Comparative study of effects of cadmium cations in free and chelated forms on activity of glutathione S-transferase, growth, and endocytosis in culture of the infusoriumTetrahymena pyriformis

  • I. V. Shemarova
  • E. B. Maizel’
  • A. E. Khovanskikh
Comparative and Ontogenic Biochemistry


Effects of cadmium cations in free (Cd2+) and chelated with EDTA (Cd2+-EDTA) forms were studied on growth, endocytosis, and activity of glutathione S-transferase (GT) in the free-living infusoriaTetrahymena pyriformis. It is shown that the cytotoxicity of Cd2+ in the free form at a concentration of 10 μM is much higher than of the Cd2+-EDTA complex at the equimolar concentration. Even at a low concentration (2 μM), Cd2+ produces an inhibition of the growth rate and endocytosis in theT. pyriformis culture, while the Cd2+-EDTA complex suppresses these functions insignificantly. Cd2+ in the free form at concentrations of 10 and 100 μM reduced activity of glutathione S-transferase by 39 and 61%. The chelated Cd2+-EDTA complex at these concentrations inhibited the GT activity by 5 and 55%, respectively.


Cadmium Evolutionary Biochemistry Stationary Growth Phase Mercapturic Acid EDTA Complex 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Nilsson, J.K., Tetrahymena in Cytotoxicology with Special Reference to Effects of Heavy Metals and Selected Drugs,Eur. J. Protistol., 1989, vol. 25, pp. 2–25.Google Scholar
  2. 2.
    Carter, J.W. and Cameron, I.L., Toxicity Bioassay of Heavy Metals in Water UsingTetrahymena pyriformis, Water Res., 1973, vol. 7, pp. 951–961.CrossRefGoogle Scholar
  3. 3.
    Hutner, S.H. and Marcus, S.L., Protozoological Approaches to the Cellular Basis of Mammalian Stress Repair,Int. Rev. Cytol., 1987, vol. 100, pp. 371–425.PubMedCrossRefGoogle Scholar
  4. 4.
    Rana, S.V.S., Species Differences in Glutathione-Dependent Enzymes in the Liver and their Implications for Cadmium Toxicity,Ichthyological Res., 1996, vol. 43, pp. 223–229.CrossRefGoogle Scholar
  5. 5.
    Korotkov, S.M., Glasunov, V.V., Rozengart, E.V.,et al., Action of Organic Cadmium Complexes of Different Degree of Hydrophobicity on Rat Liver Mitochondria,Tsitologiya, 1996, vol. 38, pp. 1075–1083.Google Scholar
  6. 6.
    Dunlop, S. and Chapman, G., Detoxication of Zinc and Cadmium by Freshwater ProtozoanTetrahymena pyriformis. II. Growth Experiments and Ultrastructural Studies on Sequestration of Heavy Metals,Environ. Res., 1981, vol. 24, pp. 264–274.CrossRefGoogle Scholar
  7. 7.
    Houba, C., Kemacle, J., and De Parmetier, F., Influence of Cadmium onTetrahymena pyriformis in Axenic Culture,Eur. J. Appl. Microbiol. Biotechnol., 1981, vol. 11, pp. 179–182.CrossRefGoogle Scholar
  8. 8.
    Jacobson, K.B. and Turner, J.E., The Interaction of Cadmium and Certain Other Metal Ions with Proteins and Nucleic Acids,Toxicology, 1980, vol. 16, pp. 1–37.PubMedCrossRefGoogle Scholar
  9. 9.
    Pyne, C.K., The Effects of Cadmium on the Growth Pattern and Ultrastructure of the CiliateTetrahymena pyriformis, and Antagonistic Effect of Calcium,Biol. Cell, 1983, vol. 48, pp. 121–132.Google Scholar
  10. 10.
    Vasconcelos, S.D.M.T., Azenha, M.A.O., and Cabrai, J.P.S., Comparison of Availability of Copper (II) Complexes with Organic Ligands to Bacterial Cell and to Chitin,Microbiology, 1997, vol. 16, pp. 2029–2039.Google Scholar
  11. 11.
    Habig, W.H., Pabst, M.I., and Jacoby, W.B., Glutathione S-Transferases: the First Enzymatic Step in Mercapturic Acid Formation,J. Biol. Chem., 1974, vol. 249, pp. 7130–7139.PubMedGoogle Scholar
  12. 12.
    Lowry, O.N., Rosebrought, N.J., Farr, A.L., and Randall, R.J., Protein Measurement with the Folin Phenol Reagent,J. Biol. Chem., 1951, vol. 193, pp. 265–275.PubMedGoogle Scholar
  13. 13.
    Piccini, E., Irato, P., and Guidolin, L., Cadmium Thionein inTetrahymena thermophila andTetrahymena pyriformis, Eur. J. Protistol., 1990, vol. 26, pp. 176–181.Google Scholar
  14. 14.
    Cherian, M.G. and Nordberg, M., Cellular Adaptation in Metal Toxicology and Metallothionein,Toxicology, 1983, vol. 28, pp. 1–15.PubMedCrossRefGoogle Scholar
  15. 15.
    Larsen, J. and Nilsson, J.P., Effects of Nickel on the Rates of Endocytosis, Mobility and Proliferation in Tetrahymena and Determination on the Cell Content of the Metal,Protoplasma, 1983, vol. 118, pp. 140–147.CrossRefGoogle Scholar
  16. 16.
    Mannervik, B., Alin, P., Guthenberg, C.,et al., Identification of Three Classes of Cytosolic Glutathione Transferase Common to Several Mammalian Species: Correlation between Structural Data and Enzymatic Properties,Proc. Natl Acad. Sci. USA, 1985, vol. 85, pp. 7202–7206.CrossRefGoogle Scholar
  17. 17.
    Dierickx, P.J.,In vitro Inhibition of the Soluble Glutathione S-Transferases from Rat Liver by Heavy Metals,Enzyme, 1982, vol. 27, pp. 25–32.PubMedGoogle Scholar
  18. 18.
    Clark, A.C. and Revie, W., The Comparative Enzymology of the Glutathione S-Transferases from Nonvertebrate Organisms,Comp. Biochem. Physiol. B, 1989, vol. 92, pp. 419–446.PubMedCrossRefGoogle Scholar
  19. 19.
    Dierickx, P.J., Glutathione S-Transferase in Aquatic Macroinvertebrates and Its Interaction with Different Organic Micropollutants,Sci. Total Environment, 1984, vol. 40, pp. 93–108.CrossRefGoogle Scholar

Copyright information

© MAIK “Nauk/Interperiodica” 2000

Authors and Affiliations

  • I. V. Shemarova
    • 1
  • E. B. Maizel’
    • 1
  • A. E. Khovanskikh
    • 1
  1. 1.Sechenov Institute of Evolutionary Physiology and BiochemistryRussian Academy of SciencesSt. PetersburgRussia

Personalised recommendations