Advertisement

Oligosaccharide Conformation and the Control of Oligosaccharide Assembly

A Model for Carbohydrate-Mediated Information Transfer
  • Harry Schachter
  • Saroja Narasimhan
  • Noam Harpaz
  • Gregory D. Longmore

Abstract

It is now generally accepted that glycoproteins and glycolipids, members of a large group of macromolecules called complex carbohydrates or glycoconjugates, are important constituents of the mammalian cell membrane. It has also been suggested that the oligosaccharide moieties of cell surface complex carbohydrates serve as probes with which the cell interacts with its environment and through which the environment delivers signals to the interior of the cell (Hughes, 1976; Sharon, 1979; Atkinson and Hakimi, 1980). Cell surface sugars have, in fact, been shown to be present on receptors for viruses, hormones, toxins, interferon, bacteria, and mitogenic lectins; however, in only a limited number of cases has the oligosaccharide moiety itself been proven to be the basis for the recognition signal. A series of phenomena in which sugars obviously must determine recognition are the various biological effects that lectins have on certain cells (Sharon, 1979; Lis and Sharon, 1977), e.g., mitogenic stimulation, agglutination, toxicity, etc. An analogous area of recent research activity has been in the field of “mammalian lectins,” cell surface and intracellular membrane receptors that recognize specific sugar moieties; for example, mammalian hepatocytes have been shown to carry on their surface and on intracellular membranes a receptor for molecules with terminal galactose residues, and human fibroblast lysosomal membranes are believed to carry a receptor that recognizes and binds mannose-6phosphate-containing macromolecules thereby determining the routing of lysosomal hydro-lases to the lysosome (Neufeld and Ashwell, 1980).

Keywords

Elution Pattern Bovine Colostrum GlcNAc Residue Mammalian Cell Membrane Analogous Area 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Atkinson, P. H., and Hakimi, J. (1980). In The Biochemistry of Glycoproteins and Proteoglycans(W. J. Lennarz, ed.), pp. 191–239, Plenum Press, New York.CrossRefGoogle Scholar
  2. Harpaz, N., and Schachter, H. (1980a). J. Biol. Chem. 255, 4885–4893.Google Scholar
  3. Harpaz, N., and Schachter, H. (1980b). J. Biol. Chem. 255, 4894–4902.Google Scholar
  4. Hughes, R. C. (1976). Membrane Glycoproteins. Butterworths, London.Google Scholar
  5. Kornfeld, R., and Kornfeld, S. (1980). In The Biochemistry of Glycoproteins and Proteoglycans(W. J. Lennarz, ed.), pp. 1–34, Plenum Press, New York.CrossRefGoogle Scholar
  6. Lis, H., and Sharon, N. (1977). In The Antigens(M. Sela, ed.), Vol. IV, pp. 429–529, Academic Press, New York.Google Scholar
  7. Longmore, G., and Schachter, H. (1980). Fed. Proc. 39, 2002.Google Scholar
  8. Narasimhan, S., Wilson, J. R., Martin, E., and Schachter, H. (1979). Can. J. Biochem. 57, 83–96.Google Scholar
  9. Narasimhan, S., Harpaz, N., Longmore, G., Carver, J. P., Grey, A. A., and Schachter, H. (1980). J. Biol. Chem. 255, 4876–4884.Google Scholar
  10. Neufeld, E. F., and Ashwell, G. (1980). In The Biochemistry of Glycoproteins and Proteoglycans(W. J. Lennarz, ed.), pp. 241–266, Plenum Press, New York.CrossRefGoogle Scholar
  11. Schachter, H., and Roseman, S. (1980). In The Biochemistry of Glycoproteins and Proteoglycans (W. J. Lennarz, ed.), pp. 85–160, Plenum Press, New York.CrossRefGoogle Scholar
  12. Sharon, N. (1979). In Structure and Function of Biomembranes(K. Yagi, ed.), pp. 63–82, Japan Scientific Societies Press, Tokyo.Google Scholar
  13. Stanley, P. (1980). In The Biochemistry of Glycoproteins and Proteoglycans (W. J. Lennarz, ed.), pp. 161–189, Plenum Press, New York.CrossRefGoogle Scholar
  14. Struck, D. K., and Lennarz, W. J. (1980). In The Biochemistry of Glycoproteins and Proteoglycans (W. J. Lennarz, ed.), pp. 35–83, Plenum Press, New York.CrossRefGoogle Scholar
  15. Takasaki, S. Ikehira, H., and Kobata, A. (1980). Biochem. Biophys. Res. Commun. 92, 735–742.CrossRefGoogle Scholar
  16. Wilson, J. R., Williams, D., and Schachter, H. (1976). Biochem. Biophys. Res. Commun. 72, 909–916.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Harry Schachter
    • 1
    • 2
  • Saroja Narasimhan
    • 1
    • 2
  • Noam Harpaz
    • 1
    • 2
  • Gregory D. Longmore
    • 1
    • 2
  1. 1.Research InstituteHospital for Sick ChildrenTorontoCanada
  2. 2.Department of BiochemistryUniversity of TorontoTorontoCanada

Personalised recommendations