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Biochemistry Research International
Volume 2015, Article ID 767204, 7 pages
http://dx.doi.org/10.1155/2015/767204
Research Article

Development of Monoclonal Antibodies against CMP-N-Acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 (ST3Gal-I) Recombinant Protein Expressed in E. coli

Yashraj Biotechnology Ltd., Plot No. C 232, TTC Industrial Area, MIDC, Navi Mumbai 400705, India

Received 6 October 2015; Revised 21 November 2015; Accepted 25 November 2015

Academic Editor: J. Justin Hsuan

Copyright © 2015 Anuj Kumar Gupta 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. R. Apweiler, H. Hermjakob, and N. Sharon, “On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database,” Biochimica et Biophysica Acta: General Subjects, vol. 1473, no. 1, pp. 4–8, 1999. View at Publisher · View at Google Scholar · View at Scopus
  2. I. Marchal, G. Golfier, O. Dugas, and M. Majed, “Bioinformatics in glycobiology,” Biochimie, vol. 85, no. 1-2, pp. 75–81, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. J. A. W. Halliday, A. H. Franks, T. E. Ramsdale, R. Martin, and E. Palant, “A rapid, semi-automated method for detection of Galβ1-4GlcNAc α2,6-sialyltransferase (EC 2.4.99.1) activity using the lectin Sambucus nigra agglutinin,” Glycobiology, vol. 11, no. 7, pp. 557–564, 2001. View at Publisher · View at Google Scholar · View at Scopus
  4. A. Varki, “Sialic acids as ligands in recognition phenomena,” The FASEB Journal, vol. 11, no. 4, pp. 248–255, 1997. View at Google Scholar · View at Scopus
  5. A. Harduin-Lepers, M.-A. Recchi, and P. Delannoy, “The year of sialyltransferase,” Glycobiology, vol. 5, no. 8, pp. 741–758, 1995. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Tsuji, A. K. Datta, and J. C. Paulson, “Systematic nomenclature for sialyltransferases,” Glycobiology, vol. 6, no. 7, pp. 5–11, 1996. View at Google Scholar · View at Scopus
  7. H. Kitagawa and J. C. Paulson, “Differential expression of five sialyltransferase genes in human tissues,” The Journal of Biological Chemistry, vol. 269, no. 27, pp. 17872–17878, 1994. View at Google Scholar · View at Scopus
  8. Y.-J. Kim, K.-S. Kim, S.-H. Kim et al., “Molecular cloning and expression of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II),” Biochemical and Biophysical Research Communications, vol. 228, no. 2, pp. 324–327, 1996. View at Publisher · View at Google Scholar
  9. V. Giordanengo, S. Bannwarth, C. Laffont et al., “Cloning and expression of cDNA for a human Gal(β1-3)GalNAc α2,3-sialyltransferase from the CEM T-cell line,” European Journal of Biochemistry, vol. 247, no. 2, pp. 558–566, 1997. View at Publisher · View at Google Scholar · View at Scopus
  10. L. R. Loureiro, M. A. Carrascal, A. Barbas et al., “Challenges in antibody development against Tn and Sialyl-Tn antigens,” Biomolecules, vol. 5, no. 3, pp. 1783–1809, 2015. View at Publisher · View at Google Scholar
  11. I. Brockhausen, “Pathways of O-glycan biosynthesis in cancer cells,” Biochimica et Biophysica Acta—General Subjects, vol. 1473, no. 1, pp. 67–95, 1999. View at Publisher · View at Google Scholar · View at Scopus
  12. P. A. Videira, M. Correia, N. Malagolini et al., “ST3Gal.I sialyltransferase relevance in bladder cancer tissues and cell lines,” BMC Cancer, vol. 9, article 357, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. I. Brockhausen, “Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions,” EMBO Reports, vol. 7, no. 6, pp. 599–604, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. F. Schneider, W. Kemmner, W. Haensch et al., “Overexpression of sialyltransferase CMP-sialic acid: Galβ1,3GalNAc-Rα6-sialyltransferase is related to poor patient survival in human colorectal carcinomas,” Cancer Research, vol. 61, no. 11, pp. 4605–4611, 2001. View at Google Scholar · View at Scopus
  15. S. R. Hull, A. Bright, K. L. Carraway, M. Abe, D. F. Hayes, and D. W. Kufe, “Oligosaccharide differences in the DF3 sialomucin antigen from normal human milk and the BT-20 human breast carcinoma cell line,” Cancer Communications, vol. 1, no. 4, pp. 261–267, 1989. View at Google Scholar · View at Scopus
  16. F. G. Hanisch, G. Uhlenbruck, J. Peter-Katalinic, H. Egge, J. Dabrowski, and U. Dabrowski, “Structures of neutral O-linked polylactosaminoglycans on human skim milk mucins. a novel type of linearly extended poly-N-acetyllactosamine backbones with Galβ(1–4)GlcNAcβ(1–6) repeating units,” The Journal of Biological Chemistry, vol. 264, no. 2, pp. 872–883, 1989. View at Google Scholar
  17. K. O. Lloyd, J. Burchell, V. Kudryashov, B. W. T. Yin, and J. Taylor-Papadimitriou, “Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. Demonstration of simpler and fewer glycan chains in tumor cells,” The Journal of Biological Chemistry, vol. 271, no. 52, pp. 33325–33334, 1996. View at Publisher · View at Google Scholar · View at Scopus
  18. A. Solatycka, T. Owczarek, F. Piller et al., “MUC1 in human and murine mammary carcinoma cells decreases the expression of core 2 β1,6-N-acetylglucosaminyltransferase and β-galactoside α2,3-sialyltransferase,” Glycobiology, vol. 22, no. 8, pp. 1042–1054, 2012. View at Publisher · View at Google Scholar · View at Scopus
  19. U. K. Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature, vol. 227, no. 5259, pp. 680–685, 1970. View at Publisher · View at Google Scholar · View at Scopus
  20. G. Kohler and C. Milstein, “Continuous cultures of fused cells secreting antibody of predefined specificity,” Nature, vol. 256, no. 5517, pp. 495–497, 1975. View at Publisher · View at Google Scholar · View at Scopus
  21. W. Weiss, F. Weiland, and A. Gorg, “Protein detection and quantitation technologies for gel-based proteome analysis,” in Methods in Molecular Biology, J. Reinders and A. Sickmann, Eds., vol. 564, pp. 59–82, Humana Press, 2009. View at Google Scholar
  22. M. R. Kudelka, T. Ju, J. Heimburg-Molinaro, and R. D. Cummings, “Simple sugars to complex disease—mucin-type O-glycans in cancer,” in Advances in Cancer Research, vol. 126, chapter 3, pp. 53–135, Elsevier, 2015. View at Publisher · View at Google Scholar
  23. P.-H. Wang, W.-L. Lee, C.-M. Juang et al., “Altered mRNA expressions of sialyltransferases in ovarian cancers,” Gynecologic Oncology, vol. 99, no. 3, pp. 631–639, 2005. View at Publisher · View at Google Scholar
  24. P. A. Videira, I. F. Amado, H. J. Crespo et al., “Surface α2-3- and α2-6-sialylation of human monocytes and derived dendritic cells and its influence on endocytosis,” Glycoconjugate Journal, vol. 25, no. 3, pp. 259–268, 2008. View at Publisher · View at Google Scholar · View at Scopus
  25. J. J. Priatel, D. Chui, N. Hiraoka et al., “The ST3Gal-I sialyltransferase controls CD8+ T lymphocyte homeostasis by modulating O-glycan biosynthesis,” Immunity, vol. 12, no. 3, pp. 273–283, 2000. View at Publisher · View at Google Scholar · View at Scopus
  26. K.-Y. Lee, H. G. Kim, M. R. Hwang et al., “The hexapeptide inhibitor of Galβ1,3GalNAc-specific α2,3-sialyltransferase as a generic inhibitor of sialyltransferases,” The Journal of Biological Chemistry, vol. 277, no. 51, pp. 49341–49351, 2002. View at Publisher · View at Google Scholar · View at Scopus