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Restricted variation in the glycosylation of human α1-acid glycoprotein

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Summary

The glycosylation patterns of multiglycosylated proteins reflect both the cellular control of glycosyl transferase activity and the local control of the transfer event. Little information is available concerning these mechanisms. Changes in glycosylation occur in the disease state and provide a convenient way of examining the control mechanism(s) operating at individual glycosylation sites. Chromatographic methods have been applied to the human orosomucoid (OMD) isolated from seventeen different pathologies. Based on the distribution of the glycans at the individual sites it is clear that the major protein-glycan interactions that restrict glycosylation in “normal” OMD remain intact in the disease state in the presence of changing glycosyl transferase activity.

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References

  1. S. Pervaiz, K. Brew, FASEB J.1, 209 (1987).

    Google Scholar 

  2. J. Pevsner, R. Reed, P. Feinstein, S. Snyder, Science241, 336 (1988).

    Google Scholar 

  3. Alpha1-acid glycoprotein: genetics, biochemistry, physiological functions and pharmacology. Baumann P., Eap C., Müller W., Tillement J-P., eds. Alan R. Liss, New York.

  4. M. J. Treuheit, C. Costello, H. B. Halsall, Biochem. J.283, 105 (1992).

    Google Scholar 

  5. M. J. Treuheit, H. B. Halsall, Chromatographia31, 478 (1991).

    Google Scholar 

  6. M.-G. Yet, M-C. Shao, FASEB J.2, 22 (1988).

    Google Scholar 

  7. N. Dahms, G. Hart, J. Biol. Chem.261, 13186 (1986).

    Google Scholar 

  8. J. Carver, D. Cummings, Pure and Appl. Chem.59, 1465 (1987).

    Google Scholar 

  9. E. Wooten, R. Bazzo, C. Edge, R. Dwek, T. Rademacher, Eur. Biophys. J.18, 139 (1990).

    Google Scholar 

  10. J. Paulson, K. Colley, J. Biol. Chem.264, 17615 (1989).

    Google Scholar 

  11. H. Schachter, S. Narasimham, P. Gleeson, G. Vella, Can. J. Biochem. Cell Biol.61, 1049 (1983).

    Google Scholar 

  12. I. Nicollet, J. Lebreton, M. Fontaine, M. Hiro, Biochim. Biophys. Acta668, 235 (1981).

    Google Scholar 

  13. J-E. Hansen, V. Larsen, T. Bøg-Hansen, Clin. Chim. Acta138, 41 (1984).

    Google Scholar 

  14. O. Pos, A. Drechou, G. Durand, M. Bierhuizen, M. van der Stelt, W. van Dijk, Clin. Chim. Acta184, 121 (1989).

    Google Scholar 

  15. O. Pos, R. Oostendorp, M. Stelt, R. Scheper, W. van Dijk, Inflammation14, 133 (1990).

    Google Scholar 

  16. J-E. Hansen, S. Jensen, B. Nørgaard-Pedersen, T. Bøg-Hansen, Electrophoresis7, 180 (1986).

    Google Scholar 

  17. B. Biou, D. Konan, J. Feger, J. Agneray, Y. Leroy, P. Cardon, B. Fournet, G. Durand, Biochim. Biophys. Acta913, 308 (1987).

    Google Scholar 

  18. N. Seta, G. Durand, M. Corbic, J. Agneray, J. Feger, J. Hepatology2, 245 (1986).

    Google Scholar 

  19. M. J. Treuheit, H. B. Halsall, Biomed. Chromatogr.6, 50 (1992).

    Google Scholar 

  20. T. Ikenaka, M. Ishigura, J. Emura, H. Kaufmann, S. Isemura, W. Bauer, K. Schmid, Biochemistry11, 3817 (1972).

    Google Scholar 

  21. U. Leammli, Nature227, 680 (1970).

    Google Scholar 

  22. S. C. Hubbard, J. Biol. Chem.262, 16403 (1987).

    Google Scholar 

  23. S. C. Hubbard, J. Biol. Chem.263, 19303 (1988).

    Google Scholar 

  24. B. Barnett, K. Schlueter, H. B. Halsall, Biophys. J.59, 619a (1991).

    Google Scholar 

  25. C. Reading, J. Hutchins, Cancer Metastasis Rev.4, 221 (1985).

    Google Scholar 

  26. K. Yamashita, Y. Tachibana, T. Ohkura, A. Kobata, J. Biol. Chem.260, 3963 (1985).

    Google Scholar 

  27. G. Cossu, L. Warren, J. Biol. Chem.258, 5603 (1983).

    Google Scholar 

  28. T. Feizi, Nature314, 53 (1985).

    Google Scholar 

  29. J. Sadler, in “Biology of Carbohydrates” V. Ginsburg, P. Robbins, eds., Vol 2, John Wiley & Sons, New York, 1984, p. 199.

    Google Scholar 

  30. J. Paulson, J. Weinstein, A. Schauer, J. Biol. Chem.264, 10931 (1989).

    Google Scholar 

  31. J. Dennis, S. Laferte, Cancer Res.49, 945 (1989).

    Google Scholar 

  32. P. Coleman, P. Fishman, R. Brady, G. Todaro, J. Biol. Chem.250, 55 (1975).

    Google Scholar 

  33. I. Brochhausen, J. Carver, H. Schachter, Can. J. Biochem. Cell Biol.66, 1134 (1988).

    Google Scholar 

  34. M. J. Treuheit, H. B. Halsall, Clin. Chim. Acta210, 237 (1992).

    Google Scholar 

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Treuheit, M.J., Halsall, H.B. Restricted variation in the glycosylation of human α1-acid glycoprotein. Chromatographia 37, 144–148 (1993). https://doi.org/10.1007/BF02275851

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