enzymes that detoxify superoxide anion and related oxyradicals in Trichoplusia ni. Arch Insect Biochem Physiol 7:85–96Google Scholar
  8. Ahmad S, Pritsos CA, Pardini RS (1990) Antioxidant enzyme activities in subcellular fractions of larvae of the black swallowtail butterfly, Papilio polyexenes. Arch Insect Biochem Physiol 15:101–109Google Scholar
  9. Anonymous (1986) Test methods for evaluating solid waste. Vol IA: Laboratory Manual Physical/Chemical Methods, SW-846, 3rd ed, U.S. Environmental Protection Agency, Washington, DCGoogle Scholar
  10. Chung A-S, Maines MD, Reynolds WA (1982) Inhibition of the enzymes of glutathione metabolism by mercuric chloride in the rat kidney: Reversal by selenium. Biochem Pharmacol 31:3093–3100Google Scholar
  11. Corbett JR (1974) The biochemical mode of action of pesticides. Academic Press, LondonGoogle Scholar
  12. Finney DJ (1964) Probit analysis. 2nd ed. Cambridge University Press, LondonGoogle Scholar
  13. Friberg L, Nordberg G, Vouk VB (1979) Introduction. In: Friberg L, Nordberg G, Vouk VB (eds). Handbook on the toxicology of metals Elsevier/North-Holland, Amsterdam, pp 1–11Google Scholar
  14. Fridovich I (1983) Superoxide radical: An endogenous toxicant. A Rev Pharmacol Toxicol 23:239–257Google Scholar
  15. Grinstein S, Rothstein A (1978) Chemically-induced cation permeability in red cell membrane vesicles. Biochim Biophys Acta 508: 236–245Google Scholar
  16. Gwozdzinski K, Roche H, Peres G (1992) The comparison of the effects of heavy metal ions on the antioxidant enzyme activities in human and fish Dicentrarchus labrax erythrocytes. Comp Biochem Physiol 102C:57–60Google Scholar
  17. Habig WH, Jakoby WB (1981) Glutathione-S-transferase in rat and human. Meth Enzymol 77:218–231Google Scholar
  18. Halliwell B, Richmond R, Wong SF, Gutteridge JMC (1980) The biological significance of the Haber-Weiss reaction. In Bannister WH, Bannister JV (eds.) Biological and clinical aspects of superoxide and superoxide dismutase Elsevier/North-Holland, Amsterdam, pp 32–41Google Scholar
  19. Luckey TD, Venugopal B, Hutcheson D (1975) Environmental quality and safety. Supplement Vol 1. Academic Press, NYGoogle Scholar
  20. Lund B-O, Miller DM, Wood JS (1991) Mercury-induced H2O2 production and lipid oxidation in vitro in rat kidney mitochondria. Biochem Pharmacol 42:181–187.Google Scholar
  21. McCord JM, Fridovich I (1969) Superoxide dismutase. J Biol Chem 244:6049–6055PubMedGoogle Scholar
  22. Miquel J (1989) Historical introduction to free radical and antioxidant biomedical research. In: Miquel J, Quintanilha AT, Weber H (eds), CRC handbook of free radicals and antioxidants in biomedicine, CRC Press, Boca Raton, FL, vol 1, pp 3–11Google Scholar
  23. Oberley LW, Spitz DR (1984) Assay of superoxide dismutase activity in tumor tissue. Meth Enzymol 105:457–464Google Scholar
  24. Passow H, Rothstein A, Clarkson TW (1961) The general pharmacology of the heavy metals. Pharmacol Rev 13:185–224Google Scholar
  25. Pritsos CA, Ahmad S, Bowen SM, Blomquist GJ, Pardini RS (1988a) Antioxidant enzymes in the southern armyworm, Spodoptera eridania. Comp Biochem Physiol 90C:423–427Google Scholar
  26. Pritsos CA, Ahmad S, Bowen SM, Elliott AJ, Blomquist GJ, Pardini RS (1988b) Antioxidant enzymes of the black swallowtail butterfly, Papilio polyxenes, and their response to the pro-oxidant allelochemical, quercetin. Arch Insect Biochem Physiol 8:101–112Google Scholar
  27. Racker E (1955) Glutathione reductase (liver and yeast). Meth Enzymol 2:722–725Google Scholar
  28. Ribarov SR, Benov LC (1981) Relationship between the hemolytic action of heavy metals and lipid peroxidation. Biochim Biophys Acta 640:721–726Google Scholar
  29. Stacey NH, Kappus H (1982) Cellular toxicity and lipid peroxidation in response to mercury. Toxicol Appl Pharmacol 63:29–35Google Scholar
  30. Stewart RM (1977) Laboratories section procedures for the characterization of water and wastes. County Sanitation Districts of Los Angeles County, 3rd ed, Whittier, CAGoogle Scholar
  31. Venugopal B, Luckey TD (1978) Metal toxicity in mammals. Part 2: Chemical toxicity of metals and metalloids. Plenum Press, NYGoogle Scholar
  32. Weinhold LC, Ahmad S, Pardini RS (1990) Insect glutathione-Stransferase: A predictor of allelochemical and oxidative stress. Comp Biochem Physiol 95B:355–363Google Scholar

Copyright information

© Springer-Verlag New York Inc 1994

Authors and Affiliations

  • K. Zaman
    • 1
  • R. S. MacGill
    • 1
  • J. E. Johnson
    • 1
  • S. Ahmad
    • 1
  • R. S. Pardini
    • 1
  1. 1.Department of BiochemistryUniversity of Nevada-RenoRenoUSA

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