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Journal of Biomedicine and Biotechnology
Volume 2011 (2011), Article ID 560850, 8 pages
http://dx.doi.org/10.1155/2011/560850
Research Article

Alpha 1,3-Galactosyltransferase Deficiency in Pigs Increases Sialyltransferase Activities That Potentially Raise Non-Gal Xenoantigenicity

1Department of Animal Biotechnology, Konkuk University, Seoul 143-701, Republic of Korea
2Department of Animal Science, College of Natural Science, Konkuk University, Chung-ju 380-701, Republic of Korea
3Division of Animal Life Science, College of Animal Bioscience & Technology, Konkuk University, Seoul 143-701, Republic of Korea

Received 29 May 2011; Revised 29 July 2011; Accepted 15 August 2011

Academic Editor: Saulius Butenas

Copyright © 2011 Jong-Yi Park 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. M. S. Sandrin and I. F. McKenzie, “Gal α(1,3)Gal, the major xenoantigen(s) recognised in pigs by human natural antibodies,” Immunological Reviews, no. 141, pp. 169–190, 1994. View at Google Scholar · View at Scopus
  2. U. Galili, S. B. Shohet, E. Kobrin, C. L. Stults, and B. A. Macher, “Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells,” Journal of Biological Chemistry, vol. 263, no. 33, pp. 17755–17762, 1988. View at Google Scholar · View at Scopus
  3. Y. Dai, T. D. Vaught, J. Boone et al., “Targeted disruption of the α1,3-galactosyltransferase gene in cloned pigs,” Nature Biotechnology, vol. 20, no. 3, pp. 251–255, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  4. L. Lai, D. Kolber-Simonds, K. W. Park et al., “Production of α-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning,” Science, vol. 295, no. 5557, pp. 1089–1092, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  5. K. Kuwaki, Y. L. Tseng, F. J. Dor et al., “Heart transplantation in baboons using α1,3-galactosyltransferase gene-knockout pigs as donors: initial experience,” Nature Medicine, vol. 11, no. 1, pp. 29–31, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  6. K. S. Ahn, Y. J. Kim, M. Kim et al., “Resurrection of an alpha-1,3-galactosyltransferase gene-targeted miniature pig by recloning using postmortem ear skin fibroblasts,” Theriogenology, vol. 75, no. 5, pp. 933–939, 2011. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. M. Ezzelarab, D. Ayares, and D. K. C. Cooper, “Carbohydrates in xenotransplantation,” Immunology and Cell Biology, vol. 83, no. 4, pp. 396–404, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. A. Shimizu, Y. Hisashi, K. Kuwaki et al., “Thrombotic microangiopathy associated with humoral rejection of cardiac xenografts from α1,3-galactosyltransferase gene-knockout pigs in baboons,” The American Journal of Pathology, vol. 172, no. 6, pp. 1471–1481, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  9. M. Ezzelarab, D. Ayares, and D. K. Cooper, “Carbohydrates in xenotransplantation,” Immunology and Cell Biology, vol. 83, no. 4, pp. 396–404, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  10. E. A. Muchmore, M. Milewski, A. Varki, and S. Diaz, “Biosynthesis of N-glycolyneuraminic acid. The primary site of hydroxylation of N-acetylneuraminic acid is the cytosolic sugar nucleotide pool,” Journal of Biological Chemistry, vol. 264, no. 34, pp. 20216–20223, 1989. View at Google Scholar · View at Scopus
  11. T. Kawano, Y. Kozutsumi, T. Kawasaki, and A. Suzuki, “Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N-acetylneuraminic acid hydroxylation system,” Journal of Biological Chemistry, vol. 269, no. 12, pp. 9024–9029, 1994. View at Google Scholar · View at Scopus
  12. M. Tanemura, S. Miyagawa, S. Koyota et al., “Reduction of the major swine xenoantigen, the α-galactosyl epitope by transfection of the α2,3-sialyltransferase gene,” Journal of Biological Chemistry, vol. 273, no. 26, pp. 16421–16425, 1998. View at Publisher · View at Google Scholar · View at Scopus
  13. K. Sasaki, E. Watanabe, K. Kawashima et al., “Expression cloning of a novel Galβ(1-3/1-4)GlcNAc α2,3- sialyltransferase using lectin resistance selection,” Journal of Biological Chemistry, vol. 268, no. 30, pp. 22782–22787, 1993. View at Google Scholar · View at Scopus
  14. S. Y. Lee, J. Y. Park, Y. J. Choi et al., “Comparative proteomic analysis associated with term placental insufficiency in cloned pig,” Proteomics, vol. 7, no. 8, pp. 1303–1315, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  15. M. R. Park, S. K. Cho, S. Y. Lee et al., “A rare and often unrecognized cerebromeningitis and hemodynamic disorder: a major cause of sudden death in somatic cell cloned piglets,” Proteomics, vol. 5, no. 7, pp. 1928–1939, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  16. A. Harduin-Lepers, R. Mollicone, P. Delannoy, and R. Oriol, “The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach,” Glycobiology, vol. 15, no. 8, pp. 805–817, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  17. S. Kelm and R. Schauer, “Sialic acids in molecular and cellular interactions,” International Review of Cytology, vol. 175, pp. 137–240, 1997. View at Google Scholar · View at Scopus
  18. C. Traving and R. Schauer, “Structure, function and metabolism of sialic acids,” Cellular and Molecular Life Sciences, vol. 54, no. 12, pp. 1330–1349, 1998. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Varki, “Diversity in the sialic acids,” Glycobiology, vol. 2, no. 1, pp. 25–40, 1992. View at Google Scholar · View at Scopus
  20. S. R. Haseley, P. Talaga, J. P. Kamerling, and J. F. Vliegenthart, “Characterization of the carbohydrate binding specificity and kinetic parameters of lectins by using surface plasmon resonance,” Analytical Biochemistry, vol. 274, no. 2, pp. 203–210, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  21. A. Imberty, C. Gautier, J. Lescar, S. Pérez, L. Wyns, and R. Loris, “An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides,” Journal of Biological Chemistry, vol. 275, no. 23, pp. 17541–17548, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  22. N. Shibuya, I. J. Goldstein, W. F. Broekaert, M. Nsimba-Lubaki, B. Peeters, and W. J. Peumans, “The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence,” Journal of Biological Chemistry, vol. 262, no. 4, pp. 1596–1601, 1987. View at Google Scholar · View at Scopus
  23. T. A. Shinkel, C. G. Chen, E. Salvaris et al., “Changes in cell surface glycosylation in α1,3-galactosyltransferase knockout and α1,2-fucosyltransferase transgenic mice,” Transplantation, vol. 64, no. 2, pp. 197–204, 1997. View at Publisher · View at Google Scholar · View at Scopus
  24. M. Tanemura and U. Galili, “Differential expression of α-Gal epitopes on pig and mouse organs,” Transplantation Proceedings, vol. 32, no. 5, p. 843, 2000. View at Publisher · View at Google Scholar · View at Scopus
  25. S. Miyagawa, S. Takeishi, A. Yamamoto et al., “Survey of glycoantigens in cells from α1-3galactosyltransferase knockout pig using a lectin microarray,” Xenotransplantation, vol. 17, no. 1, pp. 61–70, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  26. T. Hamamoto, N. Kurosawa, Y. C. Lee, and S. Tsuji, “Donor substrate specificities of Galβ1,4GlcNAc α2,6-sialyltransferase and Gal β1,3GalNAc α2,3-sialyltransferase: comparison of N-acetyl and N- glycolylneuraminic acids,” Biochimica et Biophysica Acta, vol. 1244, no. 1, pp. 223–228, 1995. View at Publisher · View at Google Scholar · View at Scopus
  27. A. E. Fedøy, N. Yang, A. Martinez, H. K. S. Leiros, and I. H. Steen, “Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila reveal a cold-active enzyme with an unusual high thermal stability,” Journal of Molecular Biology, vol. 372, no. 1, pp. 130–149, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  28. K. H. Song, Y. J. Kang, U. H. Jin et al., “Cloning and functional characterization of pig CMP- N-acetylneuraminic acid hydroxylase for the synthesis of N-glycolylneuraminic acid as the xenoantigenic determinant in pig-human xenotransplantation,” Biochemical Journal, vol. 427, no. 1, pp. 179–188, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus