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Volumn 112, Issue 5, 2011, Pages 476-484

N-terminal vacuolar sorting signal at the mouse antibody alters the N-linked glycosylation pattern in suspension-cultured tobacco BY2 cells

Author keywords

Glycosylation; IgG; Plant; Sorting signal; Sporamin; Vacuole

Indexed keywords

IGG; PLANT; SORTING SIGNAL; SPORAMIN; VACUOLE;

EID: 81255136221     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2011.07.002     Document Type: Article
Times cited : (9)

References (43)
  • 1
    • 0032168897 scopus 로고    scopus 로고
    • Compartment-specific accumulation of recombinant immunoglobulins in plant cells: an essential tool for antibody production and immunomodulation of physiological functions and pathogen activity
    • Conrad U., Fiedler U. Compartment-specific accumulation of recombinant immunoglobulins in plant cells: an essential tool for antibody production and immunomodulation of physiological functions and pathogen activity. Plant Mol. Biol. 1998, 38:101-109.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 101-109
    • Conrad, U.1    Fiedler, U.2
  • 3
    • 2442590941 scopus 로고    scopus 로고
    • Plant molecular farming: systems and products
    • Horn M.E., Woodard S.L., Howard J.A. Plant molecular farming: systems and products. Plant Cell Rep. 2004, 22:711-720.
    • (2004) Plant Cell Rep. , vol.22 , pp. 711-720
    • Horn, M.E.1    Woodard, S.L.2    Howard, J.A.3
  • 5
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: all of the theories are correct
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993, 3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 6
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular function of N-linked glycans
    • Helenius A., Aebi M. Intracellular function of N-linked glycans. Science 2001, 291:2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 7
    • 0025313449 scopus 로고
    • Isolation, characterization and properties of Saccharomyces cerevisiae mnn mutants with non-conditional protein glycosylation defects
    • Ballou C.E. Isolation, characterization and properties of Saccharomyces cerevisiae mnn mutants with non-conditional protein glycosylation defects. Methods Enzymol. 1990, 185:440-470.
    • (1990) Methods Enzymol. , vol.185 , pp. 440-470
    • Ballou, C.E.1
  • 8
    • 0035958916 scopus 로고    scopus 로고
    • Identification of core α1,3 fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster
    • Fabini G., Freilinger A., Altmann F., Wilson I.B.H. Identification of core α1,3 fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. J. Biol. Chem. 2001, 276:28058-28067.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28058-28067
    • Fabini, G.1    Freilinger, A.2    Altmann, F.3    Wilson, I.B.H.4
  • 9
    • 0034570433 scopus 로고    scopus 로고
    • N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans
    • Lerouge P., Bardor M., Pagny S., Gomord V., Faye L. N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans. Curr. Pharm. Biotechnol. 2000, 1:347-354.
    • (2000) Curr. Pharm. Biotechnol. , vol.1 , pp. 347-354
    • Lerouge, P.1    Bardor, M.2    Pagny, S.3    Gomord, V.4    Faye, L.5
  • 10
    • 0033829810 scopus 로고    scopus 로고
    • Effect of climate conditions and plant developmental stage on the stability of antibodies expressed in transgenic tobacco
    • Stevens L.H., Stoopen G.M., Elbers I.J., Molthoff J.W., Bakker H.A., Lommen A., Bosch D., Jordi W. Effect of climate conditions and plant developmental stage on the stability of antibodies expressed in transgenic tobacco. Plant Physiol. 2000, 124:173-182.
    • (2000) Plant Physiol. , vol.124 , pp. 173-182
    • Stevens, L.H.1    Stoopen, G.M.2    Elbers, I.J.3    Molthoff, J.W.4    Bakker, H.A.5    Lommen, A.6    Bosch, D.7    Jordi, W.8
  • 11
    • 0034959745 scopus 로고    scopus 로고
    • Influence of growth conditions and developmental stage on N-glycan heterogeneity of transgenic immunoglobulin G and endogenous proteins in tobacco leaves
    • Elbers I.J., Stoopen G.M., Bakker H., Stevens L.H., Bardor M., Molthoff J.W., Jordi W.J., Bosch D., Lommen A. Influence of growth conditions and developmental stage on N-glycan heterogeneity of transgenic immunoglobulin G and endogenous proteins in tobacco leaves. Plant Physiol. 2001, 126:1314-1322.
    • (2001) Plant Physiol. , vol.126 , pp. 1314-1322
    • Elbers, I.J.1    Stoopen, G.M.2    Bakker, H.3    Stevens, L.H.4    Bardor, M.5    Molthoff, J.W.6    Jordi, W.J.7    Bosch, D.8    Lommen, A.9
  • 12
    • 0034958453 scopus 로고    scopus 로고
    • Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core alpha1,3-linked fucose and xylose substitutions
    • Wilson I.B., Zeleny R., Kolarich D., Staudacher E., Stroop C.J., Kamerling J.P., Altmann F. Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core alpha1,3-linked fucose and xylose substitutions. Glycobiology 2001, 11:261-274.
    • (2001) Glycobiology , vol.11 , pp. 261-274
    • Wilson, I.B.1    Zeleny, R.2    Kolarich, D.3    Staudacher, E.4    Stroop, C.J.5    Kamerling, J.P.6    Altmann, F.7
  • 13
    • 2942606516 scopus 로고    scopus 로고
    • Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin
    • Bencurova M., Hemmer W., Focke-Tejkl M., Wilson I.B., Altmann F. Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin. Glycobiology 2004, 14:457-466.
    • (2004) Glycobiology , vol.14 , pp. 457-466
    • Bencurova, M.1    Hemmer, W.2    Focke-Tejkl, M.3    Wilson, I.B.4    Altmann, F.5
  • 15
    • 33745685217 scopus 로고    scopus 로고
    • N-linked glycan structure of a mouse monoclonal antibody produced from tobacco BY2 suspension-cultured cells
    • Fujiyama K., Misaki R., Katsura A., Tanaka T., Furukawa A., Omasa T., Seki T. N-linked glycan structure of a mouse monoclonal antibody produced from tobacco BY2 suspension-cultured cells. J. Biosci. Bioeng. 2006, 101:212-218.
    • (2006) J. Biosci. Bioeng. , vol.101 , pp. 212-218
    • Fujiyama, K.1    Misaki, R.2    Katsura, A.3    Tanaka, T.4    Furukawa, A.5    Omasa, T.6    Seki, T.7
  • 16
    • 0026023554 scopus 로고
    • Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting
    • Matsuoka K., Nakamura K. Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc. Natl. Acad. Sci. USA 1991, 88:834-838.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 834-838
    • Matsuoka, K.1    Nakamura, K.2
  • 17
    • 0029611736 scopus 로고
    • O-glycosylation of a precursor to a sweet potato vacuolar protein, sporamin, expressed in tobacco cells
    • Matsuoka K., Watanabe N., Nakamura K. O-glycosylation of a precursor to a sweet potato vacuolar protein, sporamin, expressed in tobacco cells. Plant J. 1995, 8:877-889.
    • (1995) Plant J. , vol.8 , pp. 877-889
    • Matsuoka, K.1    Watanabe, N.2    Nakamura, K.3
  • 19
    • 0031177762 scopus 로고    scopus 로고
    • The N-terminal propeptide of the precursor to sporamin acts as a vacuole-targeting signal even at the C terminus of the mature part in tobacco cells
    • Koide Y., Hirano H., Matsuoka K., Nakamura K. The N-terminal propeptide of the precursor to sporamin acts as a vacuole-targeting signal even at the C terminus of the mature part in tobacco cells. Plant Physiol. 1997, 114:863-870.
    • (1997) Plant Physiol. , vol.114 , pp. 863-870
    • Koide, Y.1    Hirano, H.2    Matsuoka, K.3    Nakamura, K.4
  • 20
    • 0027014897 scopus 로고
    • New plant binary vectors with selectable markers located proximal to the left T-DNA border
    • Becker D., Kemper E., Schell J., Masterson R. New plant binary vectors with selectable markers located proximal to the left T-DNA border. Plant Mol. Biol. 1992, 20:1195-1197.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 1195-1197
    • Becker, D.1    Kemper, E.2    Schell, J.3    Masterson, R.4
  • 21
    • 60949091047 scopus 로고    scopus 로고
    • Change in glycosylation pattern with extension of endoplasmic reticulum retention signal sequence of mouse antibody produced by suspension-cultured tobacco BY2 cells
    • Fujiyama K., Misaki R., Sakai Y., Omasa T., Seki T. Change in glycosylation pattern with extension of endoplasmic reticulum retention signal sequence of mouse antibody produced by suspension-cultured tobacco BY2 cells. J. Biosci. Bioeng. 2009, 107:165-172.
    • (2009) J. Biosci. Bioeng. , vol.107 , pp. 165-172
    • Fujiyama, K.1    Misaki, R.2    Sakai, Y.3    Omasa, T.4    Seki, T.5
  • 23
    • 0025477749 scopus 로고
    • Improved method for fluorescence labeling of sugar chains with sialic acid residues
    • Kondo A., Suzuki J., Kuraya N., Hase S., Kato I., Ikenaka T. Improved method for fluorescence labeling of sugar chains with sialic acid residues. Agric. Biol. Chem. 1990, 54:2169-2170.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 2169-2170
    • Kondo, A.1    Suzuki, J.2    Kuraya, N.3    Hase, S.4    Kato, I.5    Ikenaka, T.6
  • 25
    • 1542358140 scopus 로고    scopus 로고
    • Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha 1,3-linked fucose
    • Strasser R., Altman F., Mach L., Glössl J., Steinkellner H. Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha 1,3-linked fucose. FEBS Lett. 2004, 561:132-136.
    • (2004) FEBS Lett. , vol.561 , pp. 132-136
    • Strasser, R.1    Altman, F.2    Mach, L.3    Glössl, J.4    Steinkellner, H.5
  • 27
    • 33646842291 scopus 로고    scopus 로고
    • Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogenously throughout the plant with mostly high-mannose-type N-glycans
    • Triguero A., Cabrera G., Cremata J.A., Yuen C.T., Wheeler J., Ramirez N.I. Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogenously throughout the plant with mostly high-mannose-type N-glycans. Plant Biotechnol. J. 2005, 3:449-457.
    • (2005) Plant Biotechnol. J. , vol.3 , pp. 449-457
    • Triguero, A.1    Cabrera, G.2    Cremata, J.A.3    Yuen, C.T.4    Wheeler, J.5    Ramirez, N.I.6
  • 31
    • 0021274996 scopus 로고
    • Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removal in protein bodies
    • Vitale A., Chrispeels M.J. Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removal in protein bodies. J. Cell Biol. 1984, 99:133-140.
    • (1984) J. Cell Biol. , vol.99 , pp. 133-140
    • Vitale, A.1    Chrispeels, M.J.2
  • 35
    • 16544390244 scopus 로고    scopus 로고
    • Unexpected deposition patterns of recombinant proteins in post-endoplasmic reticulum compartments of wheat endosperm
    • Arcalis E., Marcel S., Altmann F., Kolarich D., Drakakaki G., Fischer R., Christou P., Stoger E. Unexpected deposition patterns of recombinant proteins in post-endoplasmic reticulum compartments of wheat endosperm. Plant Physiol. 2004, 36:3457-3466.
    • (2004) Plant Physiol. , vol.36 , pp. 3457-3466
    • Arcalis, E.1    Marcel, S.2    Altmann, F.3    Kolarich, D.4    Drakakaki, G.5    Fischer, R.6    Christou, P.7    Stoger, E.8
  • 36
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa T., Nakamura K., Yamane N., Shoji-Hosaka E., Kanda Y., Sakurada M., Uchida K., Anazawa H., Satoh M., Yamasaki M., Hanai N., Shitara K. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 2003, 278:3466-3473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 40
    • 34248137611 scopus 로고    scopus 로고
    • Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human β(1,4)-galactosyltransferase
    • Fujiyama K., Furukawa A., Katsura A., Misaki R., Omasa T., Seki T. Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human β(1,4)-galactosyltransferase. Biochem. Biophys. Res. Commun. 2007, 358:85-91.
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 85-91
    • Fujiyama, K.1    Furukawa, A.2    Katsura, A.3    Misaki, R.4    Omasa, T.5    Seki, T.6
  • 41
    • 29044433720 scopus 로고    scopus 로고
    • Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell
    • Misaki R., Fujiyama K., Seki T. Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell. Biochem. Biophys. Res. Commun. 2006, 339:1184-1189.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 1184-1189
    • Misaki, R.1    Fujiyama, K.2    Seki, T.3
  • 42
    • 79953302385 scopus 로고    scopus 로고
    • Stable coexpression of two human sialylation enzymes in plant suspension-cultured tobacco cells
    • Kajiura H., Misaki R., Fujiyama K., Seki T. Stable coexpression of two human sialylation enzymes in plant suspension-cultured tobacco cells. J. Biosci. Bioeng. 2011, 111:471-477.
    • (2011) J. Biosci. Bioeng. , vol.111 , pp. 471-477
    • Kajiura, H.1    Misaki, R.2    Fujiyama, K.3    Seki, T.4
  • 43
    • 0032602265 scopus 로고    scopus 로고
    • Structures of N-linked oligosaccharides of glycoproteins from tobacco BY2 suspension cultured cells
    • Palacpac N.Q., Kimura Y., Fujiyama K., Yoshida T., Seki T. Structures of N-linked oligosaccharides of glycoproteins from tobacco BY2 suspension cultured cells. Biosci. Biotechnol. Biochem. 1999, 63:35-39.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 35-39
    • Palacpac, N.Q.1    Kimura, Y.2    Fujiyama, K.3    Yoshida, T.4    Seki, T.5


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