Cell Biophysics

, 18:1 | Cite as

Contact patterns in concanavalin A agglutinated erythrocytes

  • Homa Darmani
  • W. Terence Coakley
Article
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Accepted:

Abstract

Agglutination of human erythrocytes by the lectin concanavalin A is enhanced when the erythrocytes are pretreated with neuraminidase, which removes sialic acids, or with pronase, which degrades both the glycophorins and band 3 protein. In the present work transmission electron microscopy of the enzymatically pretreated erythrocytes shows a regular pattern of interruption of contact between interacting plasma membranes. The lengths characteristic of the pattern were 0.66 and 0.50 μm for pronase- and neuraminidase-pretreated cells, respectively. Agglutination of normal erythrocytes and of neuraminidase-pretreated erythrocytes can be fully reversed by exposure to the competitive inhibitor methyl α-D-mannopyranoside. Complete reversal of contact does not occur with pronase-pretreated cells. The comparatively greater tenacity of contact between cells that were treated with pronase before exposure to lectin argues for an involvement of nonspecific interactions in the agglutination process. The results are compared with previously published studies of spatially periodic contact patterns induced by a range of other polymers.

Index Entries

Concanavalin A erythrocyte membrane spatially periodic contact interfacial instability lectin cell adhesion cell agglutination colloid stability 
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References

  1. 1.
    Goldstein, I. J. and Poretz, R. D. (1986),The Lectins: Properties, Functions and Applications in Biology and Medicine, Liener, I. E., Sharon, N., and Goldstein, I. J., eds., Academic, London, pp. 35–250.Google Scholar
  2. 2.
    Kapito, R. R. and Lodish, H. (1985),Nature 316, 234–238.CrossRefGoogle Scholar
  3. 3.
    Grant, C. W. M. and Peters, M. W. (1984),Biochim. Biophys. Acta 779, 403–422.PubMedGoogle Scholar
  4. 4.
    Gokhale, S. M. and Mehta, N. G. (1987),Biochem. J. 241, 505–511.PubMedGoogle Scholar
  5. 5.
    Brooks, D. E. and Grieg, R. G. (1981),Biorheology 18, 273, 274.Google Scholar
  6. 6.
    Grieg, R. G. and Brooks, D. E. (1979),Nature 282, 738, 739.CrossRefGoogle Scholar
  7. 7.
    Grieg, R. G. and Brooks, D.E. (1981),Biochim. Biophys. Acta 641, 410–415.CrossRefGoogle Scholar
  8. 8.
    Coakley, W. T., Hewison, L. A., and Tilley, D. (1985),Eur. Biophys. J. 13, 123–130.PubMedCrossRefGoogle Scholar
  9. 9.
    Hewison, L. A., Coakley, W. T., and Meyer, H. W. (1988),Cell Biophys. 13, 151–157.PubMedGoogle Scholar
  10. 10.
    Jan, K. M. and Chien, S. (1973),J. Gen. Physiology 61, 638–654.CrossRefGoogle Scholar
  11. 11.
    Skalak, R., Zarda, P. R., Jan, K. M., and Chien, S. (1981),Biophys. J. 35, 771–781.PubMedCrossRefGoogle Scholar
  12. 12.
    Darmani, H. and Coakley, W. T. (1990),Biochim. Biophys. Acta 1021, 182–190.PubMedCrossRefGoogle Scholar
  13. 13.
    Darmani, H., Coakley, W. T., Hann, A. C., and Brain, A. (1990),Cell Biophys. 16, 105–126.PubMedGoogle Scholar
  14. 14.
    Chien S. and Jan, K. M. (1973),J. Supramolec. Struct. 1, 385–409.CrossRefGoogle Scholar
  15. 15.
    Tilley, D., Coakley, W. T., Gould, R. K., Payne, S. E., and Hewison, L. A. (1987),Eur. Biophys. J. 14, 499–507.PubMedCrossRefGoogle Scholar
  16. 16.
    Reichstein, E. and Biostein, R. (1975),J. Biol. Chem. 16, 6256–6263.Google Scholar
  17. 17.
    Schnebli, H. P. and Bachi, T. (1975),Exp. Cell Res. 91, 175–183.PubMedCrossRefGoogle Scholar
  18. 18.
    Gokhale, S. M. and Mehta, N. G. (1987),Biochem. J. 241, 521–525.PubMedGoogle Scholar
  19. 19.
    Bachi, T. and Schnebli, H. P. (1975),Exp. Cell Res. 91, 285–295.PubMedCrossRefGoogle Scholar
  20. 20.
    Seaman, C. V. F. (1975),The Red Blood Cell, vol. 2, Surgeoner, D. M., ed., Academic, New York, pp. 1135–1229.Google Scholar
  21. 21.
    Schnebli, H. P., Roeder, C. and Tarcsay, L. (1976),Exp. Cell Res. 98, 273–276.PubMedCrossRefGoogle Scholar
  22. 22.
    Gascoine, P. S. and Fisher, D. (1985),Trans. Biochem. Soc. 12, 1085, 1086.Google Scholar
  23. 23.
    Shelton, I., Gascoine, P. S., Turner, D. M., and Fisher, D. (1985),Biochem. Soc. Trans. 13, 168, 169.Google Scholar
  24. 24.
    van Oss, C. J., Gillman, C. E., and Neumann, A. W. (1975),Phagocytic Engulfment and Cell Adhesiveness, Dekker, New York, pp. 108–131.Google Scholar
  25. 25.
    van Oss, C. J. (1978),Annu. Rev. Microbiol. 32, 19–39.PubMedCrossRefGoogle Scholar
  26. 26.
    Rosenberg, M. and Kjelleberg, S. (1987),Adv. Microbial Ecol. 9, 353–393.Google Scholar
  27. 27.
    Sung, L. A. (1983), The interaction ofHelix pomatio andDolichos bifluorus lectins with human group A red blood cells, PhD thesis, Columbia University, New York.Google Scholar
  28. 28.
    Gingell, D. (1990),Biophysics of the Cell Surface, Glaser, R. and Gingell, D., eds., Springer-Verlag, Berlin, pp. 263–286.Google Scholar
  29. 29.
    Gingell, D. and Vince, S. (1982),J. Cell Sci. 54, 255–285.Google Scholar
  30. 30.
    Coakley, W. T. and Gallez, D. (1989),Bioscience Reports 9, 675–671.PubMedCrossRefGoogle Scholar
  31. 31.
    Gallez, D. and Coakley, W. T. (1986),Prog. Biophys. Mol. Biol. 48, 155–199.PubMedCrossRefGoogle Scholar
  32. 32.
    Coakley, W. T., Darmani, H. and Baker, A. (1991),Cell and Model Membrane Interactions, Ohki S., ed., Plenum, New York, in press.Google Scholar
  33. 33.
    Edelman, G. M., Cunningham, B. A., Reeke, G. N. Jr., Becker, J. W., Waxdal, M. J., and Wang, J. L. (1972),Proc. Nat. Acad. Sci. USA 69, 2580–2584.PubMedCrossRefGoogle Scholar
  34. 34.
    Wright, C. S. (1977),J. Mol Biol 111, 439–457.PubMedCrossRefGoogle Scholar
  35. 35.
    Dimitrov, D. S. (1982),Colloid and Polymer Sci. 260, 1137–1144.CrossRefGoogle Scholar

Copyright information

© Humana Press Inc. 1991

Authors and Affiliations

  • Homa Darmani
    • 1
  • W. Terence Coakley
    • 1
  1. 1.School of Pure and Applied BiologyUniversity of Wales College of CardiffCardiffUK

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