, Volume 32, Issue 2, pp 135–140 | Cite as

The role of sialic acid in determining the life-span of circulating cells and glycoproteins

  • V. Bocci


The role of sialic acid in determining the life of circulating cells and glycoproteins is reviewed and an attempt is made to assess its real importance and to interpret the desialylation pathway. An overall view of factors, including desialylated glycoprotein fragments, that may regulate hepatic synthesis of glycoproteins is presented.


Sialic Acid Hepatic Synthesis Real Importance Glycoprotein Fragment 


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  1. 1.
    S. Roseman, Chem. Phys. Lipids,5, 270 (1970).PubMedGoogle Scholar
  2. 2.
    P. J. Winterburn andC. F. Phelps, Nature, Lond.236, 147 (1972).Google Scholar
  3. 3.
    G. Ashwell andA. G. Morell, inAdvances in Enzymology (Ed.A. Meister; J. Wiley, New York 1974), vol. 41, p. 99.Google Scholar
  4. 4.
    W. E. Pricer Jr. andG. Ashwell, J. biol. Chem.246, 4825 (1971).PubMedGoogle Scholar
  5. 5.
    V. Bocci, Experientia24, 626 (1968).PubMedGoogle Scholar
  6. 6.
    V. Bocci, G. P. Pessina andT. Conti,Protides of the Biological Fluids, 21st Colloq. (Ed.H. Peeters; Pergamon Press, Oxford 1973), p. 49.Google Scholar
  7. 7.
    C. Balduini, C. L. Balduini, A. A. Castellani andE. Storti, Boll. Soc. ital. Biol. sper.48, Abstract 65 (1972).Google Scholar
  8. 8.
    W. B. Stewart, C. W. Petenyi andH. M. Rose, Blood10, 228 (1955).PubMedGoogle Scholar
  9. 9.
    E. Gardner Jr., C.-S. Wright andB. Z. Williams, J. Lab. clin. Med.58, 743 (1961).PubMedGoogle Scholar
  10. 10.
    J. Jancik andR. Schauer, Hoppe-Seyler's Z. physiol. Chem.355, 395 (1974).PubMedGoogle Scholar
  11. 11.
    J. R. Durocher, R. C. Payne andM. E. Conrad, Blood45, 11 (1975).PubMedGoogle Scholar
  12. 12.
    P. Lalezari andH. Mendhiry, Br. J. Haemat.25, 399 (1973).Google Scholar
  13. 13.
    S.-I. Choi, J. V. Simone andL. J. Journey, Br. J. Haemat.22, 93 (1972).Google Scholar
  14. 14.
    K. A. Grottum andM. Jeremic, Thromb. Diath. haemorrh.29, 461 (1973).PubMedGoogle Scholar
  15. 15.
    E. Skutelsky andD. Danon, J. Cell Biol.43, 8 (1969).PubMedGoogle Scholar
  16. 16.
    S. N. Berney andB. M. Gesner, Immunology18, 681 (1970).PubMedGoogle Scholar
  17. 17.
    J. J. Woodruff andB. M. Gesner, J. exp. Med.129, 551 (1969).PubMedGoogle Scholar
  18. 18.
    R. L. Hudgin, W. E. Pricer Jr., G.Ashwell, R. J. Stockert andA. G. Morell, J. biol. Chem.249, 5536 (1974).PubMedGoogle Scholar
  19. 19.
    R. J. Stockert, A. G. Morell andI. H. Scheinberg, Science186, 365 (1974).PubMedGoogle Scholar
  20. 20.
    A. G. Morell, R. A. Irvine, I. Sternlieb, I. H. Scheinberg andG. Ashwell, J. biol. Chem.243, 155 (1968).PubMedGoogle Scholar
  21. 21.
    G. Gregoriadis, A. G. Morell, I. Sternlieb andI. H. Scheinberg, J. biol. Chem.245, 5833 (1970).PubMedGoogle Scholar
  22. 22.
    C. J. A. van den Hamer, A. G. Morell, I. H. Scheinberg, T. Hickman andG. Ashwell, J. biol. Chem.245, 4397 (1970).PubMedGoogle Scholar
  23. 23.
    A. G. Morell, G. Gregoriadis, I. H. Scheinberg, J. Hickman andG. Ashwell, J. biol. Chem.246, 1461 (1971).PubMedGoogle Scholar
  24. 24.
    W. H. Yang andH. Papkoff, Fert. Steril.24, 633 (1973).Google Scholar
  25. 25.
    G. L. Nelsestuen andJ. W. Suttie, Biochem. biophys. Res. Commun.45, 198 (1971).PubMedGoogle Scholar
  26. 26.
    J. S. Marshall, A. M. Green, J. Pensky, S. Williams, A. Zinn andD. M. Carlson, J. clin. Invest.54, 555 (1974).PubMedGoogle Scholar
  27. 27.
    D. W. Briggs, J. W. Fisher andW. J. George, Am. J. Physiol.227, 1385 (1974).PubMedGoogle Scholar
  28. 28.
    H. van Baelen andG. Mannaerts, Arch. Biochem. Biophys.163, 53 (1974).PubMedGoogle Scholar
  29. 29.
    E. Regoeczi, M. W. C. Hatton andK.-L. Wong, Can. J. Biochem.52, 155 (1974).PubMedGoogle Scholar
  30. 30.
    K.-L. Wong, P. A. Charlwood, M. W. C. Hatton andE. Regoeczi, Clin. Sc. molec. Med.46, 763 (1974).Google Scholar
  31. 31.
    M. W. C. Hatton, E. Regoeczi andK.-L. Wong, Can J. Biochem.52, 845 (1974).PubMedGoogle Scholar
  32. 32.
    W. C. Parker andA. G. Bearn, J. exp. Med.115, 83 (1962).PubMedGoogle Scholar
  33. 33.
    T. Bücher, D. Matzelt andD. Pette, Klin. Wschr.30, 325 (1952).PubMedGoogle Scholar
  34. 34.
    E. C. Laterre, Ricerca Clin. Lab.3, 736 (1973).Google Scholar
  35. 35.
    J. Clausen, T. Munkner, Nature, Lond.189, 60 (1961).Google Scholar
  36. 36.
    G. P. Pessina, L. Paulesu, P. Pessina andV. Bocci, Boll. Soc. ital. Biol. sper.51, 75 (1975).PubMedGoogle Scholar
  37. 37.
    V. Bocci, Archo Fisiol.67, 314 (1970).Google Scholar
  38. 38.
    R. J. Winzler andV. Bocci,Glycoproteins., Part B (Ed.A. Gottschalk (Elsevier, Amsterdam 1972), p. 1228.Google Scholar
  39. 39.
    R. K. Murray, G. E. Connell andJ. H. Pert, Blood17, 45 (1961).PubMedGoogle Scholar
  40. 40.
    R. Engler, J. Moretti andM. F. Jayle, Bull. Soc. Chim. biol.49, 263 (1967).PubMedGoogle Scholar
  41. 41.
    T. Wada, H. Ohara, K Watanabe, H. Kinoshita andH. Nishio, J. reticuloendoth. Soc.8, 185 (1970).Google Scholar
  42. 42.
    T. Freeman,Protides of the Biological Fluids, 15 Colloq. (Ed.H. Peeters; Elsevier, Amsterdam 1968), p. 1.Google Scholar
  43. 43.
    L. Mester, inFibrinogen (Ed.K. Laki; Dekker, New York 1968), p. 165.Google Scholar
  44. 44.
    M. W. Mosesson, Thromb. Res.2, 185 (1973).Google Scholar
  45. 45.
    E. Regoeczi andK.-L. Wong,Protein Turnover, Ciba Foundation Symposium 9 (ASP, Amsterdam 1973), p. 181.Google Scholar
  46. 46.
    G. P. Pessina, T. Conti, A. Pacini andV. Bocci, Ital. J. Biochem.21, 155 (1972).PubMedGoogle Scholar
  47. 47.
    A. Bezkorovainy, Physiol. Chem. Phys.4, 492 (1972).PubMedGoogle Scholar
  48. 48.
    R. J. Carrico, H. F. Deutsch, H. Beinert andW. H. Orme-Johnson, J. biol. Chem.244, 4141 (1969).PubMedGoogle Scholar
  49. 49.
    N. A. Holtzman andB. M. Gaumnitz J. biol. Chem.245, 2350 (1970).PubMedGoogle Scholar
  50. 50.
    N. A. Azari andR. E. Feeney, J. biol. Chem.245, 2354 (1970).PubMedGoogle Scholar
  51. 51.
    P. R. Azari andR. E. Feeney, J. biol. Chem.232, 293 (1958).PubMedGoogle Scholar
  52. 52.
    J. W. Drysdale andH. N. Munro, J. biol. Chem.241, 3630 (1966).PubMedGoogle Scholar
  53. 53.
    H. Rinderknecht andM. C. Geokas, Biochim. biophys Acta295, 233 (1973).PubMedGoogle Scholar
  54. 54.
    N. Heimburger K. Heide, H. Haupt andH. E. Schultze, Clin. chim. Acta10, 293 (1964).PubMedGoogle Scholar
  55. 55.
    L. van Lenten andG. Ashwell, J. biol. Chem.247, 4633 (1972).PubMedGoogle Scholar
  56. 56.
    K. Schmid, J. F. Burke, M. Debray-Sachs andK. Tokita, Nature, Lond.204, 75 (1964).Google Scholar
  57. 57.
    R. Carubelli, R. E. Trucco andR. Caputto, Biochim. biophys. Acta60, 196 (1962).PubMedGoogle Scholar
  58. 58.
    S. Mahadevan, J. C. Nduaguba andA. L. Tappel, J. biol. Chem.242, 4409 (1967).PubMedGoogle Scholar
  59. 59.
    R. Ohman, A. Rosenberg andL. Svennerholm, Biochemistry9, 3774 (1970).PubMedGoogle Scholar
  60. 60.
    N. K. Ghosh, L. Kotowitz andW. H. Fishman, Biochim. biophys. Acta167, 201 (1968).PubMedGoogle Scholar
  61. 61.
    G. P. Pessina andV. Bocci, Boll. Soc. ital. Biol. sper.50, 1201 (1974).PubMedGoogle Scholar
  62. 62.
    G. P. Pessina andV. Bocci, Boll. Soc. ital. Biol. sper.50, 1194 (1974).PubMedGoogle Scholar
  63. 63.
    W. Gielen andR. Schaper, Hoppe-Seyler's Z. physiol. Chem.355, 660 (1974).PubMedGoogle Scholar
  64. 64.
    P. N. Srivastava, L. J. D. Zaneveld andW. L. Williams, Biochem. biophys. Res. Commun.39, 575 (1970).PubMedGoogle Scholar
  65. 65.
    V. Unbehaun, Hoppe Seyler's Z. physiol. Chem.351, 705 (1970).PubMedGoogle Scholar
  66. 66.
    L. Warren andC. W. Spearing. Biochem. biophys. Res. Commun.3, 489 (1960).PubMedGoogle Scholar
  67. 67.
    C. A. Owen Jr., A. L. Orvis andJ. M. Kiely, Am. J. Physiol.211, 273 (1966).PubMedGoogle Scholar
  68. 68.
    J. Sorbie andL. S. Valberg, Am. J. Physiol.218, 647 (1970).PubMedGoogle Scholar
  69. 69.
    S. H. Song andA. C. Groom, Am. J. Physiol.220, 779 (1971).PubMedGoogle Scholar
  70. 70.
    P. F. Marton, Scand. J. Haemat.7, 177 (1970).PubMedGoogle Scholar
  71. 71.
    P. F. Marton, Scand. J. Haemat.10, 81 (1973).PubMedGoogle Scholar
  72. 72.
    L. Weiss, Am. J. Anat.111, 131 (1962).PubMedGoogle Scholar
  73. 73.
    G. Gregoriadis, D. Putman, L. Louis andD. Neerunjun, Biochem. J.140, 323 (1974).PubMedGoogle Scholar
  74. 74.
    H. F. Grundy, J. Physiol.163, 457 (1962).PubMedGoogle Scholar
  75. 75.
    L. E. McCarthy andH. L. Borison, Expl. Neurol.17, 57 (1967).Google Scholar
  76. 76.
    P. McQuiddy andJ. E. Lilien, Biochim. biophys. Acat291, 774 (1973).Google Scholar
  77. 77.
    P. Sachtleben, R. Gsell andJ. N. Mehrishi, Vox sang.25, 519 (1973).PubMedGoogle Scholar
  78. 78.
    A. C. Allison, Nature, Lond.188, 37 (1960).Google Scholar
  79. 79.
    J. E. Bourdeau andF. A. Carone, Nephron13, 22 (1974).PubMedGoogle Scholar
  80. 80.
    C.-S. Wright, M. C. Dodd, J. A. Bass andN. G. Brandt, Anat. Rec.115, 457 (1953).Google Scholar
  81. 81.
    A. Lee, Proc. Soc. exp. Biol. Med.128, 891 (1968).PubMedGoogle Scholar
  82. 82.
    M. H. Knisely, Anat. Res.65, 131 (1936).Google Scholar
  83. 83.
    M. Bessis,Corpuscles (Springer-Verlag, Berlin 1974).Google Scholar
  84. 84.
    D. M. Bissell, L. Hammaker andR. Schmid, J. Cell Biol.54, 107 (1972).PubMedGoogle Scholar
  85. 85.
    S. Goldfischer, A. B. Novikoff, A. Albala andL. Biempica, J. Cell Biol.44, 513 (1970).PubMedGoogle Scholar
  86. 86.
    D. M. Bissell, L. Hammaker andR. Schmid, Blood40, 312 (1972).Google Scholar
  87. 87.
    H. Gans andJ. T. Lowman, Blood29, 526 (1967).PubMedGoogle Scholar
  88. 88.
    M. J. Barnhart, D. C. Cress, S. M. Noonan andR. T. Walsh, inFibrinogen: Structural metabolic and Pathophysiologic Aspects (Eds.P. A. Owren, K. M. Brinkhous, I. S. Wright, H. R. Roberts, S. Hinnom andT. H. Kiesselbach; F. K. Schattauer Verlag, Stuttgart 1970), p. 143.Google Scholar
  89. 89.
    V. Bocci andA. Pacini, Thromb. Diath. haemorrh.29, 63 (1973).PubMedGoogle Scholar
  90. 90.
    V. Bocci, T. Conti, M. Muscettola, A. Pacini andG. P. Pessina, Thromb. Diath. haemorrh.31, 395 (1974).PubMedGoogle Scholar
  91. 91.
    P. T. Otis andS. I. Rapaport, Proc. Soc. exp. Biol. Med.144, 124 (1973).PubMedGoogle Scholar
  92. 92.
    K. N. Jeejeebhoy A. Bruce-Robertson, U. Sodtke andM. Foley, Biochem. J.119, 243 (1970).PubMedGoogle Scholar
  93. 93.
    A. C. Atencio andL. Lorand, Am. J. Physiol.219, 1161 (1970).PubMedGoogle Scholar
  94. 94.
    K. N. Jeejeebhoy, A. Bruce-Robertson, J. Ho andU. Sodtke, Biochem. J.130, 533 (1972).PubMedGoogle Scholar
  95. 95.
    E. E. Griffin andL. L. Miller, J. biol. Chem.249, 5062 (1974).PubMedGoogle Scholar
  96. 96.
    R. S. Pekarek, R. W. Wannemacher Jr., F. E. Chapple, M. C. Powanda andW. R. Beisel, Proc. Soc. exp. Biol. Med.141, 643 (1972).PubMedGoogle Scholar
  97. 97.
    R. F. Kampschmidt, L. A. Pulliam andH. F. Upchurch, Proc. Soc. exp. Biol. Med.144, 882 (1973).PubMedGoogle Scholar
  98. 98.
    R. F. Kampschmidt andH. F. Upchurch, Proc. Soc. exp. Biol. Med.146, 904 (1974).PubMedGoogle Scholar
  99. 99.
    D. M. Moore, P. A. Murphy, P. J. Chesney andW. S. Wood, J. exp. Med.137, 1263 (1973).PubMedGoogle Scholar
  100. 100.
    A. Pacini, G. P. Pessina, M. Muscettola andV. Bocci, Boll. Soc. ital. Biol. sper.49, 18, Abstract 78 (1973).Google Scholar
  101. 101.
    D. A. Darcy, Br. J. exp. Path.49, 525 (1968).Google Scholar

Copyright information

© Birkhäuser Verlag 1976

Authors and Affiliations

  • V. Bocci
    • 1
  1. 1.Istituto di Fisiologia GeneraleUniversità di SienaSienaItaly

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