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Volumn 450, Issue 2, 2014, Pages 953-960

Cloning, expression and characterization of Bombyx mori α1,6-fucosyltransferase

Author keywords

Bombyx mori; Core 1,6 fucosylation; 1,6 Fucosyltransferase

Indexed keywords

ALPHA1,6 FUCOSYLTRANSFERASE; AMINO ACID; COMPLEMENTARY DNA; GLYCAN DERIVATIVE; GLYCOPROTEIN; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 84905117450     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.06.087     Document Type: Article
Times cited : (10)

References (29)
  • 1
    • 0032906430 scopus 로고    scopus 로고
    • Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
    • R. Oriol, R. Mollicone, A. Cailleau, L. Balanzino, and C. Breton Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria Glycobiology 9 1999 324 334
    • (1999) Glycobiology , vol.9 , pp. 324-334
    • Oriol, R.1    Mollicone, R.2    Cailleau, A.3    Balanzino, L.4    Breton, C.5
  • 4
    • 33749045903 scopus 로고    scopus 로고
    • Decoding sugar functions by identifying target glycoproteins
    • DOI 10.1016/j.sbi.2006.08.011, PII S0959440X06001461, Carbohydrates and Glycoconjugates / Biophysical Methods
    • N. Taniguchi, E. Miyoshi, J. Gu, K. Honke, and A. Matsumoto Decoding sugar functions by identifying target glycoproteins Curr. Opin. Struct. Biol. 16 2006 561 566 (Pubitemid 44466412)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.5 , pp. 561-566
    • Taniguchi, N.1    Miyoshi, E.2    Jianguo, G.3    Honke, K.4    Matsumoto, A.5
  • 5
    • 0017193878 scopus 로고
    • The control of glycoprotein synthesis: N-acetylglucosamine linkage to a mannose residue as a signal for the attachment of l-fucose to the asparagine-linked N-acetylglucosamine residue of glycopeptide from alpha1-acid glycoprotein
    • J.R. Wilson, D. Williams, and H. Schachter The control of glycoprotein synthesis: N-acetylglucosamine linkage to a mannose residue as a signal for the attachment of l-fucose to the asparagine-linked N-acetylglucosamine residue of glycopeptide from alpha1-acid glycoprotein Biochem. Biophys. Res. Commun. 72 1976 909 916
    • (1976) Biochem. Biophys. Res. Commun. , vol.72 , pp. 909-916
    • Wilson, J.R.1    Williams, D.2    Schachter, H.3
  • 6
    • 0020108081 scopus 로고
    • Product-identification and substrate-specificity studies of the GDP-l-fucose:2-acetamido-2-deoxy-β-d-glucoside (FUC goes to Asn-linked GlcNAc) 6-α-l-fucosyltransferase in a Golgi-rich fraction from porcine liver
    • G.D. Longmore, and H. Schachter Product-identification and substrate-specificity studies of the GDP-l-fucose:2-acetamido-2-deoxy-β-d- glucoside (FUC goes to Asn-linked GlcNAc) 6-α-l-fucosyltransferase in a Golgi-rich fraction from porcine liver Carbohydr. Res. 100 1982 365 392
    • (1982) Carbohydr. Res. , vol.100 , pp. 365-392
    • Longmore, G.D.1    Schachter, H.2
  • 7
    • 0025789667 scopus 로고
    • Purification and characterization of GDP-L-fucose-N-acetyl β-D-glucosaminide α1→6fucosyltransferase from cultured human skin fibroblasts: Requirement of a specific biantennary oligosaccharide as substrate
    • J.A. Voynow, R.S. Kaiser, T.F. Scanlin, and M.C. Glick Purification and characterization of GDP-l-fucose-n-acetyl β-d-glucosaminide α1,6-fucosyltransferase from cultured human skin fibroblasts. Requirement of a specific biantennary oligosaccharide as substrate J. Biol. Chem. 266 1991 21572 21577 (Pubitemid 121000221)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.32 , pp. 21572-21577
    • Voynow, J.A.1    Kaiser, R.S.2    Scanlin, T.F.3    Glick, M.C.4
  • 8
    • 33645107042 scopus 로고    scopus 로고
    • Reaction mechanism and substrate specificity for nucleotide sugar of mammalian α1,6-fucosyltransferase - A large-scale preparation and characterization of recombinant human FUT8
    • H. Ihara, Y. Ikeda, and N. Taniguchi Reaction mechanism and substrate specificity for nucleotide sugar of mammalian α1,6-fucosyltransferase - a large-scale preparation and characterization of recombinant human FUT8 Glycobiology 16 2006 333 342
    • (2006) Glycobiology , vol.16 , pp. 333-342
    • Ihara, H.1    Ikeda, Y.2    Taniguchi, N.3
  • 10
    • 77954471013 scopus 로고    scopus 로고
    • Fucosylation of chitooligosaccharides by human α1,6- fucosyltransferase requires a non-reducing terminal chitotriose unit as a minimal structure
    • H. Ihara, S. Hanashima, T. Okada, R. Ito, Y. Yamaguchi, N. Taniguchi, and Y. Ikeda Fucosylation of chitooligosaccharides by human α1,6- fucosyltransferase requires a non-reducing terminal chitotriose unit as a minimal structure Glycobiology 20 2010 1021 1033
    • (2010) Glycobiology , vol.20 , pp. 1021-1033
    • Ihara, H.1    Hanashima, S.2    Okada, T.3    Ito, R.4    Yamaguchi, Y.5    Taniguchi, N.6    Ikeda, Y.7
  • 12
    • 84866661292 scopus 로고
    • Donor substrate binding and enzymatic mechanism of human core α1,6-fucosyltransferase (FUT8)
    • M.P. Kötzler, S. Blank, F.T. Bantleon, E. Spillner, and B. Meyer Donor substrate binding and enzymatic mechanism of human core α1,6-fucosyltransferase (FUT8) Biochim. Biophys. Acta 2012 1820 1915 1925
    • (1820) Biochim. Biophys. Acta , vol.2012 , pp. 1915-1925
    • Kötzler, M.P.1    Blank, S.2    Bantleon, F.T.3    Spillner, E.4    Meyer, B.5
  • 14
    • 24044466162 scopus 로고    scopus 로고
    • Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates
    • DOI 10.1093/glycob/cwi028
    • K. Paschinger, E. Staudacher, U. Stemmer, G. Fabini, and I.B. Wilson Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates Glycobiology 15 2005 463 474 (Pubitemid 41214392)
    • (2005) Glycobiology , vol.15 , Issue.5 , pp. 463-474
    • Paschinger, K.1    Staudacher, E.2    Stemmer, U.3    Fabini, G.4    Wilson, I.B.H.5
  • 15
    • 0028236119 scopus 로고
    • Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N)
    • DOI 10.1006/abbi.1994.1021
    • V. Kubelka, F. Altmann, G. Kornfeld, and L. März Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N) Arch. Biochem. Biophys. 308 1994 148 157 (Pubitemid 24172616)
    • (1994) Archives of Biochemistry and Biophysics , vol.308 , Issue.1 , pp. 148-157
    • Kubelka, V.1    Altmann, F.2    Kornfeld, G.3    Marz, L.4
  • 16
    • 67651001558 scopus 로고    scopus 로고
    • Comparison of the N-linked glycosylation of human β1,3-N- acetylglucosaminyltransferase 2 expressed in insect cells and silkworm larvae
    • T. Dojima, T. Nishina, T. Kato, T. Uno, H. Yagi, K. Kato, and E.Y. Park Comparison of the N-linked glycosylation of human β1,3-N- acetylglucosaminyltransferase 2 expressed in insect cells and silkworm larvae J. Biotechnol. 143 2009 27 33
    • (2009) J. Biotechnol. , vol.143 , pp. 27-33
    • Dojima, T.1    Nishina, T.2    Kato, T.3    Uno, T.4    Yagi, H.5    Kato, K.6    Park, E.Y.7
  • 17
    • 84856298339 scopus 로고    scopus 로고
    • A new glycoengineered insect cell line with an inducibly mammalianized protein N-glycosylation pathway
    • J.J. Aumiller, H. Mabashi-Asazuma, A. Hillar, X. Shi, and D.L. Jarvis A new glycoengineered insect cell line with an inducibly mammalianized protein N-glycosylation pathway Glycobiology 22 2012 417 428
    • (2012) Glycobiology , vol.22 , pp. 417-428
    • Aumiller, J.J.1    Mabashi-Asazuma, H.2    Hillar, A.3    Shi, X.4    Jarvis, D.L.5
  • 18
    • 84894282237 scopus 로고    scopus 로고
    • A novel baculovirus vector for the production of non-fucosylated recombinant glycoproteins in insect cells
    • H. Mabashi-Asazuma, C.W. Kuo, K.H. Khoo, and D.L. Jarvis A novel baculovirus vector for the production of non-fucosylated recombinant glycoproteins in insect cells Glycobiology 24 2014 325 340
    • (2014) Glycobiology , vol.24 , pp. 325-340
    • Mabashi-Asazuma, H.1    Kuo, C.W.2    Khoo, K.H.3    Jarvis, D.L.4
  • 19
    • 77955447393 scopus 로고    scopus 로고
    • N-Glycosylation engineering of lepidopteran insect cells by the introduction of the β1,4-N-acetylglucosaminyltransferase III gene
    • T. Okada, H. Ihara, R. Ito, M. Nakano, K. Matsumoto, Y. Yamaguchi, N. Taniguchi, and Y. Ikeda N-Glycosylation engineering of lepidopteran insect cells by the introduction of the β1,4-N-acetylglucosaminyltransferase III gene Glycobiology 20 2010 1147 1159
    • (2010) Glycobiology , vol.20 , pp. 1147-1159
    • Okada, T.1    Ihara, H.2    Ito, R.3    Nakano, M.4    Matsumoto, K.5    Yamaguchi, Y.6    Taniguchi, N.7    Ikeda, Y.8
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 84880485013 scopus 로고    scopus 로고
    • An assay for α1,6-fucosyltransferase (FUT8) activity based on the HPLC separation of a reaction product with fluorescence detection
    • H. Ihara, H. Tsukamoto, N. Taniguchi, and Y. Ikeda An assay for α1,6-fucosyltransferase (FUT8) activity based on the HPLC separation of a reaction product with fluorescence detection Methods Mol. Biol. 1022 2013 335 348
    • (2013) Methods Mol. Biol. , vol.1022 , pp. 335-348
    • Ihara, H.1    Tsukamoto, H.2    Taniguchi, N.3    Ikeda, Y.4
  • 23
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0034053074 scopus 로고    scopus 로고
    • A sequence motif involved in the donor substrate binding by α1,6-fucosyltransferase: The role of the conserved arginine residues
    • T. Takahashi, Y. Ikeda, A. Tateishi, Y. Yamaguchi, M. Ishikawa, and N. Taniguchi A sequence motif involved in the donor substrate binding by α1,6-fucosyltransferase: the role of the conserved arginine residues Glycobiology 10 2000 503 510 (Pubitemid 30216092)
    • (2000) Glycobiology , vol.10 , Issue.5 , pp. 503-510
    • Takahashi, T.1    Ikeda, Y.2    Tateishi, A.3    Yamaguchi, Y.4    Ishikawa, M.5    Taniguchi, N.6
  • 25
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity
    • DOI 10.1074/jbc.M202069200
    • R.L. Shields, J. Lai, R. Keck, L.Y. O'Connell, K. Hong, Y.G. Meng, S.H. Weikert, and L.G. Presta Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity J. Biol. Chem. 277 2002 26733 26740 (Pubitemid 34951677)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Gloria Meng, Y.6    Weikert, S.H.A.7    Presta, L.G.8
  • 26
    • 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
    • DOI 10.1074/jbc.M210665200
    • T. Shinkawa, K. Nakamura, N. Yamane, E. Shoji-Hosaka, Y. Kanda, M. Sakurada, K. Uchida, H. Anazawa, M. Satoh, M. Yamasaki, N. Hanai, and K. Shitara 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. 278 2003 3466 3473 (Pubitemid 36801263)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , 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
  • 27
    • 38649143213 scopus 로고    scopus 로고
    • Double knockdown of α1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: A new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC
    • H. Imai-Nishiya, K. Mori, M. Inoue, M. Wakitani, S. Iida, K. Shitara, and M. Satoh Double knockdown of α1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: a new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC BMC Biotechnol. 7 2007 84
    • (2007) BMC Biotechnol. , vol.7 , pp. 84
    • Imai-Nishiya, H.1    Mori, K.2    Inoue, M.3    Wakitani, M.4    Iida, S.5    Shitara, K.6    Satoh, M.7
  • 29
    • 84864245160 scopus 로고    scopus 로고
    • Effect of bisecting GlcNAc and core fucosylation on conformational properties of biantennary complex-type N-glycans in solution
    • W. Nishima, N. Miyashita, Y. Yamaguchi, Y. Sugita, and S. Re Effect of bisecting GlcNAc and core fucosylation on conformational properties of biantennary complex-type N-glycans in solution J. Phys. Chem. B 116 2012 8504 8512
    • (2012) J. Phys. Chem. B , vol.116 , pp. 8504-8512
    • Nishima, W.1    Miyashita, N.2    Yamaguchi, Y.3    Sugita, Y.4    Re, S.5


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