Advertisement

Species-specific aggregation factor in sponges

VIII. Nature and alteration of cell surface charge
  • Werner E. G. Müller
  • Rudolf K. Zahn
  • Branco Kurelec
  • Isabel Müller
Article

Summary

Isolated cells from the siliceous spongeGeodia cydonium have been studied with respect to their partition behaviour in a two-phase aqueous polymer system. With this method it is possible to determine subtle changes in the cell surface charge. Addition of a homologous aggregation factor to the isolated cells lowers the partition rate, a finding which indicates that after binding of the aggregation factor to the cells their surface charge is reduced. The partition rate of the cells is strongly correlated with their content of membranebound sialic acid.

Sixty-nine percent of the total, membrane-bound hexuronic acid is associated with the aggregation receptor; 1.8×107 aggregation receptor molecules are present on the surface of one cell which means that the average surface density amounts to 2.8×105 molecules per μm2.

Removal of the aggregation receptor molecules from the cell surface results in a decrease of the partition rate in the two-phase system. After charging the receptor-depleted cells with soluble aggregation receptor, the partition behaviour of these cells can be reconstituted.

Keywords

Surface Charge Sialic Acid Surface Density Polymer System Aggregation Factor 
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.

Abbreviations used

CMF

calcium- and magnesium-free artificial sea water

CMFE

CMF plus EDTA

ASW

calcium- and magnesium-containing artificial sea water

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Albertson, P.A.: Partition of Cell Particles and Macromolecules. New York: Wiley 1972Google Scholar
  2. Avigard, G.: Colorimetric assays for hexuronic acids and some keto sugars.In: Methods in Enzymology (W.A. Wood, ed.) Vol. 41, pp. 29–31. New York: Academic Press 1975Google Scholar
  3. Bolton, A.E., Hunter, W.M.: The labelling of proteins to high specific radioactivity ba conjugation to a125I-containing acylating agent. Biochem. J.133, 529–539 (1973)PubMedGoogle Scholar
  4. Cook, G.M.W., Heard, D.H., Seaman, G.V.F.: Sialic acids and the electrokinetic charge of the human erythrocyte. Nature,191, 44–47 (1961)PubMedGoogle Scholar
  5. Cook, G.M.W., Heard, D.H., Seaman, G.V.F.: The electrokinetic characterisation of the EhrlichAscites carcinoma cells. Exp. Cell Res.,28, 27–39 (1962)PubMedGoogle Scholar
  6. Cuatrecasas, P.: Interaction of wheat germ agglutinin and concanavalin A with isolated fat cells. Biochemistry,12, 1312–1323 (1973)PubMedGoogle Scholar
  7. Curtis, A.S.G.: The cell surface: Its molecular role in morphogenesis. London: Logos Press 1967Google Scholar
  8. Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A., Smith, F.: Colorimetric method for determination of sugars and related substances. Z. anal. Chem.,28, 350–356 (1956)Google Scholar
  9. Kemp, R.B.: The effect of neuraminidase (3:2:1:18) on the aggregation of cells dissociated from embryonic chick muscle tissue. J. Cell Sci.,6, 751–766 (1970)PubMedGoogle Scholar
  10. Kemp, R.B., Lloyd, C.W., Cook, G.M.W.: Glycoproteins in cell adhesion.In: Progress in Surface and Membrane Science (J.F. Danielli et al., ed.) Vol. 7, pp. 271–318. New York: Academic Press 1973Google Scholar
  11. Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurements with the Folin phenol reagent. J. Biol. Chem.193, 265–275 (1951)PubMedGoogle Scholar
  12. McQuiddy, P., Lilien, J.: Sialic acid content and cell aggregation. J. Cell Sci.,9, 823–833 (1971)PubMedGoogle Scholar
  13. Müller, W.E.G., Müller, I., Zahn, R.K.: Two different aggregation principles in reaggregation process of dissociated sponge cells (Geodia cydonium). Experientia30, 899–902 (1974)PubMedGoogle Scholar
  14. Müller, W.E.G., Zahn, R.K.: Purification and characterization of a species-specific aggregation factor in sponges. Exp. Cell Res.80, 95–104 (1973)PubMedGoogle Scholar
  15. Müller, W.E.G., Müller, I., Kurelec, B., Zahn, R.K.: Species-specific aggregation factor in sponges. IV. Inactivation of the aggregation factor by mucoid cells from another species. Exp. Cell Res.98, 31–40 (1976a)PubMedGoogle Scholar
  16. Müller, W.E.G., Müller, I., Zahn, R.K., Kurelec, B.: Species-specific aggregation factor in sponges. VI. Aggregation receptor from the cell surface. J. Cell Sci.,21, 227–241 (1976b)PubMedGoogle Scholar
  17. Müller, W.E.G., Müller, I., Zahn, R.K.: Species-specific aggregation factor in sponges. V. Influence on programmed syntheses. Biochim. Biophys. Acta,418, 217–225 (1976c)PubMedGoogle Scholar
  18. Müller, W.E.G., Müller, I., Zahn, R.K., Kurelec, B.: Speciesspecific aggregation factor in sponges. VII. Effect on cyclic AMP and cyclic GMP metabolism in cells fromGeodia cydonium: Cell and Tiss. Kinet., in press (1977)Google Scholar
  19. Svennerholm, L.: Quantitative estimation of sialic acids. II. A colorimetric resorcinol-hydrochloric acid method. Biochim. Biophys. Acta,24, 604–611 (1957)PubMedGoogle Scholar
  20. Walter, H., Selby, F.W., Garza, R.: On the counter current distribution of red blood cells: An addentum. Biochim. Biophys. Acta136, 148–150 (1967)PubMedGoogle Scholar
  21. Walter, H., Tung, R., Jackson, L.J., Seaman, G.V.F.: The nature of the cell membrane charge measured by partition in aqueous two-polymer phase system: Differentiation of classes of beef erythrocytes. Biochem. Biophys. Res. Commun.48, 565–571 (1972)PubMedGoogle Scholar
  22. Weiss, L.: Studies on cellular adhesion in tissue culture. XIV. Positively charged surface groups and the rate of cell adhesion. Exp. Cell Res.,83, 311–318 (1974)PubMedGoogle Scholar
  23. Zahn, R.K., Müller, W.E.G., Geisert, M., Reinmüller, J., Michaelis, M., Pondeljak, V., Beyer, R.: Species-specific aggregation factor in sponges. I. Characterization of the large circular proteid particle. Cell Differentiation,5, 129–137 (1976)Google Scholar

Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • Werner E. G. Müller
    • 1
    • 2
  • Rudolf K. Zahn
    • 1
    • 2
  • Branco Kurelec
    • 1
    • 2
  • Isabel Müller
    • 1
    • 2
  1. 1.Physiologisch-chemisches InstitutUniversität MainzMainzGermany
  2. 2.Laboratory for Marine Molecular BiologyInstitut Ruder BoškovićRovinjJugoslavia

Personalised recommendations