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Studies on the inhibition of sialyl- and galactosyltransferases

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Abstract

The inhibition of the α-2,6-sialyltransferase from rat liver, the α-2,3-sialyltransferase from porcine submandibular gland and of the galactosyltransferase from human milk were studied using monosaccharide-, nucleoside- and nucleotide-derivatives of their naturally occurring donor substrates cytidine 5′-monophosphate-N-acetylneuraminic acid and uridine 5′-diphosphate-galactose, respectively. Only the corresponding nucleosides/nucleotides showed inhibitory activity. Periodate oxidation of CMP or CMP-Neu5Ac and of UMP or UDP-Gal led to reduced inhibitory efficiency with the respective transferase. The type and reversibility of the inhibition of some of these compounds, as well as the corresponding Ki values were determined.

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References

  1. Beyer TA, Sadler, JE, Rearick JI, Paulson JC, Hill RL (1981) Adv. Enzymol Relat Areas Mol Biol 5: 23–175.

    Google Scholar 

  2. Kornfield R, Kornfield S (1985) Annu Rev Biochem 54: 631–64.

    Google Scholar 

  3. Basu S, Basu M, Basu SS (1995) In Biology of the Sialic Acids (Rosenburg A, ed.) pp. 69–96. New York: Plenum Press.

    Google Scholar 

  4. Schachter H, Jabbal I, Hudgin RL, Pinteric L, McGuire EJ, Roseman S (1970) J Biol Chem 245: 1090–100.

    Google Scholar 

  5. Fleischer B (1981) J Cell Biol 89: 246–55.

    Google Scholar 

  6. Bartholomew BA, Jourdian GW, Roseman S (1973) J Biol Chem 248: 5751–62.

    Google Scholar 

  7. Kleene R, Berger EG (1993) Biochim Biophys Acta 1154: 283–325.

    Google Scholar 

  8. Yogeeswaran G (1983) Adv Cancer Res 38: 289–350.

    Google Scholar 

  9. Hakomori S-I (1985) Cancer Res 45: 2405–14.

    Google Scholar 

  10. Collard JG, Schijven JF, Bikker A, LaRiviere G, Bolscher JGM, Roos E (1986) Cancer Res 46: 3521–7.

    Google Scholar 

  11. Petrick AT, Meterissian S, Steele G, Thomas P (1994) Clin Exper Metastasis 12: 108–16.

    Google Scholar 

  12. Harvey BE, Toth CA, Wagner HE, Steele GD, Thomas P (1992) Cancer Res 52: 1775–9.

    Google Scholar 

  13. Kijima-Suda I, Miyamoto Y, Toyoshima S, Itoh M, Osawa T (1986) Cancer Res 46: 858–62.

    Google Scholar 

  14. Kijima-Suda I, Miyazawa T, Itoh M, Toyoshima S, Osawa T (1988) Cancer Res 48: 3728–32.

    Google Scholar 

  15. Wagner HE, Thomas P, Wolf BC, Rapoza A, Steele G, Jr (1990) Arch Surg 125: 351–4.

    Google Scholar 

  16. Harvey BE, Thomas P (1993) Biochim Biophys Res Commun 190: 571–5.

    Google Scholar 

  17. Bernacki RJ (1975) Eur J Biochem 58: 477–81.

    Google Scholar 

  18. Shah SN, Raghupathy E (1977) Proc Soc Exp Biol Med 155: 516–18.

    Google Scholar 

  19. Klohs WD, Bernacki RJ, Korytnyk W (1979) Cancer Res 39: 1231–8.

    Google Scholar 

  20. Paulson JC, Rearick JI, Hill RL (1977b) J Biol Chem 252: 2363–71.

    Google Scholar 

  21. Cambron LD, Leskawa KC (1993) Biochim Biophys Res Commun 193: 585–90.

    Google Scholar 

  22. Baumberger F, Vasella A (1986) Helv Chim Acta 69: 1535–41.

    Google Scholar 

  23. Zbiral E, Brandstetter HH, Schreiner E (1988) Monatsh Chem 119: 127–41.

    Google Scholar 

  24. Zbiral E, Brandstetter HH (1985) Monatsh Chem 116: 87–98.

    Google Scholar 

  25. Schmid W, Christian R, Zbiral E (1988) Tetrahedron Lett 29: 3643–6.

    Google Scholar 

  26. Wallimann K, Vasella A (1990) Helv Chim Acta 73: 1359–72.

    Google Scholar 

  27. Vasella A, Wyler R (1990) Helv Chim Acta 73: 1742–63.

    Google Scholar 

  28. Furuhata K, Ogura H (1992) Chem Pharm Bull 40: 3197–200.

    Google Scholar 

  29. Sato S, Fujita S, Furuhata K, Ogura H, Yoshimura S, Itoh M, Shitori Y (1987) Chem Pharm Bull 35: 4043–8.

    Google Scholar 

  30. Ogura H, Fujita S, Furuhata K, Itoh M, Shitori Y (1986) Chem Pharm Bull 34: 1479–84.

    Google Scholar 

  31. Ogura H, Furuhata K, Itoh M, Shitori Y (1986) Carbohydr Res 158: 37–51.

    Google Scholar 

  32. Sato S, Furuhata K, Itoh M, Shitori Y, Ogura H (1988) Chem Pharm Bull 36: 914–19.

    Google Scholar 

  33. Albarracin I, Lassaga FE, Caputto R (1988) Biochem J 254: 559–65.

    Google Scholar 

  34. van den Eijnden DH, Schiphorst WECM (1988) In Sialic Acids 1988, Proceedings of the Japanese-German Symposium on Sialic acids (Schauer R, Yamakawa T, eds) pp. 128–9. Kiel: Verlag Wissenschaft und Bildung.

    Google Scholar 

  35. Schauer R, Corfield AP, Wember M, Danon D (1975) Hoppe-Seyler's Z Physiol Chem 356: 1727–32.

    Google Scholar 

  36. Bo¬hm P, Dauber S, Baumeister L (1954) Klin Wochenschr 32: 289–92.

    Google Scholar 

  37. Schauer R (1978) Methods Enzymol 50: 64–89.

    Google Scholar 

  38. Warren L (1959) J Biol Chem 234: 1971–5.

    Google Scholar 

  39. Avigad G (1983) Anal. Biochem 134: 499–504.

    Google Scholar 

  40. Yu RK, Ledeen R (1969) J Biol Chem 244: 1306–13.

    Google Scholar 

  41. Ogura H, Furuhata F, Iwaki K, Takahashi H (1981) Nucleic Acids Symp Ser 10: 23–6.

    Google Scholar 

  42. Holy A, Pischel H (1974) Collect Czech Chem Commun 39: 3763–72.

    Google Scholar 

  43. Shukla AK, Schauer R (1982) J Chromatogr 244: 81–9.

    Google Scholar 

  44. Paulson JC, Beranek WE, Hill RL (1977a) J Biol Chem 252: 2356–62.

    Google Scholar 

  45. Dixon M (1953) Biochem J 55: 170–1.

    Google Scholar 

  46. Cornish-Bowden A (1974) Biochem J 137: 143–4.

    Google Scholar 

  47. Schachter H, Roseman S (1980) In The Biochemistry of Glyco-proteins and Proteoglycans (Lennarz WJ, ed.) pp. 85–160. New York: Plenum Press.

    Google Scholar 

  48. Reuter G, Schauer R, Szeiki C, Kamerling JP, Vliegenthart JFG (1989) Glycoconjugate J 6: 35–44.

    Google Scholar 

  49. Guthrie RD (1961) Adv Carbohydr Chem 16: 105–58.

    Google Scholar 

  50. Oritz AI, Reglero A, Rodriguez-Aparicio LB, Luengo JM (1989) Eur J Biochem 178: 741–9.

    Google Scholar 

  51. Prehm P (1985) Biochem J 225: 699–705.

    Google Scholar 

  52. Fujiwara T, Oda K, Yokota S, Takatsuki A, Ikehara Y (1988) J Biol Chem 263: 18545–52.

    Google Scholar 

  53. Misumi Y, Misumi Y, Miki K, Takatsuki A, Tamura G, Ikehara Y (1986) J Biol Chem 261: 11398–403.

    Google Scholar 

  54. Dixon M, Webb EC (1979) In Enzymes, 3rd edition (Dixon M, Webb EC ed) pp. 337–8. London: Longman.

    Google Scholar 

  55. Vaghefi MM, Bernacki RJ, Dalley NK, Wilson BE, Robins RK (1987a) J Med Chem 30: 1383–91.

    Google Scholar 

  56. Vaghefi MM, Bernacki RJ, Hennen WJ, Robins RK (1987b) J Med Chem 30: 1391–9.

    Google Scholar 

  57. Orbe M, Claesson A (1989) Eur J Med Chem 24: 447–51.

    Google Scholar 

  58. Yamamoto N, Hirano S, Ishida H, Kiso M, Hasagawa A (1990) In Xth International Carbohydrate Symposium, August 12-17, 1990 p. 135. Yokohama, Japan.

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Authors and Affiliations

  1. Biochemisches Institut, Christian-Albrechts-Universitat, Olshausenstrasse 40, D-24098, Kiel, Germany

    Reinhard G Kleineidam, Tillmann Schmelter & Roland Schauer

  2. Zentrum fur Hygiene und Medizinische Mikrobiologie, Philipps-Universitat, Robert-Koch-Strasse 17, D-35037, Marburg, Germany

    Ralph T Schwarz

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  1. Reinhard G Kleineidam
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  2. Tillmann Schmelter
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  3. Ralph T Schwarz
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  4. Roland Schauer
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Kleineidam, R.G., Schmelter, T., Schwarz, R.T. et al. Studies on the inhibition of sialyl- and galactosyltransferases. Glycoconj J 14, 57–66 (1997). https://doi.org/10.1023/A:1018560931389

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