The Role of Sialic Acid in the Catabolism of Plasma Glycoproteins

  • Gregory Gregoriadis


The fashion by which glycoproteins or, in general, protein molecules in plasma are eliminated from the circulation and eventually degraded is at present unknown. A vast amount of work on protein turnover, mainly pertaining to albumin, has established that unlike more complicated organized structures (i.e., cells) proteins have no definite life span and each protein molecule, regardless of age, has statistically the same chance of being eliminated.1


Sialic Acid Enzyme Replacement Therapy Hepatic Uptake Sialic Acid Residue Liver Cell Membrane 
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  1. 1.
    H. E. Schultze and J. F. Heremans, Molecular Biology of Human Proteins, Vol. 1 (Elsevier Publ. Co., Amsterdam, 1966), p. 450.Google Scholar
  2. 2.
    S. B. Anderson, J. Glenert, and K. Wallevik, Protides of the Biological Fluids, Proc. 11th Colloq., Bruges, 1963 (Elsevier Publ. Co., Amsterdam, 1964), p. 272.Google Scholar
  3. 3.
    T. Freeman, Protides Biol. Fluids, Proc. Colloq., 15, 1 (1968).Google Scholar
  4. 4.
    R. Engler, J. Moretti, and M. F. Jayle, Bull. Soc. Chim. Biol., 49, 263 (1967).PubMedGoogle Scholar
  5. 5.
    U. Muller-Eberhard, New England J. Med., 283, 1090 (1970).CrossRefGoogle Scholar
  6. 6.
    A. C. Allison, Nature, 188, 37 (1960).PubMedCrossRefGoogle Scholar
  7. 7.
    I. M. Spector, Nature, 249, 66 (1974).PubMedCrossRefGoogle Scholar
  8. 8.
    J. Katz, S. Rosenfeld, and A. L. Sellers, Amer. J. Physiol., 200, 1301 (1961).PubMedGoogle Scholar
  9. 9.
    A. G. Morell, G. Gregoriadis, I. H. Scheinberg, J. Hickman, and G. Ashwell, J. Biol. Chem., 246, 1461 (1971).PubMedGoogle Scholar
  10. 10.
    G. Gregoriadis, Lysosomes in Biology and Pathology, Vol. 4, p. 265. (North Holland Publ. Co., Amsterdam (1975).Google Scholar
  11. 11.
    A. G. Morell, R. A. Irvine, I. Sternlieb, I. H. Scheinberg, and G. Ashwell, J. Biol. Chem., 243, 155 (1968).PubMedGoogle Scholar
  12. 12.
    P. Aisen, A. G. Morell, S. Alpert, and I. Sternlieb, Nature, 203, 873 (1964).PubMedCrossRefGoogle Scholar
  13. 13.
    C. J. A. Van Den Hamer, A. G. Morell, I. H. Scheinberg, J. Hickman, and G. Ashwell, J. Biol. Chem., 245, 4397 (1970).Google Scholar
  14. 14.
    G. L. Nelsestuen and J. W. Suttie, Biochem. Biophys. Res. Commun., 45, 198 (1971).PubMedCrossRefGoogle Scholar
  15. 15.
    W. A. Lukowsky and R. H. Painter, Can. J. Biochem., 50, 909 (1972).PubMedCrossRefGoogle Scholar
  16. 16.
    W. H. Yang and H. Parkoff, Fertility and Sterility, 24, 633 (1973).PubMedGoogle Scholar
  17. 17.
    H. Van Baelen and G. Mannaerts, Arch. Biochem. Biophys., 163, 53 (1974).PubMedCrossRefGoogle Scholar
  18. 18.
    J. S. Marshall, A. M. Green, J. Pensky, S. Williams, A. Zinn, and D. M. Carlson, J. Clin. Invest., 54, 555 (1974).PubMedCrossRefGoogle Scholar
  19. 19.
    E. Regoeczi and M. W. C. Hatton (eds., R. Bianchi, G. Mariani, and A. S. M. McFarlane), Plasma Protein Turnover, p. 133 (MacMillan, London, 1976).Google Scholar
  20. 20.
    G. Gregoriadis, D. Putman, L. Louis, and E. D. Neerunjun, Biochem. J., 140, 323 (1974).PubMedGoogle Scholar
  21. 21.
    C. L. Schengrund, D. S. Jensen, and A. Rosenberg, J. Biol. Chem., 247, 2742 (1972).PubMedGoogle Scholar
  22. 22.
    A. Visser and P. Emmelot, J. Membrane Biol., 14, 73 (1973).CrossRefGoogle Scholar
  23. 23.
    W. E. Pricer, Jr., and G. Ashwell, J. Biol. Chem., 246, 4825 (1971).PubMedGoogle Scholar
  24. 24.
    A. G. Morell and I. H. Scheinberg, Biochem. Biophys. Res. Commun., 48, 808 (1972).PubMedCrossRefGoogle Scholar
  25. 25.
    R. L. Hudgin, W. E. Pricer, Jr., G. Ashwell, R. J. Stockert, and A. G. Morell, J. Biol. Chem., 249, 5536 (1974).PubMedGoogle Scholar
  26. 26.
    N. N. Aronson, Jr., L. Y. Tan, and B. P. Peters, Biochem. Biophys. Res. Commun. 53, 112 (1973).PubMedCrossRefGoogle Scholar
  27. 27.
    G. Gregoriadis, A. G. Morell, I. Sternlieb, and I. H. Scheinberg, J. Biol. Chem., 245: 5833 (1970).PubMedGoogle Scholar
  28. 28.
    R. Wattiaux, M. Wibo, and P. Baudhuin, Arch. Int. Physiol. Biochem., 71, 140 (1963).Google Scholar
  29. 29.
    P. Baudhuin, H. Beaufay, and C. De Duve, J. Cell Biol., 26, 219 (1965).PubMedCrossRefGoogle Scholar
  30. 30.
    A. H. Gordon (ed., J. T. Dingle), Lysosomes in Biology and Pathology, p. 89. (North Holland Publ. Co., Amsterdam, 1973).Google Scholar
  31. 31.
    J. S. Marshall, A. M. Green, J. Pensky, S. Williams, A. Zinn, and D. M. Carlson, J. Clin. Invest., 54, 555 (1974).PubMedCrossRefGoogle Scholar
  32. 32.
    M. Eliakim, A. Zlotnick, and S. Slavin, Progr. Liver Dis. 4, 403 (1972).PubMedGoogle Scholar
  33. 33.
    N. N. Aronson, Jr, and C. De Duve, J. Biol. Chem., 243, 4564 (1968).PubMedGoogle Scholar
  34. 34.
    T. J. Langley, Arch. Biochem. Biophys., 128, 304 (1968).PubMedCrossRefGoogle Scholar
  35. 35.
    S. Mahadevan and A. L. Tappel, Arch. Biochem. Biophys., 128, 129 (1968).PubMedCrossRefGoogle Scholar
  36. 36.
    R. D. Marshall, Ann. Rev. Biochem., 41, 673 (1972).PubMedCrossRefGoogle Scholar
  37. 37.
    P. A. Öckerman, Lancet, 2, 239 (1967).CrossRefGoogle Scholar
  38. 38.
    S. Okada and J. S. O’Brien, Science, 160, 1002 (1968).PubMedCrossRefGoogle Scholar
  39. 39.
    M. C. MacBrinn, S. Okada, M. W. Ho, C. C. Hu, and J. S. O’Brien, Science, 163, 946 (1969).PubMedCrossRefGoogle Scholar
  40. 40.
    K. O. Raivio and J. E. Seegmiller, Ann. Rev. Biochem., 41, 543 (1972).PubMedCrossRefGoogle Scholar
  41. 41.
    G. Hug, W. K. Schubert, and G. Chuck, Clin. Res., 16, 345 (1968).Google Scholar
  42. 42.
    R. M. Lauer, T. Mascarinas, A. S. Racela, A. M. Diehl, and B. I. Brown, Pediatrics 42, 672 (1968).PubMedGoogle Scholar
  43. 43.
    C. A. Mapes, R. L. Anderson, C. C. Sweeley, R. J. Desnick, and W. Krivit, Science 169, 987 (1970).PubMedCrossRefGoogle Scholar
  44. 44.
    A. G. Knudson Jr., N. Diferrante, and J. E. Curtis, Proc. Nat. Acad. Sci. U.S.A., 68, 1738 (1971).CrossRefGoogle Scholar
  45. 45.
    R. O. Brady, J. F. Tallman, W. G. Johnson, A. E. Gal, W. R. Leahy, J. M. Quirk, and A. S. Dekaban, New England J. Med., 289, 9 (1973).CrossRefGoogle Scholar
  46. 46.
    R. O. Brady, P. G. Pentchev, A. E. Gal, S. R. Hibbert, and A. S. Dekaban, New England J. Med., 291, 989 (1974).CrossRefGoogle Scholar
  47. 47.
    G. Gregoriadis (eds., J. M. Tager, G. J. M. Hooghwinkel, W. T. Daems), Enzyme Therapy in Lysosomal Storage Diseases p. 131 (North Holland Publ. Co., Amsterdam, Oxford; American Elsevier Publ. Co., New York, 1974).Google Scholar
  48. 48.
    G. Gregoriadis and A. C. Allison, Febs Lett., 45, 71 (1974).PubMedCrossRefGoogle Scholar
  49. 49.
    G. Gregoriadis and E. D. Neerunjun, Biochem. Biophys. Res. Comm. 65, 537 (1975).PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Gregory Gregoriadis
    • 1
  1. 1.Clinical Research CentreHarrow, MiddlesexUK

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