1887

Abstract

SUMMARY

The susceptibility of human leukocyte (α), fibroblast () and recombinant α-2-interferons to clearance by the isolated and perfused rabbit liver has been evaluated. Human leukocyte and recombinant α-2-interferons were stable and their initial levels were maintained in the perfusate even if they had been treated with neuraminidase, thus suggesting that α-interferons have no exposed sugars recognizable by hepatic binding proteins. On the other hand, native, and particularly desialylated human -interferon, underwent marked hepatic uptake confirming the importance of the liver as a catabolic site for glycosylated interferons.

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1982-06-01
2022-01-19
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References

  1. Allen G., Fantes K. H. 1980; A family of structural genes for human lymphoblastoid (leukocyte-type) interferon. Nature, London 287:408–411
    [Google Scholar]
  2. Aminoff D. 1961; Methods for the quantitative estimation of V-acetyl-neuraminic acid and their application to hydrolysates of sialomucoids. Biochemical Journal 81:384–392
    [Google Scholar]
  3. Ashwell G., Morell A. G. 1974; The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Advances in Enzymology 41:99–128
    [Google Scholar]
  4. Baenziger J. V., Maynard Y. 1980; Human hepatic lectin. Journal of Biological Chemistry 255:4607–4613
    [Google Scholar]
  5. Bocci V. 1977; Distribution of interferon in body fluids and tissues. Texas Reports on Biology and Medicine 35:436–441
    [Google Scholar]
  6. Bocci V. 1981; Pharmacokinetic studies of interferons. Pharmacology and Therapeutics 13:421–440
    [Google Scholar]
  7. Bocci V., Viti A., Russi M., Rita G. 1971; Isoelectric fractionation of desialyzed interferon. Experientia 27:1160–1161
    [Google Scholar]
  8. Bocci V., Pacini A., Pessina G. P., Bargigli V., Russi M. 1977a; Metabolism of interferon: hepatic clearance of native and desialylated interferon. Journal of General Virology 35:525–534
    [Google Scholar]
  9. Bocci V., Pacini A., Pessina G. P., Bargigli V., Russi M. 1977b; The role of sialic acid in determining the survival of circulating interferon. Experientia 33:164–165
    [Google Scholar]
  10. Bocci V., Pacini A., Muscettola M., Paulesu L., Pessina G. P. 1981; Renal metabolism of rabbit serum interferon. Journal of General Virology 55:297–304
    [Google Scholar]
  11. Bose S., Hickman J. 1977; Role of the carbohydrate moiety in determining the survival of interferon in the circulation. Journal of Biological Chemistry 252:8336–8337
    [Google Scholar]
  12. Chadha K. C., Grob P. M., Hamill R. L., Sulkowski E. 1980; Glycosylation of human leukocyte interferon: effects of tunicamycin. Archives of Virology 64:109–117
    [Google Scholar]
  13. Finter N. B. 1969; Dye uptake methods for assessing viral cytopathogenicity and their application to interferon assays. Journal of General Virology 5:419–427
    [Google Scholar]
  14. Mogensen K. E., Pyhala L., Torma E., Cantell K. 1974; No evidence for a carbohydrate moiety affecting the clearance of circulating human leukocyte interferon in rabbits. Acta Pathologica et Microbiologica Scandinavica 82:305–310
    [Google Scholar]
  15. Morser J., Kabayo J. P., Hutchinson D. W. 1978; Differences in sialic acid content of human interferons. Journal of General Virology 41:175–178
    [Google Scholar]
  16. Prieels J.-P., Pizzo S. V., Glasgow L. R., Paulson J. C., Hill R. L. 1978; Hepatic receptor that specifically binds oligosaccharides containing fucosyl a l-3 V-acetylglucosamine linkages. Proceedings of the National Academy of Sciences of the United States of America 75:2215–2219
    [Google Scholar]
  17. Rubinstein M., Rubinstein S., Familletti P. C., Miller R. S., Waldman A. A., Pestka S. 1979; Human leukocyte interferon: production, purification to homogeneity, and initial characterization. Proceedings of the National Academy of Sciences of the United States of America 76:640–644
    [Google Scholar]
  18. Schellekens H., De Reus A., Bolhuist R., Fountoulakis M., Schein C., Ecsod1 J., Nagata S., Weissmann C. 1981; Comparative antiviral efficiency of leukocyte and bacterially produced human a-interferon in rhesus monkeys. Nature, London 292:775–776
    [Google Scholar]
  19. Schonne E., Billiau A., De Somer P. 1970; The properties of interferon. IV. Isoelectric focusing of rabbit interferon (NDV-RK13). In Symposia Series in Immunological Standardisation vol 14: pp 61–68 Basel: S. Karger;
    [Google Scholar]
  20. Stewart W. E. Jr 1979 The Interferon System Wien: Springer-Verlag;
    [Google Scholar]
  21. Stockert R. J., Morell A. G., Scheinberg I. H. 1976; The existence of a second route for the transfer of certain glycoproteins from the circulation into the liver. Biochemical and Biophysical Research Communications 68:988–993
    [Google Scholar]
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