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Volumn 11, Issue 10, 2016, Pages 2734-2743

Facile Modulation of Antibody Fucosylation with Small Molecule Fucostatin Inhibitors and Cocrystal Structure with GDP-Mannose 4,6-Dehydratase

Author keywords

[No Author keywords available]

Indexed keywords

FUCOSE; GUANOSINE DIPHOSPHATE MANNOSE; HYDROLYASE; MOLECULAR LIBRARY;

EID: 84992176859     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00460     Document Type: Article
Times cited : (47)

References (45)
  • 1
    • 60849120154 scopus 로고    scopus 로고
    • Development and production of commercial therapeutic monoclonal antibodies in mammalian cell expression systems: An overview of the current upstream technologies
    • Chartrain, M. and Chu, L. (2008) Development and production of commercial therapeutic monoclonal antibodies in mammalian cell expression systems: an overview of the current upstream technologies Curr. Pharm. Biotechnol. 9, 447-467 10.2174/138920108786786367
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 447-467
    • Chartrain, M.1    Chu, L.2
  • 2
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker, D. J. and Lowe, J. B. (2003) Fucose: biosynthesis and biological function in mammals Glycobiology 13, 41R-53R 10.1093/glycob/cwg054
    • (2003) Glycobiology , vol.13 , pp. 41R-53R
    • Becker, D.J.1    Lowe, J.B.2
  • 3
    • 33746750608 scopus 로고    scopus 로고
    • Challenges in therapeutic glyoprotein production
    • Sethuraman, N. and Stadheim, T. A. (2006) Challenges in therapeutic glyoprotein production Curr. Opin. Biotechnol. 17, 341-346 10.1016/j.copbio.2006.06.010
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 341-346
    • Sethuraman, N.1    Stadheim, T.A.2
  • 4
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler, P., Khattak, S. F., and Li, Z. J. (2009) Optimal and consistent protein glycosylation in mammalian cell culture Glycobiology 19, 936-949 10.1093/glycob/cwp079
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1    Khattak, S.F.2    Li, Z.J.3
  • 5
    • 84979164980 scopus 로고    scopus 로고
    • Engineering of the product: Control of biotheraputics glycosylation
    • (Hauser, H. and Wagner, R. Eds), De Gruyter, Berlin
    • Vo Bennun, S., Heffner, K. M., Blake, E., Chung, A., and Betenbaugh, M. J. (2015) Engineering of the product: control of biotheraputics glycosylation, in Animal Cell Biotechnology (Hauser, H. and Wagner, R., Eds), pp 247-279, De Gruyter, Berlin.
    • (2015) Animal Cell Biotechnology , pp. 247-279
    • Vo Bennun, S.1    Heffner, K.M.2    Blake, E.3    Chung, A.4    Betenbaugh, M.J.5
  • 6
    • 0020728745 scopus 로고
    • Castanospermine, a tetrahydroxylated alkaloid that inhibits beta-glucosidase and beta-glucocerebrosidase
    • Saul, R., Chambers, J. P., Molyneux, R. J., and Elbein, A. D. (1983) Castanospermine, a tetrahydroxylated alkaloid that inhibits beta-glucosidase and beta-glucocerebrosidase Arch. Biochem. Biophys. 221, 593-597 10.1016/0003-9861(83)90181-9
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 593-597
    • Saul, R.1    Chambers, J.P.2    Molyneux, R.J.3    Elbein, A.D.4
  • 7
    • 0028328856 scopus 로고
    • A phase i study of swainsonine in patients with advanced malignancies
    • Goss, P. E., Baptiste, J., Fernandes, B., Baker, M., and Dennis, J. W. (1994) A phase I study of swainsonine in patients with advanced malignancies Cancer Res. 54, 1450-1457
    • (1994) Cancer Res. , vol.54 , pp. 1450-1457
    • Goss, P.E.1    Baptiste, J.2    Fernandes, B.3    Baker, M.4    Dennis, J.W.5
  • 8
    • 0028176432 scopus 로고
    • N-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis
    • Platt, F. M., Neises, G. R., Dwek, R. A., and Butters, T. D. (1994) N-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis J. Biol. Chem. 269, 8362-8365
    • (1994) J. Biol. Chem. , vol.269 , pp. 8362-8365
    • Platt, F.M.1    Neises, G.R.2    Dwek, R.A.3    Butters, T.D.4
  • 9
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • Goetze, A. M., Liu, Y. D., Zhang, Z., Shah, B., Lee, E., Bondarenko, P. V., and Flynn, G. C. (2011) High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans Glycobiology 21, 949-959 10.1093/glycob/cwr027
    • (2011) Glycobiology , vol.21 , pp. 949-959
    • Goetze, A.M.1    Liu, Y.D.2    Zhang, Z.3    Shah, B.4    Lee, E.5    Bondarenko, P.V.6    Flynn, G.C.7
  • 10
    • 84869234450 scopus 로고    scopus 로고
    • Metabolic inhibition of sialyl-Lewis X biosynthesis by 5-thiofucose remodels the cell surface and impairs selectin-mediated cell adhesion
    • Zandberg, W. F., Kumarasamy, J., Pinto, B. M., and Vocadlo, D. J. (2012) Metabolic inhibition of sialyl-Lewis X biosynthesis by 5-thiofucose remodels the cell surface and impairs selectin-mediated cell adhesion J. Biol. Chem. 287, 40021-40030 10.1074/jbc.M112.403568
    • (2012) J. Biol. Chem. , vol.287 , pp. 40021-40030
    • Zandberg, W.F.1    Kumarasamy, J.2    Pinto, B.M.3    Vocadlo, D.J.4
  • 12
    • 79951855712 scopus 로고    scopus 로고
    • Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells
    • Gloster, T. M., Zandberg, W. F., Heinonen, J. E., Shen, D. L., Deng, L., and Vocadlo, D. J. (2011) Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells Nat. Chem. Biol. 7, 174-181 10.1038/nchembio.520
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 174-181
    • Gloster, T.M.1    Zandberg, W.F.2    Heinonen, J.E.3    Shen, D.L.4    Deng, L.5    Vocadlo, D.J.6
  • 15
    • 84859977215 scopus 로고    scopus 로고
    • Fluorosugar chain termination agents as probes of the sequence specificity of a carbohydrate polymerase
    • Brown, C. D., Rusek, M. S., and Kiessling, L. L. (2012) Fluorosugar chain termination agents as probes of the sequence specificity of a carbohydrate polymerase J. Am. Chem. Soc. 134, 6552-6555 10.1021/ja301723p
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 6552-6555
    • Brown, C.D.1    Rusek, M.S.2    Kiessling, L.L.3
  • 16
    • 67649171495 scopus 로고    scopus 로고
    • Chemical approaches to perturb, profile, and perceive glycans
    • Agard, N. J. and Bertozzi, C. R. (2009) Chemical approaches to perturb, profile, and perceive glycans Acc. Chem. Res. 42, 788-797 10.1021/ar800267j
    • (2009) Acc. Chem. Res. , vol.42 , pp. 788-797
    • Agard, N.J.1    Bertozzi, C.R.2
  • 17
    • 84863245763 scopus 로고    scopus 로고
    • Chemoenzymatic probes for detecting and imaging fucose-α(1-2)-galactose glycan biomarkers
    • Chaubard, J. L., Krishnamurthy, C., Yi, W., Smith, D. F., and Hsieh-Wilson, L. C. (2012) Chemoenzymatic probes for detecting and imaging fucose-α(1-2)-galactose glycan biomarkers J. Am. Chem. Soc. 134, 4489-4492 10.1021/ja211312u
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 4489-4492
    • Chaubard, J.L.1    Krishnamurthy, C.2    Yi, W.3    Smith, D.F.4    Hsieh-Wilson, L.C.5
  • 19
    • 84923344751 scopus 로고    scopus 로고
    • The fucosylation inhibitor, 2-fluorofucose, inhibits vaso-occlulsion, leukocyte-endothelium interactions and NF-kB activation in transgenic sickle mice
    • Belcher, J. D., Chen, C., Nguyen, J., Abdulla, F., Nguyen, P., Nguyen, M., Okeley, N. M., Benjamin, D. R., Senter, P. D., and Vercellotti, G. M. (2015) The fucosylation inhibitor, 2-fluorofucose, inhibits vaso-occlulsion, leukocyte-endothelium interactions and NF-kB activation in transgenic sickle mice PLoS One 10 (2) e0117772 10.1371/journal.pone.0117772
    • (2015) PLoS One , vol.10 , Issue.2 , pp. e0117772
    • Belcher, J.D.1    Chen, C.2    Nguyen, J.3    Abdulla, F.4    Nguyen, P.5    Nguyen, M.6    Okeley, N.M.7    Benjamin, D.R.8    Senter, P.D.9    Vercellotti, G.M.10
  • 20
    • 0033868508 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis of fluorinated sugar nucleotide: Useful mechanistic probes for glycosyltransferases
    • Burkart, M. D., Vincent, S. P., Duffels, A., Murray, B. W., Ley, S. V., and Wong, C.-H. (2000) Chemo-enzymatic synthesis of fluorinated sugar nucleotide: useful mechanistic probes for glycosyltransferases Bioorg. Med. Chem. 8, 1937-1946 10.1016/S0968-0896(00)00139-5
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 1937-1946
    • Burkart, M.D.1    Vincent, S.P.2    Duffels, A.3    Murray, B.W.4    Ley, S.V.5    Wong, C.-H.6
  • 21
    • 0028168457 scopus 로고
    • L -Fucose is accumulated via a specific transport system in eukaryotic cells
    • Wiese, T. J., Dunlap, J. A., and Yorek, M. A. (1994) l -Fucose is accumulated via a specific transport system in eukaryotic cells J. Biol. Chem. 269, 22705-22711
    • (1994) J. Biol. Chem. , vol.269 , pp. 22705-22711
    • Wiese, T.J.1    Dunlap, J.A.2    Yorek, M.A.3
  • 22
    • 37049088316 scopus 로고
    • Synthesis of trifluoromethyl analog of l -fucose and 6-deoxy- d -altrose Chem. Soc
    • Bansal, R. C., Dean, B., Hakomori, S.-I., and Toyokuni, T. J. (1991) Synthesis of trifluoromethyl analog of l -fucose and 6-deoxy- d -altrose Chem. Soc J. Chem. Soc., Chem. Commun. 796-798 10.1039/c39910000796
    • (1991) J. Chem. Soc., Chem. Commun. , pp. 796-798
    • Bansal, R.C.1    Dean, B.2    Hakomori, S.-I.3    Toyokuni, T.J.4
  • 23
    • 0018361781 scopus 로고
    • 2-Deoxy-2-fluoro- l -fucose and its effect on l -fucose-1-14C utilization in mammalian cells
    • Winterbourne, D. J., Butchard, C. G., and Kent, P. W. (1979) 2-Deoxy-2-fluoro- l -fucose and its effect on l -fucose-1-14C utilization in mammalian cells Biochem. Biophys. Res. Commun. 87, 989-992 10.1016/S0006-291X(79)80004-2
    • (1979) Biochem. Biophys. Res. Commun. , vol.87 , pp. 989-992
    • Winterbourne, D.J.1    Butchard, C.G.2    Kent, P.W.3
  • 26
    • 78650849540 scopus 로고    scopus 로고
    • The C-glucosyl bond of puerarin was cleaved hydrolytically by a human intestinal bacterium strain PUE to yield its aglycone daidzein and an intact glucose
    • Nakamura, K., Nishihata, T., Jin, J.-S., Ma, C.-M., Komatsu, K., Iwashima, M., and Hattori, M. (2011) The C-glucosyl bond of puerarin was cleaved hydrolytically by a human intestinal bacterium strain PUE to yield its aglycone daidzein and an intact glucose Chem. Pharm. Bull. 59, 23-27 10.1248/cpb.59.23
    • (2011) Chem. Pharm. Bull. , vol.59 , pp. 23-27
    • Nakamura, K.1    Nishihata, T.2    Jin, J.-S.3    Ma, C.-M.4    Komatsu, K.5    Iwashima, M.6    Hattori, M.7
  • 28
    • 0032478832 scopus 로고    scopus 로고
    • Molecular cloning of human GDP-mannose 4,6-dehydratase and reconstitution of GDP-fucose biosynthesis in vitro
    • Sullivan, F. X., Kumar, R., Kriz, R., Stahl, M., Xu, G.-Y., Rouse, J., Chang, X., Boodhoo, A., Potvin, B., and Cumming, D. A. (1998) Molecular cloning of human GDP-mannose 4,6-dehydratase and reconstitution of GDP-fucose biosynthesis in vitro J. Biol. Chem. 273, 8193-8202 10.1074/jbc.273.14.8193
    • (1998) J. Biol. Chem. , vol.273 , pp. 8193-8202
    • Sullivan, F.X.1    Kumar, R.2    Kriz, R.3    Stahl, M.4    Xu, G.-Y.5    Rouse, J.6    Chang, X.7    Boodhoo, A.8    Potvin, B.9    Cumming, D.A.10
  • 31
    • 84929957067 scopus 로고    scopus 로고
    • Monensin, a small molecule ionophore, can be used to increase high mannose levels on monoclonal antibodies generated by Chinese hamster ovary production cell-lines
    • Pande, S., Rahardjo, A., Livingston, B., and Mujacic, M. (2015) Monensin, a small molecule ionophore, can be used to increase high mannose levels on monoclonal antibodies generated by Chinese hamster ovary production cell-lines Biotechnol. Bioeng. 112, 1383-1394 10.1002/bit.25551
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 1383-1394
    • Pande, S.1    Rahardjo, A.2    Livingston, B.3    Mujacic, M.4
  • 32
    • 0034651725 scopus 로고    scopus 로고
    • Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose
    • Somoza, J. R., Menon, S., Schmidt, H., Joseph-McCarthy, D., Dessen, A., Stahl, M. L., Somers, W. S., and Sullivan, F. X. (2000) Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose Structure 8, 123-135 10.1016/S0969-2126(00)00088-5
    • (2000) Structure , vol.8 , pp. 123-135
    • Somoza, J.R.1    Menon, S.2    Schmidt, H.3    Joseph-McCarthy, D.4    Dessen, A.5    Stahl, M.L.6    Somers, W.S.7    Sullivan, F.X.8
  • 33
    • 0842328952 scopus 로고    scopus 로고
    • Active site mapping of 2-deoxy-scyllo-inosose synthase, the key starter enzyme for the biosynthesis of 2-deoxystreptamine. Mechanism-based inhibition and identification of lysine-141 as the entrapped nucleophile
    • Nango, E., Eguchi, T., and Kakinuma, K. (2004) Active site mapping of 2-deoxy-scyllo-inosose synthase, the key starter enzyme for the biosynthesis of 2-deoxystreptamine. Mechanism-based inhibition and identification of lysine-141 as the entrapped nucleophile J. Org. Chem. 69, 593-600 10.1021/jo034706y
    • (2004) J. Org. Chem. , vol.69 , pp. 593-600
    • Nango, E.1    Eguchi, T.2    Kakinuma, K.3
  • 34
    • 0017566996 scopus 로고
    • Mechanism of inactivation of γ-cystathionase by β,β,β-trifluoroalanine
    • Silverman, R. B. and Abeles, R. H. (1977) Mechanism of inactivation of γ-cystathionase by β,β,β-trifluoroalanine Biochemistry 16, 5515-5520 10.1021/bi00644a019
    • (1977) Biochemistry , vol.16 , pp. 5515-5520
    • Silverman, R.B.1    Abeles, R.H.2
  • 35
    • 0032560956 scopus 로고    scopus 로고
    • CDP-6-deoxy-6,6-difluoro- d -glucose: A mechanism-based inhibitor for CDP- d -glucose 4,6-dehydratase
    • Chang, C-H. W. T, Chen, X. H., and Liu, H.-W. (1998) CDP-6-deoxy-6,6-difluoro- d -glucose: a mechanism-based inhibitor for CDP- d -glucose 4,6-dehydratase J. Am. Chem. Soc. 120, 9698-9699 10.1021/ja982198h
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9698-9699
    • Chang, C.-H.W.T.1    Chen, X.H.2    Liu, H.-W.3
  • 36
    • 84871770952 scopus 로고    scopus 로고
    • A critical review of the role of Fc gamma receptor polymorphisms in the response to monoclonal antibodies in cancer
    • Mellor, J. D., Brown, M. P., Irving, H. R., Zalcberg, J. R., and Dobrovic, A. (2013) A critical review of the role of Fc gamma receptor polymorphisms in the response to monoclonal antibodies in cancer J. Hematol. Oncol. 6, 1-10 10.1186/1756-8722-6-1
    • (2013) J. Hematol. Oncol. , vol.6 , pp. 1-10
    • Mellor, J.D.1    Brown, M.P.2    Irving, H.R.3    Zalcberg, J.R.4    Dobrovic, A.5
  • 37
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgRIIIagene
    • Cartron, G., Dacheux, L., Salles, G., Solal-Celigny, P., Bardos, P., Colombat, P., and Watier, H. (2002) Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgRIIIagene Blood 99, 754-758 10.1182/blood.V99.3.754
    • (2002) Blood , vol.99 , pp. 754-758
    • Cartron, G.1    Dacheux, L.2    Salles, G.3    Solal-Celigny, P.4    Bardos, P.5    Colombat, P.6    Watier, H.7
  • 38
  • 39
    • 33645107042 scopus 로고    scopus 로고
    • Reaction mechanism and substrate specificity for nucleotide sugar of mammalian alpha1,6-fucosyltransferase - A large-scale preparation and characterization of recombinant human FUT8
    • Ihara, H., Ikeda, Y., and Taniguchi, N. (2006) Reaction mechanism and substrate specificity for nucleotide sugar of mammalian alpha1,6-fucosyltransferase - a large-scale preparation and characterization of recombinant human FUT8 Glycobiology 16, 333-342
    • (2006) Glycobiology , vol.16 , pp. 333-342
    • Ihara, H.1    Ikeda, Y.2    Taniguchi, N.3
  • 40
    • 0033826441 scopus 로고    scopus 로고
    • Novel approaches for designing 5′-O-ester prodrugs of 3′-Azido-2′,3′-dideoxythymidine (AZT)
    • Parang, K., Wiebe, L. I., and Knaus, E. E. (2000) Novel approaches for designing 5′-O-ester prodrugs of 3′-Azido-2′,3′-dideoxythymidine (AZT) Curr. Med. Chem. 7, 995-1039 10.2174/0929867003374372
    • (2000) Curr. Med. Chem. , vol.7 , pp. 995-1039
    • Parang, K.1    Wiebe, L.I.2    Knaus, E.E.3
  • 41
    • 33947578642 scopus 로고    scopus 로고
    • Comparative and phylogenetic analysis of α- L -fucosidase genes
    • Intra, J., Perotti, M.-E., Pavesi, G., and Horner, D. (2007) Comparative and phylogenetic analysis of α- l -fucosidase genes Gene 392, 34-46 10.1016/j.gene.2006.11.002
    • (2007) Gene , vol.392 , pp. 34-46
    • Intra, J.1    Perotti, M.-E.2    Pavesi, G.3    Horner, D.4
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-rays diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-rays diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326 10.1016/S0076-6879(97)76066-X
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45


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