SpringerLink
Log in

Alterations in the surface glycoproteins of chicken erythrocytes following transformation with erythroblastosis strain R virus

  • Published:
The Journal of Membrane Biology Aims and scope Submit manuscript

Summary

Erythroblasts from marrows of chicks infected with RNA-virus (strain Rerythroblastosis virus) were found to possess a small but consistent increase in the number of concanavalin A binding sites per cell compared to erythroblasts derived from the marrows of phenylhydrazine-treated birds. Both types of erythroblast possessed more surface glycoproteins per cell accessible to concanavalin A (Con A) than marrow and peripheral blood erythrocytes. Employment of concanavalin A conjugated to ferritin showed marked differences in the spatial arrangement of the Con A receptors between phenylhydrazine and virus-induced erythroblasts but little difference was observed in the surface density of the Con A sites between erythrocytes and erythroblasts, a result which agrees with the amount of bound labeled Con A when this data is expressed in terms of the cell surface.

The amount of labeled Con A bound to erythrocytes derived from the marrow was greater than that derived from the peripheral circulation, a result which is substantiated by the ferritin Con A studies which show an increase in the density of Con A sites on the marrow blood cells. Trypsinization increases the number of sites and the agglutininability of the marrow cells.

The increase in the susceptibility of the cells to agglutinate with concanavalin A paralleled the observed increase in the number of binding sites per cell.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Subscribe and save

Springer+ Basic
EUR 32.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or Ebook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Agrawal, B. B. L., Goldstein, I. J., Hassing, G. S., So, L. L. 1968. Protein-carbohydrate interaction. XVIII. The preparation and properties of acetylated concanavalin A, the hemagglutin of Jack Bean.Biochemistry 7:4211

    PubMed  Google Scholar 

  2. Beaudreau, G. S., Bonar, R. A., Beard, D., Beard, J. W. 1956. Virus of avian erythroblastosis. II. Influence of host age and route of inoculation on dose-response.J. Nat. Cancer Inst. 17:91

    PubMed  Google Scholar 

  3. Burger, M. M., Goldberg, A. R. 1967. Identification of a tumor-specific determinant on neoplastic cell surfaces.Proc. Nat. Acad. Sci. 57:359

    Google Scholar 

  4. Burger, M. M., Martin, G. S. 1972. Agglutination of cells transformed by Rous sarcoma virus by wheat germ agglutinin and concanavalin A.Nature, New Biol. 237:9

    Google Scholar 

  5. Cline, M. J., Livingstone, D. C. 1971. Binding of3H-concanavalin A by normal and transformed cells.Nature, New Biol. 232:155

    Google Scholar 

  6. Gordon, J. A., Sharon, N., Lis, H. 1972. Binding of soybean agglutinin by normal and trypsin-treated red blood cells.Biochim. Biophys. Acta 264:387

    PubMed  Google Scholar 

  7. Inbar, M., Sachs, L. 1969. Structural differences in sites on the surface membrane of normal and transformed cells.Nature 223:710

    PubMed  Google Scholar 

  8. Inbar, M., Sachs, L. 1969. Interaction of the carbohydrate-binding protein concanavalin A with normal and transformed cells.Proc. Nat. Acad. Sci. 63:1418

    PubMed  Google Scholar 

  9. Ishizaki, R., Shimizu, R. 1970. Heterogeneity of strain R avian (erythroblastosis) virus.Cancer Res. 30:2827

    PubMed  Google Scholar 

  10. Kalb, A. J., Levitzki, A. 1968. Metal-binding sites of concanavalin A and their role in the binding of α-methylD-glucopyranoside.Biochem. J. 109:669

    PubMed  Google Scholar 

  11. Kapeller, M., Doljanski, F. 1972. Agglutination of normal and Rous sarcoma virustransformed chick embryo cells by concanavalin A and wheat germ agglutinin.Nature, New Biol. 235:184

    Google Scholar 

  12. Lanfrom, H. 1961. Factors determining the specificity of hemoglobin synthesized in a cell-free system.J. Mol. Biol. 3:241

    PubMed  Google Scholar 

  13. Lehman, E. M., Sheppard, J. R. 1972. Agglutinability by plant lectins increases after RNA virus transformation.Virology 49:339

    PubMed  Google Scholar 

  14. Lucas, A. M., Jamroz, C. 1961. Atlas of Avian Hematology. pp. 22, 183, 200. United States Dept. of Agriculture, Washington, D. C.

    Google Scholar 

  15. Moore, E. G., Temin, H. N. 1971. Lack of correlation between conversion by RNA tumour viruses and increased agglutinability of cells by concanavalin A and wheat germ agglutinin.Nature, New Biol. 231:117

    Google Scholar 

  16. Nicolson, G. L. 1971. Differences in topology of normal and tumour cell membranes shown by different surface distributions of ferritin-conjugated concanavalin A.Nature, New Biol. 233:244

    Google Scholar 

  17. Nicolson, G. L. 1972. Topography of membrane cocanavalin A sites modified by proteolysis.Nature, New Biol. 239:193

    Google Scholar 

  18. Nicolson, G. L., Singer, S. J. 1971. Ferritin-conjugated plant agglutinins as specific saccharide stains for electron microscopy: Application to saccharide bound to cell membranes.Proc. Nat. Acad. Sci. 68:942

    PubMed  Google Scholar 

  19. Ozanne, B., Sambrook, J. 1971. Binding of radioactively labeled concanavalin A and wheat germ agglutinin to normal and virus-transformed cells.Nature, New Biol. 232:156

    Google Scholar 

  20. Post, G., Reeve, P. 1972. Agglutination of normal cells by plant lectins following infection with nononcogenic viruses.Nature, New Biol. 237:113

    Google Scholar 

  21. Reynolds, E. S. 1963. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy.J. Cell Biol. 17:208

    PubMed  Google Scholar 

  22. Shoham, J., Sachs, L. 1972. Differences in the binding of fluorescent concanavalin A to the surface membrane of normal and transformed cells.Proc. Nat. Acad. Sci. 69:2479

    PubMed  Google Scholar 

  23. Staines, R. L., Yamada, E. W. 1970. RNA polymerase activity of erythroblasts isolated from regenerating or erythroblastosis-infected avian bone marrow.Biochim. Biophys. Acta 209:75

    PubMed  Google Scholar 

  24. Weiser, M. W. 1972. Concanavalin A agglutination of intestinal cells from the human fetus.Science 177:525

    PubMed  Google Scholar 

  25. Williams, A. F. 1972. DNA synthesis in purified population of avian erythroid cells.J. Cell Sci. 10:27

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Lady Davis Institute of the Jewish General Hospital, Montreal, Quebec, Canada

    E. Barbarese, H. Sauerwein & H. Simpkins

  2. Department de Biochimie, Faculte de Medicine, Universite de Montreal, Quebec, Canada

    E. Barbarese, H. Sauerwein & H. Simpkins

Authors
  1. E. Barbarese
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. H. Sauerwein
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. H. Simpkins
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Barbarese, E., Sauerwein, H. & Simpkins, H. Alterations in the surface glycoproteins of chicken erythrocytes following transformation with erythroblastosis strain R virus. J. Membrain Biol. 13, 129–142 (1973). https://doi.org/10.1007/BF01868224

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01868224

Keywords

Search

Navigation