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Cytotechnology

, Volume 11, Supplement 1, pp S53–S55 | Cite as

Oxidative stress and transferrin receptor recycling

  • W. Malorni
  • F. Iosi
  • M. T. Santini
  • R. Rivabene
  • U. Testa
Session 2 Intracellular Architecture and Traffic Selected Papers

Abstract

Perturbation of the oxidative balance in biological systems plays an important role in numerous pathological states as well as in many physiological processes such as receptor activity. In order to evaluate if oxidative stress induced by menadione influences membrane receptor processes, a study was conducted on the transferrin receptor. Consequently, biochemical, biophysical and ultrastructural studies were carried out on different cell lines. The results obtained seem to indicate that oxidative stress is able of inducing a rapid and specific down-modulation of membrane transferrin receptor due to a block of receptor recycling on the cell surface without affecting binding affinity.

Keywords

Oxidative Stress Cell Surface Biological System Binding Affinity Pathological State 
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.

References

  1. Bellomo, G., Mirabelli, F., Vairetti, M., Iosi, F., and Malorni, W. (1990) ‘Cytoskeleton as a target in menadione-induced oxidative stress in cultured mammalian cells. 1. Biochemical and immunocytochemical features’. J. Cell. Physiol. 143, 118–128.Google Scholar
  2. Huebers, H.A., Finch, C.A. (1987) ‘The physiology of transferrin and transferrin receptors’, Physiol Rev. 67, 520–602.Google Scholar
  3. Martinez-Medellin, J. and Schulman, H.M. (1972) ‘The kinetics of Iron and transferrin incorporation into rabbit erythroid cells and the nature of stromal bound iron’. Biochim. Biophys. Acta 264, 272–283.Google Scholar
  4. Santini, M.T., Indovina, P.L., Simmons, J.R., and Peterson, S.W. (1990) ‘Human erythrocyte insulin receptor down-regulation is accompanied by a transient decrease in membrane order’. Biochim. Biophys. Acta 1054, 333–336.Google Scholar
  5. Schliwa, M. (1986) ‘Membrane-cytoskeleton interactions’, in M. Schliwa (ed.), The cytoskeleton, Springer-Verlag, Wien, pp. 179–236.Google Scholar
  6. Snyder, L.M., Fortier N.L., Trainor, J., Jacobs, J., Leb, L., Lubin, B., Chiu, D., Shohet, S., Mohandas, N. (1985) ‘Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics, and spectrinhemoglobin cross-linking’ J. Clin. Invest. 76, 1971–1977.Google Scholar
  7. Testa, U. (1985) ‘Transferrin receptor: structure and function’, Curr. Top. Hematol. 5, 127–181.Google Scholar

Copyright information

© Kluwer Academic Publishers 1993

Authors and Affiliations

  • W. Malorni
    • 1
  • F. Iosi
    • 1
  • M. T. Santini
    • 1
  • R. Rivabene
    • 1
  • U. Testa
    • 1
  1. 1.Department of UltrastructuresIstituto Superiore di SanitàRomeItaly

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