Table of Contents
International Journal of Carbohydrate Chemistry
Volume 2009, Article ID 398284, 4 pages
http://dx.doi.org/10.1155/2009/398284
Research Article

-Cyclodextrin Increases Hydrolysis of Gangliosides by Sialidase from Arthrobacter ureafaciens: Hydrolysis of Gangliosides

1Japan Chemical Innovation Institute, 1-3-5 Jimbocho, Chiyoda-ku, Tokyo 101-0051, Japan
2Kaneka Corporation, 3-2-4, Nakanoshima, Kita-ku, Osaka 530-8288, Japan
3Institute of Industrial Science, The University of Tokyo, 4-6-1, Komaba, Meguro-ku, Tokyo 153-8505, Japan

Received 3 November 2008; Accepted 16 December 2008

Academic Editor: Chun-Hung Lin

Copyright © 2009 Rie Mitsumori et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. Y. Nagai and M. Iwamori, “Cellular biology of gangliosides,” in Biology of the Sialic Acids, A. Rosenberg, Ed., pp. 197–241, Plenum Press, New York, NY, USA, 1995. View at Google Scholar
  2. S.-I. Hakomori, “Cancer-associated glycosphingolipid antigens: their structure, organization, and function,” Acta Anatomica, vol. 161, no. 1–4, pp. 79–90, 1998. View at Publisher · View at Google Scholar
  3. A. Varki, “Biological roles of oligosaccharides: all of the theories are correct,” Glycobiology, vol. 3, no. 2, pp. 97–130, 1993. View at Publisher · View at Google Scholar
  4. M. Saito and R. K. Yu, “Biochemisty and function of sialidases,” in Biology of the Sialic Acids, A. Rosenberg, Ed., pp. 261–313, Plenum Press, New York, NY, USA, 1995. View at Google Scholar
  5. R. Schauer and J. G. Vliegenthart, “Introduction to sialic acids,” in Sialic Acids: Chemistry, Metabolism and Functions, R. Schauer, Ed., pp. 1–3, Springer, Vienna, Austria, 1982. View at Google Scholar
  6. M.-Y. Chou, S.-C. Li, M. Kiso, A. Hasegawa, and Y.-T. Li, “Purification and characterization of sialidase L, a NeuAc α23Gal-specific sialidase,” The Journal of Biological Chemistry, vol. 269, no. 29, pp. 18821–18826, 1994. View at Google Scholar
  7. M.-Y. Chou, S.-C. Li, and Y.-T. Li, “Cloning and expression of sialidase L, a NeuAcα23Gal-specific sialidase from the leech, Macrobdella decora,” The Journal of Biological Chemistry, vol. 271, no. 32, pp. 19219–19224, 1996. View at Publisher · View at Google Scholar
  8. T. Corfield, “Bacterial sialidases—roles in pathogenicity and nutrition,” Glycobiology, vol. 2, no. 6, pp. 509–521, 1992. View at Publisher · View at Google Scholar
  9. M. Iwamori, Y. Ohta, Y. Uchida, and Y. Tsukada, “Arthrobacter ureafaciens sialidase isoenzymes, L, m1 and m2, cleave fucosyl GM1,” Glycoconjugate Journal, vol. 14, no. 1, pp. 67–73, 1997. View at Publisher · View at Google Scholar
  10. M. Iwamori, S. Sunada, E. Ishihara, M. Moki, S. Fujimoto, and Y. Nagai, “Differential expression of fucosyl GM1 and a disialoganglioside with a NeuAcα2-6Ga1NAc linkage (GD1e) in various rat ascites hepatoma cells,” FEBS Letters, vol. 198, no. 1, pp. 66–70, 1986. View at Publisher · View at Google Scholar
  11. L. O. Sillerud, R. K. Yu, and D. E. Schafer, “Assignment of the carbon-13 nuclear magnetic resonance spectra of gangliosides GM4, GM3, GM2, GM1, GD1a, GD1b, and GT1b,” Biochemistry, vol. 21, no. 6, pp. 1260–1271, 1982. View at Publisher · View at Google Scholar
  12. M. Iwamori, T. Kaido, Y. Iwamori, Y. Ohta, K. Tsukamoto, and S. Kozaki, “Involvement of the C-terminal tail of Arthrobacter ureafaciens sialidase isoenzyme M in cleavage of the internal sialic acid of ganglioside GM1,” The Journal of Biochemistry, vol. 138, no. 3, pp. 327–334, 2005. View at Publisher · View at Google Scholar
  13. I. Nagashima, H. Shimizu, T. Matsushita, and S.-I. Nishimura, “Chemical and enzymatic synthesis of neoglycolipids in the presence of cyclodextrins,” Tetrahedron Letters, vol. 49, no. 21, pp. 3413–3418, 2008. View at Publisher · View at Google Scholar
  14. H. Tsuda, K. Sekine, N. Takasuka, H. Toriyama-Baba, and M. Iigo, “Prevention of colon carcinogenesis and carcinoma metastasis by orally administered bovine lactoferrin in animals,” BioFactors, vol. 12, no. 1–4, pp. 83–88, 2000. View at Publisher · View at Google Scholar
  15. B. Gatterbauer, A. Neisser, H. Bernheimer, and B. Schwerer, “Antiglycosphingolipid immune responses in neurology: the Vienna experience with isotypes, subclasses, and disease,” Annals of the New York Academy of Sciences, vol. 845, pp. 353–362, 1998. View at Publisher · View at Google Scholar
  16. Y. Uchida, Y. Tsukada, and T. Sugimori, “Enzymatic properties of neuraminidases from Arthrobacter ureafaciens,” The Journal of Biochemistry, vol. 86, no. 5, pp. 1573–1585, 1979. View at Google Scholar
  17. M. C. Z. Kasuya, L. X. Wang, Y. C. Lee et al., “Azido glycoside primer: a versatile building block for the biocombinatorial synthesis of glycosphingolipid analogues,” Carbohydrate Research, vol. 329, no. 4, pp. 755–763, 2000. View at Publisher · View at Google Scholar
  18. L. Svennerholm, “Quantitive estimation of sialic acids—II: a colorimetric resorcinol-hydrochloric acid method,” Biochimica et Biophysica Acta, vol. 24, pp. 604–611, 1957. View at Publisher · View at Google Scholar
  19. T. Shiraishi, M. Hiraiwa, and Y. Uda, “Effects of cyclodextrins on the hydrolysis of ganglioside GM1 by acid β-galactosidases,” Glycoconjugate Journal, vol. 10, no. 2, pp. 170–174, 1993. View at Publisher · View at Google Scholar