442
Views
16
CrossRef citations to date
0
Altmetric
Original Articles

N-Linked Glycan Structures of Human Lactoferrin Produced by Transgenic Rice

, , , , , & show all
Pages 2565-2570 | Received 05 Aug 2004, Accepted 18 Sep 2004, Published online: 22 May 2014

  • 1) Kusnadi, A. R., Nikolov, Z. L., and Howard, J. A., Production of recombinant proteins in transgenic plants: Practical considerations. Biotechnol. Bioeng., 56, 473–484 (1997).
  • 2) Daniell, H., Streatfield, S. J., and Wycoff, K., Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants. Trends Plant Sci., 6, 219–226 (2001).
  • 3) Dwek, R. A., Glycobiology: “Towards understanding the function of sugars”. Biochem. Soc. Trans., 23, 1–25 (1995).
  • 4) Jenkins, N., and Curling, E. M., Glycosylation of recombinant proteins: problems and prospects. Enzyme Microb. Technol., 16, 354–364 (1994).
  • 5) Sturm, A., N-Glycosylation of plant proteins. In “New Comprehensive Biochemistry” Glycoproteins Vol. 29a, eds. Montreuil, J., Schachter, H., and Vliegenthart, J. F. G., Elsevier Science Publishers B. V., The Netherlands, pp. 521–541 (1995).
  • 6) Palacpac, N. Q., Kimura, Y., Fujiyama, K., Yoshida, T., and Seki, T., Structures of N-linked oligosaccharides of glycoproteins from tobacco BY2 suspension cultured cells. Biosci. Biotechnol. Biochem., 63, 35–39 (1999).
  • 7) Palacpac, N. Q., Yoshida, S., Sakai, H., Kimura, Y., Fujiyama, K., Yoshida, T., and Seki, T., Stable expression of human β1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns. Proc. Natl. Acad. Sci. U.S.A., 96, 4692–4697 (1999).
  • 8) Ward, P. P., Piddington, C. S., Cunningham, G. A., Zhou, X., Wyatt, R. D., and Conneely, O. M., A system for production of commercial quantities of human lactoferrin: a broad spectrum natural antibiotic. Biotechnol., 13, 498–503 (1995).
  • 9) Legrand, D., Salmon, V., Coddeville, B., Benaissa, M., Plancke, Y., and Spik, G., Structural determination of two N-linked glycans isolated from recombinant human lactoferrin expressed in BHK cells. FEBS Lett., 365, 57–60 (1995).
  • 10) Salmon, V., Legrand, D., Georges, B., Slomianny, M. C., Coddeville, B., and Spik, G., Characterization of human lactoferrin produced in the baculovirus expression system. Protein Expr. Purif., 9, 203–210 (1997).
  • 11) Salmon, V., Legrand, D., Slomianny, M. C., Yazidi, I., Spik, G., Gruber, V., Bournat, P., Olagnier, B., Mison, D., Theisen, M., and Merot, B., Production of human lactoferrin in transgenic tobacco plants. Protein Expr. Purif., 13, 127–135 (1998).
  • 12) Samyn-Petit, B., Gruber, V., Flahaut, C., Wajda-Dubos, J. P., Farrer, S., Pons, A., Desmaizieres, G., Slomianny, M. C., Theisen, M., and Delannoy, P., N-glycosylation potential of maize: the human lactoferrin used as a model. Glycoconj. J., 18, 519–527 (2001).
  • 13) Lerouge, P., Bardor, M., Pagny, S., Gomord, V., and Faye, L., N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans. Curr. Pharm. Biotechnol., 1, 347–354 (2000).
  • 14) Sturm, A., Van Kuik, J. A., Vliegenthart, J. F., and Chrispeels, M. J., Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin. J. Biol. Chem., 262, 13392–13403 (1987).
  • 15) Wilson, I. B., Harthill, J. E., Mullin, N. P., Ashford, D. A., and Altmann, F., Core α1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts. Glycobiol., 8, 651–661 (1998).
  • 16) Lonnerdal, B., Expression of human milk proteins in plants. J. Am. Coll. Nutr., 21 (3 Suppl.), 218S–221S (2002).
  • 17) Suzuki, Y. A., Kelleher, S. L., Yalda, D., Wu, L., Huang, J., Huang, N., and Lonnerdal, B., Expression, characterization, and biologic activity of recombinant human lactoferrin in rice. J. Pediatr. Gastroenterol. Nutr., 36, 190–199 (2003).
  • 18) Powell, M. J., and Ogden, J. E., Nucleotide sequence of a human lactoferrin cDNA. Nucleic Acids Res., 18, 4013 (1990).
  • 19) Anzai, H., Takaiwa, F., and Katsumata, K., Production of human lactoferrin in transgenic plants. In “Lactoferrin: Structure, Function and Applications”, eds. Tsuda, H., Tomita, M., Kuwata, T., Perraudin, J. P., and Shimazaki, K., Elsevier Science Publishers B. V., The Netherlands, pp. 265–271 (2000).
  • 20) Murakami, T., Anzai, H., Imai, S., Nagaoka, K., and Thompson, C. J., The bialaphos biosynthetic genes of Streptomyces hygroscopicus: molecular cloning and characterization of the gene cluster. Molec. Gen. Genet., 205, 42–50 (1986).
  • 21) Hase, S., Ikenaka, T., and Matsushima, Y., A highly sensitive method for analyses of sugar moieties of glycoproteins by fluorescence labeling. J. Biochem., 90, 407–414 (1981).
  • 22) Misaki, R., Fujiyama, K., Yokoyama, H., Ido, Y., Miyauchi, K., Yoshida, T., and Seki, T., Characterization of almond α-Mannosidase and its application for structure analysis of sugar chain. J. Biosci. Bioeng., 96, 187–192 (2003).
  • 23) Abe, K., McKibbin, J. M., and Hakomori, S., The monoclonal antibody directed to difucosylated type 2 chain (Fucα1→2Galβ1→4[Fucα1→3]GlcNAc; Y Determinant). J. Biol. Chem., 258, 11793–11797 (1983).
  • 24) Gray, J. S., Yang, B. Y., and Montgomery, R., Heterogeneity of glycans at each N-glycosylation site of horseradish peroxidase. Carbohydr. Res., 311, 61–69 (1998).
  • 25) Takahashi, N., Lee, K. B., Nakagawa, H., Tsukamoto, Y., Masuda, K., and Lee, Y. C., New N-glycans in horseradish peroxidase. Anal. Biochem., 255, 183–187 (1998).
  • 26) Shimazaki, A., Makino, Y., Omichi, K., Odani, S., and Hase, S., A new sugar chain of the proteinase inhibitor from latex of Carica papaya. J. Biochem., 125, 560–565 (1999).
  • 27) Scocca, J., and Lee, Y. C., The composition and structure of the carbohydrate of pineapple stem bromelain. J. Biol. Chem., 244, 4852–4863 (1969).
  • 28) Spik, G., Strecker, G., Fournet, B., Bouquelet, S., Montreuil, J., Dorland, L., van Halbeek, H., and Vliegenthart, J. F., Primary structure of the glycans from human lactotransferrin. Eur. J. Biochem., 121, 413–419 (1982).
  • 29) Yasuda, Y., Takahashi, N., and Murachi, T., The composition and structure of carbohydrate moiety of stem bromelain. Biochemistry, 9, 25–32 (1970).
  • 30) Wilson, I. B., Zeleny, R., Kolarich, D., Staudacher, E., Stroop, C. J., Kamerling, J. P., and Altmann, F., Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core α1,3-linked fucose and xylose substitutions. Glycobiol., 11, 261–274 (2001).
  • 31) Altmann, F., Schwihla, H., Staudacher, E., Glossl, J., and Marz, L., Insect cells contain an unusual, membrane-bound β-N-acetylglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem., 270, 17344–17349 (1995).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.