Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Investigation of malignancy-related glycopeptides and their releasein vitro andin vivo from ascites tumour cells

  • 9 Accesses

  • 1 Citations

Summary

LANDSCHÜTZ mouse ascites tumour cells contain trypsin-sensitive fucopeptides similar to those known in other tumour cell types to be closely related to malignancy. These components were found not to be released from the cellsIn vitro unless trypsin was present. They were, however, spontaneously shed from the tumourin vivo into ascitic fluid within 24 h. Comparison of cellular and released fucopeptides showed that the components releasedin vitro andin vivo represented a specific population of cellular fucopeptides. The action of trypsin in releasing these entitiesin vitro was found to be the sum of several small changes involving various fucopeptide species, mainly of intermediate size and charge. Trypsin-inducedin vitro release and spontaneous releasein vivo involved slightly different proportions of individual fucopeptide species.

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

References

  1. Black, P. 1980. Shedding from the cell surface of normal and cancer cells. Adv. Cancer Res. 32, 75–199.

  2. Baumann, H. and Eldredge, D. 1982. Influence of the liver on the profile of circulating antigens recognised by antiserum against hepatoma membrane glycoproteins. Cancer Res. 42, 2398–2406.

  3. Cossu, G., Warren, L., Boetigger, D., Holtzer, H. and Pacifici, M. 1982. Similar glycopeptides in normal chondroblasts and in Rous Sarcomatransformed fibroblasts. J. Biol. Chem. 257, 4463–4468.

  4. Dubois, M., Gillies, K. A., Hamilton, J. K., Rebers, P. A., and Smith, F. 1956. Colorimetric method for the determination of sugars and related substances. Anal. Chem. 28, 350–356.

  5. Geurts Van Kessel, A. H., Smets, L. A., Van Rooy, H. and Hagemeijer, A. 1981. Expression of chronic myeloid leukaemia-associated changes in membrane glycopeptides in somatic cell hybrids. J. Cell Sci. 51, 121–130.

  6. Glick, M. C., Kimhi, Y. and Littauer, U. Z. 1973. Glycopeptides from suaface membranes of neuroblastoma cells. Proc. Nat. Acad. Sci. (USA). 70, 1682–1687.

  7. Hammond, K. S. and Papermaster, D. S. 1976. Fluorimetric assay of sialic acid in the picomole range: a modificaton of the thiobarbituric acid assay. Anal. Biochem. 74, 292–297.

  8. Ogata, S., Muramatsu, T. and Kobata, A. 1976. New structural characteristic of the large glycopeptides from transformed cells. Nature (Lond.) 259, 580–582.

  9. Rachesky, M. H., Hard, G. C. and Glick, M. C. 1982. Membrane glycopeptides from chemically transformed cells: comparison between mesenchymal and epithelial cell lines derived from dimethylnitrosamine-treated rat kidney. Cancer Res. 42, 39–43.

  10. Santer, U. V. and Glick, M. C. 1979. Partial structure of a membrane glycopeptide from virustransformed hamster cells. Biochemistry 18, 2533–2540.

  11. Smets, L. A., Enniga, I. C. and Van Rooy, H. 1982. Cell communication reduced by changes in cell surface carbohydrates. Exp. Cell Res. 139, 181–189.

  12. Smith, T. C. and Levinson, C. 1979. Ehrlich ascites tumour cell surface labelling and kinetics of glycocalyx release. J. Supramol. Struct. 12, 115–125.

  13. Takasaki, S., Ikehira, H. and Kobata, A. 1980. Increase of asparagine-linked oligosaccharides with branched outer chains caused by cell transformation. Biochem. Biophys. Res. Comm. 92, 735–742.

  14. Van Beek, W. P., Smets, L. A. and Emmelot, P. 1973. Increased sialic acid density in surface glycoproteins of transformed and malignant cells; a general phenomenon? Cancer Res. 33, 2913–2922.

  15. Van Beek, W. P., Breekveldt, J. P., Bakker, E., Hilgers, J., Hilgers, F. and Nilsson, K. 1981. Early changes in the glycopeptides of human B lymphocytes after Epstein-Barr virus infectionin vitro. Int. J. Cancer 27, 23–28.

  16. Van Beek, W. P., Tulp, A., Egbers-Bogaards, M., Roozendaal, K. J. and Smets, L. A. 1982. Continuous expression of cancer-related fucosyl glycopeptides on the surface of human promyelocyte leukaemia cells (HL-60) following terminal differentiationin vitro. Cancer Res. 42, 5222–5230.

  17. Van Beek, W. P., Vernole, P. and Neri, G. 1983. Appearance of altered cell surface fucosyl glycopeptides in concomitance with chromosomal alterations in the Gross virus-infected pre-leukaemic thymus of the rat. Eur. J. Cancer Clin. Oncol. 19, 555–559.

  18. Van Blitterswijk, W. J., Hilgers, J., Feltkamp, C. A. and Emmelot, P. 1981. Mammary tumour virus expression and dynamics in the cell surface.In: Mammary Tumours in the Mouse. (Hilgers and Sluyser, eds.) Ch. 14. Elsevier/North Holland Biomedical Press, Amsterdam.

  19. Van Blitterswijk, W. P., De Veer, G., Krol, J. H. and Emmelot, P. 1982. Comparative lipid analysis of purified plasma membranes and shed extracellular membrane vesicles from normal murine thymocytes and leukaemic GRSL cells. Biochim. Biophys. Acta. 688, 495–504.

  20. Van Halbeek, H., Van Beek, W. P., Blanked-Aarsen, G. J. and Vliegenthart, J. F. G. 1983. Investigation of the structural alterations of the carbohydrate chains of cell surface glycoproteins in relation to malignant cell transformation. Proc. 7th Int. Symp. on Glycoconjugates (M. A. Chesteret al, eds.), Lund, Sweden, pp. 864–865.

  21. Van Nest, V. A. and Grimes, W. J. 1977. A comparison of the membrane composition of normal and malignancy transformed balb/c cells. Biochemistry. 16, 2902–2908.

  22. Walsh, E., O’Kennedy, R. and Smyth, H. 1980. Some characteristics of the trypsin-sensitive glycoproteins from Landschutz ascites tumour cells, Ir. J. Med. Sci. 149, 79.

  23. Walsh, E., Smyth, H. and Corrigan, A. 1982. Tumour-related membrane carbohydrate components: condtions of release from ascites tumour cellsin vivo andin vitro. Ir. J. Med. Sci. 151, 133.

  24. Walsh, E., Smyth, H., Corrigan, A. and O’Kennedy, R., 1983. Examination of the role of trypsin in the release of malignancy-related glycopeptides from cells. Proc. 7th Int. Symp. on Glycoconjugates (M. A. Chesteret al, eds.), Lund, Sweden. 887–888.

  25. Warren, L., Fuhrer, J. P. and Buck, C. A. 1972. Surface glycoproteins of normal and transformed cells: a difference determined by sialic acid and a growth-dependent sialyl transferase. Proc. Nat. Acad. Sci. (USA). 69, 1838–1842.

  26. Warren, L., Buck, C. A. and Tushynski, G. P. 1978. Glycopeptide changes and malignant transformation: a possible role for carbohydrate in malignant behaviour. Biochim. Biophys. Acta. 516, 97–127.

  27. Warren, L. and Buck, C. A. 1980. The membrane glycoproteins of the malignant cell. Clin. Biochem. 13(5), 191–197.

Download references

Author information

Correspondence to E. Walsh or H. Smyth or A. Corrigan.

Additional information

We are grateful to The Medical Research council of Ireland for financial support for this project, Dr. M. L. Conalty and staff of the M.R.C. Laboratories, trinity Colletge, Dublin for supplying tumour mice, and Drs. R. O’Kennedy and M. Clynes, N.I.H.E.,Dublin for helpful comments.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Walsh, E., Smyth, H. & Corrigan, A. Investigation of malignancy-related glycopeptides and their releasein vitro andin vivo from ascites tumour cells. I.J.M.S. 154, 292–305 (1985). https://doi.org/10.1007/BF02937168

Download citation

Keywords

  • Sialic Acid
  • Hexose
  • Glycopeptide
  • Fucose
  • Ascitic Fluid