請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/58285
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 翁啟惠(Chi-Huey Wong) | |
dc.contributor.author | Tsung-I Tsai | en |
dc.contributor.author | 蔡宗義 | zh_TW |
dc.date.accessioned | 2021-06-16T08:10:18Z | - |
dc.date.available | 2019-07-10 | |
dc.date.copyright | 2014-07-10 | |
dc.date.issued | 2014 | |
dc.date.submitted | 2014-03-27 | |
dc.identifier.citation | 1. Hakomori S-i. Structure and function of glycosphingolipids and sphingolipids: Recollections and future trends. Biochim Biophys Acta, Gen Subj. 2008;1780(3):325-46.
2. Hakomori S-I, Zhang Y. Glycosphingolipid antigens and cancer therapy. Chem Biol. 1997;4(2):97-104. 3. Zhang S, Cordon-Cardo C, Zhang HS, Reuter VE, Adluri S, Hamilton WB, et al. Selection of tumor antigens as targets for immune attack using immunohistochemistry: I. Focus on gangliosides. Int J Cancer. 1997;73(1):42-9. 4. Zhang S, Zhang HS, Cordon-Cardo C, Reuter VE, Singhal AK, Lloyd KO, et al. Selection of tumor antigens as targets for immune attack using immunohistochemistry: II. Blood group-related antigens. Int J Cancer. 1997;73(1):50-6. 5. Kannagi R, Levery SB, Ishigami F, Hakomori S, Shevinsky LH, Knowles BB, et al. New globoseries glycosphingolipids in human teratocarcinoma reactive with the monoclonal antibody directed to a developmentally regulated antigen, stage-specific embryonic antigen 3. J Biol Chem. 1983;258(14):8934-42. 6. Kannagi R, Cochran NA, Ishigami F, Hakomori S, Andrews PW, Knowles BB, et al. Stage-specific embryonic antigens (SSEA-3 and -4) are epitopes of a unique globo-series ganglioside isolated from human teratocarcinoma cells. EMBO J. 1983;2(12):2355-61. 7. Bremer EG, Levery SB, Sonnino S, Ghidoni R, Canevari S, Kannagi R, et al. Characterization of a glycosphingolipid antigen defined by the monoclonal antibody MBr1 expressed in normal and neoplastic epithelial cells of human mammary gland. J Biol Chem. 1984;259(23):14773-7. 8. Menard S, Tagliabue E, Canevari S, Fossati G, Colnaghi MI. Generation of Monoclonal Antibodies Reacting with Normal and Cancer Cells of Human Breast. Cancer Res. 1983;43(3):1295-300. 9. Canevari S, Fossati G, Balsari A, Sonnino S, Colnaghi MI. Immunochemical Analysis of the Determinant Recognized by a Monoclonal Antibody (MBr1) Which Specifically Binds to Human Mammary Epithelial Cells. Cancer Res. 1983;43(3):1301-5. 10. Ragupathi G, Slovin SF, Adluri S, Sames D, Kim IJ, Kim HM, et al. A Fully Synthetic Globo H Carbohydrate Vaccine Induces a Focused Humoral Response in Prostate Cancer Patients: A Proof of Principle. Angew Chem Int Ed. 1999;38(4):563-6. 11. Perrone F, Menard S, Canevari S, Calabrese M, Boracchi P, Bufalino R, et al. Prognostic significance of the CaMBr1 antigen on breast carcinoma: Relevance of the type of recognised glycoconjugate. Eur J Cancer. 1993;29(15):2113-7. 12. Martignone S, Menard S, Bedini A, Paccagnella A, Fasolato S, Veggian R, et al. Study of the expression and function of the tumour-associated antigen CaMBr1 in small cell lung carcinomas. Eur J Cancer. 1993;29(14):2020-5. 13. Slovin SF, Ragupathi G, Adluri S, Ungers G, Terry K, Kim S, et al. Carbohydrate vaccines in cancer: Immunogenicity of a fully synthetic globo H hexasaccharide conjugate in man. Proc Natl Acad Sci USA. 1999;96(10):5710-5. 14. Wang Z-G, Williams LJ, Zhang X-F, Zatorski A, Kudryashov V, Ragupathi G, et al. Polyclonal antibodies from patients immunized with a globo H-keyhole limpet hemocyanin vaccine: Isolation, quantification, and characterization of immune responses by using totally synthetic immobilized tumor antigens. Proc Natl Acad Sci USA. 2000;97(6):2719-24. 15. Gilewski T, Ragupathi G, Bhuta S, Williams LJ, Musselli C, Zhang X-F, et al. Immunization of metastatic breast cancer patients with a fully synthetic globo H conjugate: A phase I trial. Proc Natl Acad Sci USA. 2001;98(6):3270-5. 16. Burkhart F, Zhang Z, Wacowich-Sgarbi S, Wong C-H. Synthesis of the Globo H Hexasaccharide Using the Programmable Reactivity-Based One-Pot Strategy. Angew Chem Int Ed. 2001;40(7):1274-7. 17. Chang W-W, Lee CH, Lee P, Lin J, Hsu C-W, Hung J-T, et al. Expression of Globo H and SSEA3 in breast cancer stem cells and the involvement of fucosyl transferases 1 and 2 in Globo H synthesis. Proc Natl Acad Sci USA. 2008;105(33):11667-72. 18. Huang Y-L, Hung J-T, Cheung SKC, Lee H-Y, Chu K-C, Li S-T, et al. Carbohydrate-based vaccines with a glycolipid adjuvant for breast cancer. Proc Natl Acad Sci USA. 2013;110(7):2517-22. 19. Huang C-Y, Thayer DA, Chang AY, Best MD, Hoffmann J, Head S, et al. Carbohydrate microarray for profiling the antibodies interacting with Globo H tumor antigen. Proc Natl Acad Sci USA. 2006;103(1):15-20. 20. Wang C-C, Huang Y-L, Ren C-T, Lin C-W, Hung J-T, Yu J-C, et al. Glycan microarray of Globo H and related structures for quantitative analysis of breast cancer. Proc Natl Acad Sci USA. 2008;105(33):11661-6. 21. Slamon DJ, Leyland-Jones B, Shak S, Fuchs H, Paton V, Bajamonde A, et al. Use of Chemotherapy plus a Monoclonal Antibody against HER2 for Metastatic Breast Cancer That Overexpresses HER2. N Engl J Med. 2001;344(11):783-92. 22. Allen JR, Allen JG, Zhang X-F, Williams LJ, Zatorski A, Ragupathi G, et al. A Second Generation Synthesis of the MBr1 (Globo-H) Breast Tumor Antigen: New Application of the n-Pentenyl Glycoside Method for Achieving Complex Carbohydrate Protein Linkages. Chem Eur J. 2000;6(8):1366-75. 23. Wong CH, Haynie SL, Whitesides GM. Enzyme-catalyzed synthesis of N-acetyllactosamine with in situ regeneration of uridine 5'-diphosphate glucose and uridine 5'-diphosphate galactose. J Org Chem. 1982;47(27):5416-8. 24. Bilodeau MT, Park TK, Hu S, Randolph JT, Danishefsky SJ, Livingston PO, et al. Total Synthesis of a Human Breast Tumor Associated Antigen. J Am Chem Soc. 1995;117(29):7840-1. 25. Park TK, Kim IJ, Hu S, Bilodeau MT, Randolph JT, Kwon O, et al. Total Synthesis and Proof of Structure of a Human Breast Tumor (Globo-H) Antigen. J Am Chem Soc. 1996;118(46):11488-500. 26. Bosse F, Marcaurelle LA, Seeberger PH. Linear Synthesis of the Tumor-Associated Carbohydrate Antigens Globo-H, SSEA-3, and Gb3. J Org Chem. 2002;67(19):6659-70. 27. Werz DB, Castagner B, Seeberger PH. Automated Synthesis of the Tumor-Associated Carbohydrate Antigens Gb-3 and Globo-H: Incorporation of α-Galactosidic Linkages. J Am Chem Soc. 2007;129(10):2770-1. 28. Wang Z, Zhou L, El-Boubbou K, Ye X-s, Huang X. Multi-Component One-Pot Synthesis of the Tumor-Associated Carbohydrate Antigen Globo-H Based on Preactivation of Thioglycosyl Donors. J Org Chem. 2007;72(17):6409-20. 29. Jeong JK, Kwon O, Lee YM, Oh D-B, Lee JM, Kim S, et al. Characterization of the Streptococcus pneumoniae BgaC Protein as a Novel Surface β-Galactosidase with Specific Hydrolysis Activity for the Galβ1-3GlcNAc Moiety of Oligosaccharides. J Bacteriol. 2009;191(9):3011-23. 30. Hsu C-H, Chu K-C, Lin Y-S, Han J-L, Peng Y-S, Ren C-T, et al. Highly Alpha-Selective Sialyl Phosphate Donors for Efficient Preparation of Natural Sialosides. Chem Eur J. 2010;16(6):1754-60. 31. Wang Z, Gilbert M, Eguchi H, Yu H, Cheng J, Muthana S, et al. Chemoenzymatic Syntheses of Tumor-Associated Carbohydrate Antigen Globo-H and Stage-Specific Embryonic Antigen 4. Adv Synth Catal. 2008;350(11-12):1717-28. 32. Mizanur RM, Pohl NLB. Phosphomannose isomerase/GDP-mannose pyrophosphorylase from Pyrococcus furiosus: a thermostable biocatalyst for the synthesis of guanidinediphosphate-activated and mannose-containing sugar nucleotides. Organic & Biomolecular Chemistry. 2009;7(10):2135-9. 33. Schmaltz RM, Hanson SR, Wong C-H. Enzymes in the Synthesis of Glycoconjugates. Chem Rev. 2011;111(7):4259-307. 34. Gijsen HJM, Qiao L, Fitz W, Wong C-H. Recent Advances in the Chemoenzymatic Synthesis of Carbohydrates and Carbohydrate Mimetics. Chem Rev. 1996;96(1):443-74. 35. Su DM, Eguchi H, Yi W, Li L, Wang PG, Xia C. Enzymatic Synthesis of Tumor-Associated Carbohydrate Antigen Globo-H Hexasaccharide. Org Lett. 2008;10(5):1009-12. 36. Wong C-H, Wang R, Ichikawa Y. Regeneration of sugar nucleotide for enzymic oligosaccharide synthesis: use of Gal-1-phosphate uridyltransferase in the regeneration of UDP-galactose, UDP-2-deoxygalactose, and UDP-galactosamine. J Org Chem. 1992;57(16):4343-4. 37. Kotake T, Yamaguchi D, Ohzono H, Hojo S, Kaneko S, Ishida H-k, et al. UDP-sugar Pyrophosphorylase with Broad Substrate Specificity Toward Various Monosaccharide 1-Phosphates from Pea Sprouts. J Biol Chem. 2004;279(44):45728-36. 38. Litterer LA, Schnurr JA, Plaisance KL, Storey KK, Gronwald JW, Somers DA. Characterization and expression of Arabidopsis UDP-sugar pyrophosphorylase. Plant Physiol Biochem. 2006;44(4):171-80. 39. Kotake T, Hojo S, Yamaguchi D, Aohara T, Konishi T, Tsumuraya Y. Properties and Physiological Functions of UDP-Sugar Pyrophosphorylase in Arabidopsis. Biosci, Biotechnol, Biochem. 2007;71(3):761-71. 40. Muthana MM, Qu J, Li Y, Zhang L, Yu H, Ding L, et al. Efficient one-pot multienzyme synthesis of UDP-sugars using a promiscuous UDP-sugar pyrophosphorylase from Bifidobacterium longum (BLUSP). Chem Commun. 2012;48(21):2728-30. 41. Damerow S, Lamerz A-C, Haselhorst T, Fuhring J, Zarnovican P, von Itzstein M, et al. Leishmania UDP-sugar Pyrophosphorylase. J Biol Chem. 2010;285(2):878-87. 42. Malekan H, Fung G, Thon V, Khedri Z, Yu H, Qu J, et al. One-pot multi-enzyme (OPME) chemoenzymatic synthesis of sialyl-Tn-MUC1 and sialyl-T-MUC1 glycopeptides containing natural or non-natural sialic acid. Biorg Med Chem. 2013;21(16):4778-85. 43. Persson K, Ly HD, Dieckelmann M, Wakarchuk WW, Withers SG, Strynadka NCJ. Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs. Nat Struct Mol Biol. 2001;8(2):166-75. 44. Antoine T, Bosso C, Heyraud A, Samain E. Large scale in vivo synthesis of globotriose and globotetraose by high cell density culture of metabolically engineered Escherichia coli. Biochimie. 2005;87(2):197-203. 45. Shao J, Zhang J, Kowal P, Lu Y, George Wang P. Overexpression and biochemical characterization of [beta]-1,3-N-acetylgalactosaminyltransferase LgtD from Haemophilus influenzae strain Rd. Biochem Biophys Res Commun. 2002;295(1):1-8. 46. Shao J, Zhang J, Kowal P, Lu Y, Wang PG. Efficient synthesis of globoside and isogloboside tetrasaccharides by using β(1→3)N-acetylgalactosaminyltransferase/UDP-N-acetylglucosamine C4 epimerase fusion protein. Chem Commun. 2003(12):1422-3. 47. Shao J, Zhang J, Kowal P, Wang PG. Donor Substrate Regeneration for Efficient Synthesis of Globotetraose and Isoglobotetraose. Appl Environ Microbiol. 2002;68(11):5634-40. 48. Vanessa B, Martine C, Friedrich P, Veronique P. Efficient Enzymatic Glycosylation of Peptides and Oligosaccharides from GalNAc and UTP. ChemBioChem. 2007;8(1):37-40. 49. Nishimoto M, Kitaoka M. Identification of N-Acetylhexosamine 1-Kinase in the Complete Lacto-N-Biose I/Galacto-N-Biose Metabolic Pathway in Bifidobacterium longum. Appl Environ Microbiol. 2007;73(20):6444-9. 50. Agnew A, Timson D. Mechanistic studies on human N-acetylgalactosamine kinase. J Enzyme Inhib Med Chem. 2010;25(3):370-6. 51. Fang J, Guan W, Cai L, Gu G, Liu X, Wang PG. Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12. Bioorg Med Chem Lett. 2009;19(22):6429-32. 52. Hood DW, Cox AD, Wakarchuk WW, Schur M, Schweda EKH, Walsh SL, et al. Genetic basis for expression of the major globotetraose-containing lipopolysaccharide from H. influenzae strain Rd (RM118). Glycobiology. 2001;11(11):957-67. 53. Randriantsoa M, Drouillard S, Breton C, Samain E. Synthesis of globopentaose using a novel [beta]1,3-galactosyltransferase activity of the Haemophilus influenzae [beta]1,3-N-acetylgalactosaminyltransferase LgtD. FEBS Lett. 2007;581(14):2652-6. 54. Coyne MJ, Reinap B, Lee MM, Comstock LE. Human Symbionts Use a Host-Like Pathway for Surface Fucosylation. Science. 2005;307(5716):1778-81. 55. Wang W, Hu T, Frantom PA, Zheng T, Gerwe B, del Amo DS, et al. Chemoenzymatic synthesis of GDP-l-fucose and the Lewis X glycan derivatives. Proc Natl Acad Sci USA. 2009;106(38):16096-101. 56. Koizumi S, Endo T, Tabata K, Nagano H, Ohnishi J, Ozaki A. Large-scale production of GDP-fucose and Lewis X by bacterial coupling. J Ind Microbiol Biotechnol. 2000;25(4):213-7. 57. Stein Daniel B, Lin Y-N, Lin C-H. Characterization of Helicobacter pylori alpha1,2-Fucosyltransferase for Enzymatic Synthesis of Tumor-Associated Antigens. Adv Synth Catal. 2008;350(14-15):2313-21. 58. Tanner ME. The enzymes of sialic acid biosynthesis. Bioorg Chem. 2005;33(3):216-28. 59. Kushi Y, Kamimiya H, Hiratsuka H, Nozaki H, Fukui H, Yanagida M, et al. Sialyltransferases of marine bacteria efficiently utilize glycosphingolipid substrates. Glycobiology. 2010;20(2):187-98. 60. Yamamoto T. Marine Bacterial Sialyltransferases. Marine Drugs. 2010;8(11):2781-94. 61. Takakura Y, Tsukamoto H, Yamamoto T. Molecular Cloning, Expression and Properties of an α/β-Galactoside α2,3-Sialyltransferase from Vibrio sp. JT-FAJ-16. J Biochem. 2007;142(3):403-12. 62. Li Y, Yu H, Cao H, Muthana S, Chen X. Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity. Appl Microbiol Biotechnol. 2011:1-13. 63. Puigbo P, Guzman E, Romeu A, Garcia-Vallve S. OPTIMIZER: a web server for optimizing the codon usage of DNA sequences. Nucleic Acids Res. 2007;35(suppl 2):W126-W31. 64. Murray BW, Wittmann V, Burkart MD, Hung S-C, Wong C-H. Mechanism of Human α-1,3-Fucosyltransferase V: Glycosidic Cleavage Occurs Prior to Nucleophilic Attack†. Biochemistry. 1997;36(4):823-31. 65. Ghaderi D, Zhang M, Hurtado-Ziola N, Varki A. Production platforms for biotherapeutic glycoproteins. Occurrence, impact, and challenges of non-human sialylation. Biotechnol Genet Eng Rev. 2012;28(1):147-75. 66. Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins. Annual Review of Immunology. 2007;25(1):21-50. 67. Durocher Y, Butler M. Expression systems for therapeutic glycoprotein production. Curr Opin Biotechnol. 2009;20(6):700-7. 68. Lux A, Nimmerjahn F. Impact of Differential Glycosylation on IgG Activity. In: Pulendran B, Katsikis PD, Schoenberger SP, editors. Crossroads between Innate and Adaptive Immunity III. Advances in Experimental Medicine and Biology. 780: Springer New York; 2011. p. 113-24. 69. Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov. 2009;8(3):226-34. 70. Yamane-Ohnuki N, Satoh M. Production of therapeutic antibodies with controlled fucosylation. mAbs. 2009;1(3):230-6. 71. Hristodorov D, Fischer R, Linden L. With or Without Sugar? (A)glycosylation of Therapeutic Antibodies. Molecular Biotechnology. 2013;54(3):1056-68. 72. Ferrara C, Grau S, Jager C, Sondermann P, Brunker P, Waldhauer I, et al. Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose. Proc Natl Acad Sci USA. 2011;108(31):12669-74. 73. Ferrara C, Brunker P, Suter T, Moser S, Puntener U, Umana P. Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co-expression of heterologous β1, 4-N-acetylglucosaminyltransferase III and Golgi α-mannosidase II. Biotechnol Bioeng. 2006;93(5):851-61. 74. Mori K, Iida S, Yamane-Ohnuki N, Kanda Y, Kuni-Kamochi R, Nakano R, et al. Non-fucosylated therapeutic antibodies: the next generation of therapeutic antibodies. Cytotechnology. 2007;55(2-3):109-14. 75. Iida S, Misaka H, Inoue M, Shibata M, Nakano R, Yamane-Ohnuki N, et al. Nonfucosylated Therapeutic IgG1 Antibody Can Evade the Inhibitory Effect of Serum Immunoglobulin G on Antibody-Dependent Cellular Cytotoxicity through its High Binding to FcγRIIIa. Clinical Cancer Research. 2006;12(9):2879-87. 76. Kanda Y, Yamada T, Mori K, Okazaki A, Inoue M, Kitajima-Miyama K, et al. Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types. Glycobiology. 2007;17(1):104-18. 77. Malhotra R, Wormald MR, Rudd PM, Fischer PB, Dwek RA, Sim RB. Glycosylation changes of IgG associated with rheumatooid arthritis can activate complement via the mannose-binding protein. Nat Med. 1995;1(3):237-43. 78. Bosques CJ, Collins BE, Meador JW, Sarvaiya H, Murphy JL, DelloRusso G, et al. Chinese hamster ovary cells can produce galactose-[alpha]-1, 3-galactose antigens on proteins. Nat Biotech. 2011;29(5):459-. 79. Macher BA, Galili U. The Galα1,3Galβ1,4GlcNAc-R (α-Gal) epitope: A carbohydrate of unique evolution and clinical relevance. Biochim Biophys Acta, Gen Subj. 2008;1780(2):75-88. 80. Chung CH, Mirakhur B, Chan E, Le Q-T, Berlin J, Morse M, et al. Cetuximab-Induced Anaphylaxis and IgE Specific for Galactose-α-1,3-Galactose. N Engl J Med. 2008;358(11):1109-17. 81. Chou H-H, Takematsu H, Diaz S, Iber J, Nickerson E, Wright KL, et al. A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence. Proc Natl Acad Sci USA. 1998;95(20):11751-6. 82. Tangvoranuntakul P, Gagneux P, Diaz S, Bardor M, Varki N, Varki A, et al. Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid. Proc Natl Acad Sci USA. 2003;100(21):12045-50. 83. Padler-Karavani V, Yu H, Cao H, Chokhawala H, Karp F, Varki N, et al. Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: Potential implications for disease. Glycobiology. 2008;18(10):818-30. 84. Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation. Science. 2006;313(5787):670-3. 85. Anthony RM, Nimmerjahn F, Ashline DJ, Reinhold VN, Paulson JC, Ravetch JV. Recapitulation of IVIG Anti-Inflammatory Activity with a Recombinant IgG Fc. Science. 2008;320(5874):373-6. 86. Becker DJ, Lowe JB. Fucose: biosynthesis and biological function in mammals. Glycobiology. 2003;13(7):41R-53R. 87. Schiestl M, Stangler T, Torella C, Cepeljnik T, Toll H, Grau R. Acceptable changes in quality attributes of glycosylated biopharmaceuticals. Nat Biotech. 2011;29(4):310-2. 88. Miyoshi E, Noda K, Yamaguchi Y, Inoue S, Ikeda Y, Wang W, et al. The α1-6-fucosyltransferase gene and its biological significance. Biochim Biophys Acta, Gen Subj. 1999;1473(1):9-20. 89. Malphettes L, Freyvert Y, Chang J, Liu P-Q, Chan E, Miller JC, et al. Highly efficient deletion of FUT8 in CHO cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies. Biotechnol Bioeng. 2010;106(5):774-83. 90. Omasa T, Tanaka R, Doi T, Ando M, Kitamoto Y, Honda K, et al. Decrease in antithrombin III fucosylation by expressing GDP-fucose transporter siRNA in Chinese hamster ovary cells. J Biosci Bioeng. 2008;106(2):168-73. 91. Marino K, Bones J, Kattla JJ, Rudd PM. A systematic approach to protein glycosylation analysis: a path through the maze. Nat Chem Biol. 2010;6(10):713-23. 92. Tharmalingam T, Adamczyk B, Doherty M, Royle L, Rudd P. Strategies for the profiling, characterisation and detailed structural analysis of N-linked oligosaccharides. Glycoconjugate J. 2013;30(2):137-46. 93. Huang W, Giddens J, Fan S-Q, Toonstra C, Wang L-X. Chemoenzymatic Glycoengineering of Intact IgG Antibodies for Gain of Functions. J Am Chem Soc. 2012;134(29):12308-18. 94. Tsai T-I, Lee H-Y, Chang S-H, Wang C-H, Tu Y-C, Lin Y-C, et al. Effective Sugar Nucleotide Regeneration for the Large-Scale Enzymatic Synthesis of Globo H and SSEA4. J Am Chem Soc. 2013;135(39):14831-9. 95. Ninonuevo MR, Park Y, Yin H, Zhang J, Ward RE, Clowers BH, et al. A Strategy for Annotating the Human Milk Glycome. J Agric Food Chem. 2006;54(20):7471-80. 96. Kunz C, Rudloff S, Baier W, Klein N, Strobel S. OLIGOSACCHARIDES IN HUMAN MILK: Structural, Functional, and Metabolic Aspects. Annual Review of Nutrition. 2000;20(1):699-722. 97. Bode L. Human milk oligosaccharides: Every baby needs a sugar mama. Glycobiology. 2012;22(9):1147-62. 98. Lin K-I, Kao Y-Y, Kuo H-K, Yang W-B, Chou A, Lin H-H, et al. Reishi Polysaccharides Induce Immunoglobulin Production through the TLR4/TLR2-mediated Induction of Transcription Factor Blimp-1. J Biol Chem. 2006;281(34):24111-23. 99. Chien CM, Cheng J-L, Chang W-T, Tien M-H, Tsao C-M, Chang Y-H, et al. Polysaccharides of Ganoderma lucidum alter cell immunophenotypic expression and enhance CD56+ NK-cell cytotoxicity in cord blood. Biorg Med Chem. 2004;12(21):5603-9. 100. Liao S-F, Liang C-H, Ho M-Y, Hsu T-L, Tsai T-I, Hsieh YS-Y, et al. Immunization of fucose-containing polysaccharides from Reishi mushroom induces antibodies to tumor-associated Globo H-series epitopes. Proc Natl Acad Sci USA. 2013;110(34):13809-14. 101. Pang P-C, Chiu PCN, Lee C-L, Chang L-Y, Panico M, Morris HR, et al. Human Sperm Binding Is Mediated by the Sialyl-Lewisx Oligosaccharide on the Zona Pellucida. Science. 2011;333(6050):1761-4. 102. Sun H-Y, Lin S-W, Ko T-P, Pan J-F, Liu C-L, Lin C-N, et al. Structure and Mechanism of Helicobacter pylori Fucosyltransferase. J Biol Chem. 2007;282(13):9973-82. 103. Nilsson C, Skoglund A, Moran AP, Annuk H, Engstrand L, Normark S. An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection. Proc Natl Acad Sci USA. 2006;103(8):2863-8. 104. Xu J, Bjursell MK, Himrod J, Deng S, Carmichael LK, Chiang HC, et al. A Genomic View of the Human-Bacteroides thetaiotaomicron Symbiosis. Science. 2003;299(5615):2074-6. 105. Zhu Y, Suits MDL, Thompson AJ, Chavan S, Dinev Z, Dumon C, et al. Mechanistic insights into a Ca2+-dependent family of α-mannosidases in a human gut symbiont. Nat Chem Biol. 2010;6(2):125-32. 106. Katayama T, Sakuma A, Kimura T, Makimura Y, Hiratake J, Sakata K, et al. Molecular Cloning and Characterization of Bifidobacterium bifidum 1,2-α-l-Fucosidase (AfcA), a Novel Inverting Glycosidase (Glycoside Hydrolase Family 95). J Bacteriol. 2004;186(15):4885-93. 107. Cobucci-Ponzano B, Conte F, Rossi M, Moracci M. The α-l -fucosidase from Sulfolobus solfataricus. Extremophiles. 2008;12(1):61-8. 108. Eneyskaya EV, Kulminskaya AA, Kalkkinen N, Nifantiev NE, Arbatskii NP, Saenko AI, et al. An α-L-fucosidase from Thermus sp. with unusually broad specificity. Glycoconjugate J. 2001;18(10):827-34. 109. Ashida H, Miyake A, Kiyohara M, Wada J, Yoshida E, Kumagai H, et al. Two distinct α-l-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates. Glycobiology. 2009;19(9):1010-7. 110. Wong-Madden ST, Landry D. Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas. Glycobiology. 1995;5(1):19-28. 111. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(suppl 1):D233-D8. 112. Leonard R, Pabst M, Bondili JS, Chambat G, Veit C, Strasser R, et al. Identification of an Arabidopsis gene encoding a GH95 alpha1,2-fucosidase active on xyloglucan oligo- and polysaccharides. Phytochemistry. 2008;69(10):1983-8. 113. Collin M, Olsen A. EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG. EMBO J. 2001;20(12):3046-55. 114. Wang X, Inoue S, Gu J, Miyoshi E, Noda K, Li W, et al. Dysregulation of TGF-β1 receptor activation leads to abnormal lung development and emphysema-like phenotype in core fucose-deficient mice. Proc Natl Acad Sci USA. 2005;102(44):15791-6. 115. Chen C-Y, Jan Y-H, Juan Y-H, Yang C-J, Huang M-S, Yu C-J, et al. Fucosyltransferase 8 as a functional regulator of nonsmall cell lung cancer. Proc Natl Acad Sci USA. 2013;110(2):630-5. 116. Saldova R, Piccard H, Perez-Garay M, Harvey DJ, Struwe WB, Galligan MC, et al. Increase in Sialylation and Branching in the Mouse Serum N-glycome Correlates with Inflammation and Ovarian Tumour Progression. PLoS ONE. 2013;8(8):e71159. 117. Chen H-S, Tsai Y-F, Lin S, Lin C-C, Khoo K-H, Lin C-H, et al. Studies on the immuno-modulating and anti-tumor activities of Ganoderma lucidum (Reishi) polysaccharides. Biorg Med Chem. 2004;12(21):5595-601. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/58285 | - |
dc.description.abstract | 醣類,脂質,蛋白質為生命組成的三大基本元素.其中,醣類的特性最為複雜.相較於DNA及protein,醣類具有較多的單醣組成,多元的連結可能及複雜的空間構型.此外,醣類還會連結到DNA, protein及脂類,如同本身的被修飾,構成了生物分子的多樣性.而在癌細胞生物學的領域,有幾個重要的醣脂質Gb5, Globo H及SSEA4,已被證明會大量表達在細胞的表面.目前的一些研究報導指出,相較與常見的蛋白質標靶, 這些醣分子更適合開發成為癌症的標靶治療.然而,因為化學合成上的一些限制與困境,導致大量製備上的困難.因此,發展更有效率的合成方法有高度的急迫性.
在本篇論文當中,我集中在兩個部份.一:藉由原位核苷醣再生技術搭配化學酵素法來合成醣分子疫苗Gb5, Globo H, 及SSEA4. 這個方式提供了一個新的方法來大規模合成寡醣,只需三個純化步驟.二:利用新的岩藻醣水解酶來製備無核心岩藻醣的醣蛋白,此外,再搭配其他內切水解酶的情況之下,可用來判斷岩藻醣的位置.之後,利用glycosynthase可以進一步合成無核心岩藻醣的均質化醣蛋白.此舉有助於醣類結構活性的學習. | zh_TW |
dc.description.abstract | Carbohydrate, lipid and protein are basic components of the life. Among these, carbohydrate is significantly complicated than others: more basic units, many possibility of linkages, and complex steric existence. Furthermore, carbohydrate conjugated to DNA, protein and lipid, as well as the modification of carbohydrate itself, also create the biological diversify. Currently, several studies already showed the glycolipid molecules: Gb5, Globo H and SSEA4, are more suitable for target therapy than traditional protein cancer marker. However, due to the difficult and low yield of chemical synthesis, the development of efficient synthetic methodologies for complex glycans preparation has therefore been in high demand.
In this thesis, I focus on two parts. First part is the chemoenzymatic synthesis of carbohydrate vaccine Gb5, Globo H, and SSEA4 by in situ sugar nucleotide regeneration. This method paves a new way to a large scale synthesis of complicated oligosaccharide in just three purification steps, superior to the tedious and laborious traditional chemical methods. The second part is the discovery of new fucosidase for core-fucose eradication and fucose position determination. Subsequently, the core-fucose free glycoprotein can be further utilized for homogeneous glycoprotein preparation by glycosynthase. This way opens a window for gSAR (glycan structure-activity relationship) study. | en |
dc.description.provenance | Made available in DSpace on 2021-06-16T08:10:18Z (GMT). No. of bitstreams: 1 ntu-103-D97642014-1.pdf: 10674812 bytes, checksum: e1af975732d1b0e096181069d122d63f (MD5) Previous issue date: 2014 | en |
dc.description.tableofcontents | INDEX ii
CONTENT OF FIGURES vii CONTENT OF TABLES ix CONTENT OF SCHEMES x ABBRECIATION xi 致謝 xii Abstract 1 論文摘要 2 Chapter I. General Introduction of Glycobiology 3 1.1 Common monosaccharide units of glycoconjugates 3 1.1.1 Pentose, hexose, hexosamine, deoxyhexose, uronic acid, sialic acid 3 1.2 Major classes of glycoconjugates and glycans 4 1.2.1 Glycoprotein 5 1.2.1.1 N-glycoprotein 6 1.2.1.2 O-glycoprotein 7 1.2.1.3 Other glycoprotein 8 1.2.2 Proteoglycan, glycosaminoglycans (GAGs) 11 1.2.3 Glycolipid 12 1.2.4 Lipopolysaccharide (LPS) 14 1.3 Cellular organization of glycosylation 14 1.4 Glycosylation substrate 15 1.4.1 General principle of sugar nucleotide synthesis 15 1.4.2 Classification of glycosyltransferase 17 1.4.2.1 Catalytic mechanism 18 1.5 Glycosidase 20 1.5.1 Inverting glycosidase 20 1.5.2 Retaining glycosidase 20 1.6 Glycosynthase 21 Chapter II. Enzyme in carbohydrate vaccine Globo H synthesis 23 2.1 Introduction 23 2.2 Challenges of carbohydrate synthesis 24 2.2.1 Chemical synthesis of glycans 25 2.2.2 Enzymatic synthesis of glycans 26 2.3 Historical background and overview: sugar nucleotide regeneration 26 2.3.1 UDP-Glc and UDP-Gal regeneration 27 2.3.2 UDP-GlcNAc and UDP-GalNAc regeneration 28 2.3.3 GDP-Man and GDP-Fuc regeneration 29 2.3.4 CMP-Neu5Ac regeneration 30 2.4 Cofactor regeneration system 31 2.5 Enzymatic method for Globo H synthesis 32 2.6 Methodological improvement 33 2.7 Results and discussion 35 2.7.1 Large-scale synthesis of allyl-Gb3 35 2.7.2 Large-scale synthesis of allyl-Gb4 40 2.7.3 Purification of allyl-Gb4 44 2.7.4 Large-scale synthesis of allyl-Gb5 44 2.7.5 Purification of allyl-Gb5 47 2.7.6 Large-scale synthesis of allyl-Globo H 48 2.7.7 Purification of allyl-Globo H 51 2.7.8 Large-scale synthesis of allyl-SSEA4 51 2.7.9 Purification of allyl-SSEA4 54 2.7.10 TLC portfolio of allyl-Globo series of oligosaccharide 54 2.8 Conclusion 55 2.9 Materials and methods 55 2.9.1 Cloning of genes for sugar nucleotide synthesis, glycosyltransferases and ATP regeneration 56 2.9.2 Enzyme assay 56 2.9.2.1 Activity of the galactokinase (GalK), N-acetylhexosamine kinase (NahK), fucokinase (FKP) and cytidine monophosphate kinase (CMK) 57 2.9.2.2 Activity of UDP-sugar pyrophosphorylase (AtUSP), N-acetyl glucosamine-1-phosphate uridyltransferase (GlmU), GDP-L-fucose pyrophosphorylase (FKP) and CMP-sialic acid synthetases (CSS) 57 2.9.2.3 Activity measurement of glycosyltransferase: α-1,4-galactosyltransferase (LgtC), β-1,3-N-acetylgalactosaminyltransferase (β1,3GalNAcT, LgtD), β-1,3-galactosyltransferase (β1,3GalT, LgtD), α-1,2-fucosyltransferase (FutC) and α-2,3-sialyltransferase (JT-FAJ-16) 58 2.9.2.4 Activity measurement of pyruvate kinase (PK) 59 2.9.2.5 Activity measurement of inorganic pyrophosphatase (PPA) 60 2.9.2.6 Measurement of optimum pH 60 2.9.2.7 Measurement of optimum divalent metal ion 61 2.9.2.8 Measurement of optimum temperature 61 2.9.3 Synthesis of allyl-Gb3 61 2.9.4 Synthesis of allyl-Gb4 62 2.9.5 Synthesis of allyl-Gb5 62 2.9.6 Synthesis of allyl-Globo H 62 2.9.7 Synthesis of allyl-SSEA4 63 2.9.8 Purification and Characterization of oligosaccharides 63 Chapter III. Enzyme in carbohydrate hydrolysis and remodeling 65 3.1 Introduction 65 3.2 The roles of glycan in antibody 65 3.3 The drawback of heterogeneous glycoprotein 66 3.4 The drawback of core fucose in IgG and solution 68 3.5 Glycan sequencing 69 3.5.1 Other fucosyl-conjugate 69 3.6 Rationale 71 3.7 Specific aim of study 72 3.8 Results and discussion 73 3.8.1 Screening of bacterial fucosidases for broad substrate specificity and biochemical characterization 73 3.8.2 Screening of bacterial fucosidases for core-fucose remove ability in IgG 77 3.8.3 Characterization of bacterial fucosidases for core-fucose remove ability in other glycoproteins 79 3.8.4 BfFucH activity on N-linked glycan for glycan sequence 81 3.8.5 BfFucH activity for Natural product, Reishi F3 83 3.8.6 Fucosidase activity for LPS of E.coli O128 84 3.8.7 Homogeneous preparation by transglycosylation 85 3.9 Conclusion 86 3.10 Materials and methods 87 3.10.1 Cloning, Expression and Purification of the Recombinant Bacterial fucosidases, endoF1, endoF2, endoF3, endoH, endoS, PNGaseF, L-Fucose dehydrogenase (FDH) in Escherichia coli. 87 3.10.2 BfFucH Activity Analytical Methods 89 3.10.3 Substrate Specificity of BfFucH for pNP- α/β-glycosides 89 3.10.4 Activity Measurement of optimum pH of BfFucH 89 3.10.5 Activity Measurement of optimum divalent metal ion of BfFucH 90 3.10.6 Activity Measurement of optimum temperature of BfFucH 90 3.10.7 Fucose dehydrogenase-based (FDH) assay 90 3.10.8 Generation of mono-GlcNAc or GlcNAc-(Fuc α-1,6) of immunoglobulin G, Fc-fusion protein, EPO, interferon (IFNβ1a) and Influenza Hemagglutinin (HA) 91 3.10.9 SCT (sialoglycan) glycan preparation 91 3.10.10 SCT-oxazoline preparation 92 3.10.11 Generation of homogeneous fucose free IgG by endoS-D233Q 92 References 93 Appendix. HRMS and NMR spectra of allyl-oligosaccharides and data 104 | |
dc.language.iso | en | |
dc.title | 酵素在醣類的合成,水解及重組 | zh_TW |
dc.title | Enzyme in carbohydrate synthesis, hydrolysis and remodeling | en |
dc.type | Thesis | |
dc.date.schoolyear | 102-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 方俊民(Jim-Min Fang),劉啟德(Chi-Te Liu),吳宗益(Chung-Yi Wu),林俊成(Chun-Cheng Lin) | |
dc.subject.keyword | 酵素,醣類合成,醣類水解,醣類重組,醣分子疫苗, | zh_TW |
dc.subject.keyword | Enzyme,carbohydrate synthesis,carbohydrate hydrolysis,carbohydrate remodeling,carbohydrate vaccine, | en |
dc.relation.page | 129 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2014-03-27 | |
dc.contributor.author-college | 生物資源暨農學院 | zh_TW |
dc.contributor.author-dept | 生物科技研究所 | zh_TW |
顯示於系所單位: | 生物科技研究所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-103-1.pdf 目前未授權公開取用 | 10.42 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。