請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/64231完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 林俊宏(Chun-Hung Lin) | |
| dc.contributor.author | Min-Chuan Kao | en |
| dc.contributor.author | 高敏絹 | zh_TW |
| dc.date.accessioned | 2021-06-16T17:35:58Z | - |
| dc.date.available | 2017-08-28 | |
| dc.date.copyright | 2012-08-28 | |
| dc.date.issued | 2012 | |
| dc.date.submitted | 2012-08-15 | |
| dc.identifier.citation | 1 Delves, P. J. The role of glycosylation in autoimmune disease. Autoimmunity 27, 239-253,(1998).
2 Moloney, D. J., Shair, L. H., Lu, F. M., Xia, J., Locke, R., Matta, K. L. & Haltiwanger, R. S. Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules. J Biol Chem 275, 9604-9611,(2000). 3 Haltiwanger, R. S. & Lowe, J. B. Role of glycosylation in development. Annu Rev Biochem 73, 491-537,(2004). 4 Greenwell, P. Blood group antigens: molecules seeking a function? Glycoconj J 14, 159-173,(1997). 5 Ma, B., Simala-Grant, J. L. & Taylor, D. E. Fucosylation in prokaryotes and eukaryotes. Glycobiology 16, 158R-184R,(2006). 6 Alhadeff, J. A., Khunsook, S., Choowongkomon, K., Baney, T., Heredia, V., Tweedie, A. & Bean, B. Characterization of human semen alpha-L-fucosidases. Mol Hum Reprod 5, 809-815,(1999). 7 Hooper, L. V. & Gordon, J. I. Glycans as legislators of host-microbial interactions: spanning the spectrum from symbiosis to pathogenicity. Glycobiology 11, 1R-10R,(2001). 8 Aspholm-Hurtig, M., Dailide, G., Lahmann, M., Kalia, A., Ilver, D., Roche, N., Vikstrom, S., Sjostrom, R., Linden, S., Backstrom, A., Lundberg, C., Arnqvist, A., Mahdavi, J., Nilsson, U. J., Velapatino, B., Gilman, R. H., Gerhard, M., Alarcon, T., Lopez-Brea, M., Nakazawa, T., Fox, J. G., Correa, P., Dominguez-Bello, M. G., Perez-Perez, G. I., Blaser, M. J., Normark, S., Carlstedt, I., Oscarson, S., Teneberg, S., Berg, D. E. & Boren, T. Functional adaptation of BabA, the H. pylori ABO blood group antigen binding adhesin. Science 305, 519-522,(2004). 9 Becker, D. J. & Lowe, J. B. Fucose: biosynthesis and biological function in mammals. Glycobiology 13, 41R-53R,(2003). 10 Becker, D. J. & Lowe, J. B. Leukocyte adhesion deficiency type II. Biochim Biophys Acta 1455, 193-204,(1999). 11 Tarling, C. A., He, S., Sulzenbacher, G., Bignon, C., Bourne, Y., Henrissat, B. & Withers, S. G. Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Thermotoga maritima through trapping of a covalent glycosyl-enzyme intermediate and mutagenesis. J Biol Chem 278, 47394-47399,(2003). 12 Lucas, H., Bercegeay, S., Le Pendu, J., Jean, M., Mirallie, S. & Barriere, P. A fucose-containing epitope potentially involved in gamete interaction on the human zona pellucida. Hum Reprod 9, 1532-1538,(1994). 13 Khunsook, S., Bean, B. S., McGowan, S. R. & Alhadeff, J. A. Purification and characterization of plasma membrane-associated human sperm alpha-L-fucosidase. Biol Reprod 68, 709-716,(2003). 14 Tesarik, J., Mendoza, C., Ramirez, J. P. & Moos, J. Solubilized human zona pellucida competes with a fucosylated neoglycoprotein for binding sites on the human sperm surface. Fertil Steril 60, 344-350,(1993). 15 Cobucci-Ponzano, B., Mazzone, M., Rossi, M. & Moracci, M. Probing the catalytically essential residues of the alpha-L-fucosidase from the hyperthermophilic archaeon Sulfolobus solfataricus. Biochemistry 44, 6331-6342,(2005). 16 Wong-Madden, S. T. & Landry, D. Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas. Glycobiology 5, 19-28,(1995). 17 Focarelli, R., Cacace, M. G., Seraglia, R. & Rosati, F. A nonglycosylated, 68-kDa alpha-L-fucosidase is bound to the mollusc bivalve Unio elongatulus sperm plasma membrane and differs from a glycosylated 56-kDa form present in the seminal fluid. Biochem Biophys Res Commun 234, 54-58,(1997). 18 Berteau, O., McCort, I., Goasdoue, N., Tissot, B. & Daniel, R. Characterization of a new alpha-L-fucosidase isolated from the marine mollusk Pecten maximus that catalyzes the hydrolysis of alpha-L-fucose from algal fucoidan (Ascophyllum nodosum). Glycobiology 12, 273-282,(2002). 19 Johnson, S. W. & Alhadeff, J. A. Mammalian alpha-L-fucosidases. Comp Biochem Physiol B 99, 479-488,(1991). 20 Sano, M., Hayakawa, K. & kato, I. Purification and characterization of alpha-L-fucosidase from Streptomyces species. J Biol Chem 267, 1522-1527,(1992). 21 Butters, T. D., Scudder, P., Rotsaert, J., Petursson, S., Fleet, G. W., Willenbrock, F. W. & Jacob, G. S. Purification to homogeneity of Charonia lampas alpha-fucosidase by using sequential ligand-affinity chromatography. Biochem J 279 ( Pt 1), 189-195,(1991). 22 Chien, S. F. & Dawson, G. Purification and properties of two forms of human alpha-L-fucosidase. Biochim Biophys Acta 614, 476-488,(1980). 23 DiCioccio, R. A., Barlow, J. J. & Matta, K. L. Heat stability and pH activity data of alpha-L-fucosidase in human serum vary with enzyme concentration. Enzyme 30, 122-128,(1983). 24 Thorpe, R. The hydrolysis of L-fucose from some naturally occurring compounds by purified human-liver alpha-L-fucosidase. Carbohydr Res 60, 407-411,(1978). 25 Nagae, M., Tsuchiya, A., Katayama, T., Yamamoto, K., Wakatsuki, S. & Kato, R. Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum. J Biol Chem 282, 18497-18509,(2007). 26 Hidaka, M., Fushinobu, S., Honda, Y., Wakagi, T., Shoun, H. & Kitaoka, M. Structural explanation for the acquisition of glycosynthase activity. J Biochem 147, 237-244,(2010). 27 Henrissat, B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280 ( Pt 2), 309-316,(1991). 28 White, W. J., Jr., Schray, K. J., Legler, G. & Alhadeff, J. A. Further studies on the catalytic mechanism of human liver alpha-L-fucosidase. Biochim Biophys Acta 912, 132-138,(1987). 29 Cobucci-Ponzano, B., Trincone, A., Giordano, A., Rossi, M. & Moracci, M. Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant. Biochemistry 42, 9525-9531,(2003). 30 Eneyskaya, E. V., Kulminskaya, A. A., Kalkkinen, N., Nifantiev, N. E., Arbatskii, N. P., Saenko, A. I., Chepurnaya, O. V., Arutyunyan, A. V., Shabalin, K. A. & Neustroev, K. N. An alpha-L-fucosidase from Thermus sp. with unusually broad specificity. Glycoconj J 18, 827-834,(2001). 31 Intra, J., Perotti, M. E., Pavesi, G. & Horner, D. Comparative and phylogenetic analysis of alpha-L-fucosidase genes. Gene 392, 34-46,(2007). 32 Alhadeff, J. A., Miller, A. L., Wenaas, H., Vedvick, T. & O'Brien, J. S. Human liver alpha-L-fucosidase. Purification, characterization, and immunochemical studies. J Biol Chem 250, 7106-7113,(1975). 33 DiCioccio, R. A., Barlow, J. J. & Matta, K. L. Substrate specificity and other properties of alpha-L-fucosidase from human serum. J Biol Chem 257, 714-718,(1982). 34 Hopfer, R. L., Johnson, S. W., Masserini, M., Giuliani, A. & Alhadeff, J. A. Hydrolysis of fucosyl-GM1 ganglioside by purified pellet-associated human brain and human liver alpha-L-fucosidases without activator proteins or detergents. Biochem J 266, 491-496,(1990). 35 Liu, T. W., Ho, C. W., Huang, H. H., Chang, S. M., Popat, S. D., Wang, Y. T., Wu, M. S., Chen, Y. J. & Lin, C. H. Role for alpha-L-fucosidase in the control of Helicobacter pylori-infected gastric cancer cells. Proc Natl Acad Sci U S A 106, 14581-14586,(2009). 36 Li, Y. K. & Liu, S. W. Expression, Purification and Characterization of Human alpha-L-Fucosidase. J. Chin. Chem. Soc. (Taipei, Taiwan) 56, 850-858,(2009). 37 Scanlin, T. F. & Glick, M. C. Terminal glycosylation and disease: influence on cancer and cystic fibrosis. Glycoconj J 17, 617-626,(2000). 38 Abdel-Aleem, H., Ahmed, A., Sabra, A. M., Zakhari, M., Soliman, M. & Hamed, H. Serum alpha L-fucosidase enzyme activity in ovarian and other female genital tract tumors. Int J Gynaecol Obstet 55, 273-279,(1996). 39 Ayude, D., Fernandez-Rodriguez, J., Rodriguez-Berrocal, F. J., Martinez-Zorzano, V. S., de Carlos, A., Gil, E. & Paez de La Cadena, M. Value of the serum alpha-L-fucosidase activity in the diagnosis of colorectal cancer. Oncology 59, 310-316,(2000). 40 Giardina, M. G., Matarazzo, M., Morante, R., Lucariello, A., Varriale, A., Guardasole, V. & De Marco, G. Serum alpha-L-fucosidase activity and early detection of hepatocellular carcinoma: a prospective study of patients with cirrhosis. Cancer 83, 2468-2474,(1998). 41 Yuan, K., Kucik, D., Singh, R. K., Listinsky, C. M., Listinsky, J. J. & Siegal, G. P. Alterations in human breast cancer adhesion-motility in response to changes in cell surface glycoproteins displaying alpha-L-fucose moieties. Int J Oncol 32, 797-807,(2008). 42 Shah, M., Telang, S., Raval, G., Shah, P. & Patel, P. S. Serum fucosylation changes in oral cancer and oral precancerous conditions: alpha-L-fucosidase as a marker. Cancer 113, 336-346,(2008). 43 Ayude, D., Paez De La Cadena, M., Martinez-Zorzano, V. S., Fernandez-Briera, A. & Rodriguez-Berrocal, F. J. Preoperative serum alpha-L-fucosidase activity as a prognostic marker in colorectal cancer. Oncology 64, 36-45,(2003). 44 Szajda, S. D., Snarska, J., Puchalski, Z. & Zwierz, K. Lysosomal exoglycosidases in serum and urine of patients with colon adenocarcinoma. Hepatogastroenterology 55, 921-925,(2008). 45 Hutchinson, W. L., Johnson, P. J., Du, M. Q. & Williams, R. Serum and tissue alpha-L-fucosidase activity in the pre-clinical and clinical stages of hepatocellular carcinoma. Clin Sci (Lond) 81, 177-182,(1991). 46 Pancewicz, S., Popko, J., Rutkowski, R., Knas, M., Grygorczuk, S., Guszczyn, T., Bruczko, M., Szajda, S., Zajkowska, J., Kondrusik, M., Sierakowski, S. & Zwierz, K. Activity of lysosomal exoglycosidases in serum and synovial fluid in patients with chronic Lyme and rheumatoid arthritis. Scand J Infect Dis 41, 584-589,(2009). 47 Merino-Trigo, A., Rodriguez-Berrocal, F. J., de Miguel, E. & Paez de la Cadena, M. Activity and properties of alpha-L-fucosidase are dependent on the state of enterocytic differentiation of HT-29 colon cancer cells. Int J Biochem Cell Biol 34, 1291-1303,(2002). 48 Dariusz Szajda, S., Waszkiewicz, N., Stypulkowska, A., Dadan, J. & Zwierz, K. Lysosomal exoglycosidases in serum and urine of patients with pancreatic adenocarcinoma. Folia Histochem Cytobiol 48, 351-357,(2010). 49 Attia, M. S., Othman, A. M., Aboaly, M. M. & Abdel-Mottaleb, M. S. Novel spectrofluorimetric method for measuring the activity of the enzyme alpha-L-fucosidase using the nano composite optical sensor samarium(III)-doxycycline complex doped in sol-gel matrix. Anal Chem 82, 6230-6236,(2010). 50 Willems, P. J., Seo, H. C., Coucke, P., Tonlorenzi, R. & O'Brien, J. S. Spectrum of mutations in fucosidosis. Eur J Hum Genet 7, 60-67,(1999). 51 Barker, C., Dell, A., Rogers, M., Alhadeff, J. A. & Winchester, B. Canine alpha-L-fucosidase in relation to the enzymic defect and storage products in canine fucosidosis. Biochem J 254, 861-868,(1988). 52 Ip, P., Goh, W., Chan, K. W. & Cheung, P. T. A novel FUCA1 mutation causing fucosidosis in a Chinese boy. J Inherit Metab Dis 25, 415-416,(2002). 53 Michalski, J. C., Wieruszeski, J. M., Alonso, C., Cache, P., Montreuil, J. & Strecker, G. Characterization and 400-MHz 1H-NMR analysis of urinary fucosyl glycoasparagines in fucosidosis. Eur J Biochem 201, 439-458,(1991). 54 Noronkoski, T. & Mononen, I. Influence of L-fucose attached alpha 1-->6 to the asparagine-linked N-acetylglucosamine on the hydrolysis of the N-glycosidic linkage by human glycosylasparaginase. Glycobiology 7, 217-220,(1997). 55 de Carlos, A., Montenegro, D., Alonso-Rodriguez, A., Paez de la Cadena, M., Rodriguez-Berrocal, F. J. & Martinez-Zorzano, V. S. Purification of human alpha-L-fucosidase precursor expressed in Escherichia coli as a glutathione S-transferase fusion protein. J Chromatogr B Analyt Technol Biomed Life Sci 786, 7-15,(2003). 56 Liu, S. W., Chen, C. S., Chang, S. S., Mong, K. K., Lin, C. H., Chang, C. W., Tang, C. Y. & Li, Y. K. Identification of essential residues of human alpha-L-fucosidase and tests of its mechanism. Biochemistry 48, 110-120,(2009). 57 Mungall, A. J., Palmer, S. A., Sims, S. K., Edwards, C. A., Ashurst, J. L., Wilming, L., Jones, M. C., Horton, R., Hunt, S. E., Scott, C. E., Gilbert, J. G., Clamp, M. E., Bethel, G., Milne, S., Ainscough, R., Almeida, J. P., Ambrose, K. D., Andrews, T. D., Ashwell, R. I., Babbage, A. K., Bagguley, C. L., Bailey, J., Banerjee, R., Barker, D. J., Barlow, K. F., Bates, K., Beare, D. M., Beasley, H., Beasley, O., Bird, C. P., Blakey, S., Bray-Allen, S., Brook, J., Brown, A. J., Brown, J. Y., Burford, D. C., Burrill, W., Burton, J., Carder, C., Carter, N. P., Chapman, J. C., Clark, S. Y., Clark, G., Clee, C. M., Clegg, S., Cobley, V., Collier, R. E., Collins, J. E., Colman, L. K., Corby, N. R., Coville, G. J., Culley, K. M., Dhami, P., Davies, J., Dunn, M., Earthrowl, M. E., Ellington, A. E., Evans, K. A., Faulkner, L., Francis, M. D., Frankish, A., Frankland, J., French, L., Garner, P., Garnett, J., Ghori, M. J., Gilby, L. M., Gillson, C. J., Glithero, R. J., Grafham, D. V., Grant, M., Gribble, S., Griffiths, C., Griffiths, M., Hall, R., Halls, K. S., Hammond, S., Harley, J. L., Hart, E. A., Heath, P. D., Heathcott, R., Holmes, S. J., Howden, P. J., Howe, K. L., Howell, G. R., Huckle, E., Humphray, S. J., Humphries, M. D., Hunt, A. R., Johnson, C. M., Joy, A. A., Kay, M., Keenan, S. J., Kimberley, A. M., King, A., Laird, G. K., Langford, C., Lawlor, S., Leongamornlert, D. A., Leversha, M., Lloyd, C. R., Lloyd, D. M., Loveland, J. E., Lovell, J., Martin, S., Mashreghi-Mohammadi, M., Maslen, G. L., Matthews, L., McCann, O. T., McLaren, S. J., McLay, K., McMurray, A., Moore, M. J., Mullikin, J. C., Niblett, D., Nickerson, T., Novik, K. L., Oliver, K., Overton-Larty, E. K., Parker, A., Patel, R., Pearce, A. V., Peck, A. I., Phillimore, B., Phillips, S., Plumb, R. W., Porter, K. M., Ramsey, Y., Ranby, S. A., Rice, C. M., Ross, M. T., Searle, S. M., Sehra, H. K., Sheridan, E., Skuce, C. D., Smith, S., Smith, M., Spraggon, L., Squares, S. L., Steward, C. A., Sycamore, N., Tamlyn-Hall, G., Tester, J., Theaker, A. J., Thomas, D. W., Thorpe, A., Tracey, A., Tromans, A., Tubby, B., Wall, M., Wallis, J. M., West, A. P., White, S. S., Whitehead, S. L., Whittaker, H., Wild, A., Willey, D. J., Wilmer, T. E., Wood, J. M., Wray, P. W., Wyatt, J. C., Young, L., Younger, R. M., Bentley, D. R., Coulson, A., Durbin, R., Hubbard, T., Sulston, J. E., Dunham, I., Rogers, J. & Beck, S. The DNA sequence and analysis of human chromosome 6. Nature 425, 805-811,(2003). 58 Venter, J. C., Adams, M. D., Myers, E. W., Li, P. W., Mural, R. J., Sutton, G. G., Smith, H. O., Yandell, M., Evans, C. A., Holt, R. A., Gocayne, J. D., Amanatides, P., Ballew, R. M., Huson, D. H., Wortman, J. R., Zhang, Q., Kodira, C. D., Zheng, X. H., Chen, L., Skupski, M., Subramanian, G., Thomas, P. D., Zhang, J., Gabor Miklos, G. L., Nelson, C., Broder, S., Clark, A. G., Nadeau, J., McKusick, V. A., Zinder, N., Levine, A. J., Roberts, R. J., Simon, M., Slayman, C., Hunkapiller, M., Bolanos, R., Delcher, A., Dew, I., Fasulo, D., Flanigan, M., Florea, L., Halpern, A., Hannenhalli, S., Kravitz, S., Levy, S., Mobarry, C., Reinert, K., Remington, K., Abu-Threideh, J., Beasley, E., Biddick, K., Bonazzi, V., Brandon, R., Cargill, M., Chandramouliswaran, I., Charlab, R., Chaturvedi, K., Deng, Z., Di Francesco, V., Dunn, P., Eilbeck, K., Evangelista, C., Gabrielian, A. E., Gan, W., Ge, W., Gong, F., Gu, Z., Guan, P., Heiman, T. J., Higgins, M. E., Ji, R. R., Ke, Z., Ketchum, K. A., Lai, Z., Lei, Y., Li, Z., Li, J., Liang, Y., Lin, X., Lu, F., Merkulov, G. V., Milshina, N., Moore, H. M., Naik, A. K., Narayan, V. A., Neelam, B., Nusskern, D., Rusch, D. B., Salzberg, S., Shao, W., Shue, B., Sun, J., Wang, Z., Wang, A., Wang, X., Wang, J., Wei, M., Wides, R., Xiao, C., Yan, C., Yao, A., Ye, J., Zhan, M., Zhang, W., Zhang, H., Zhao, Q., Zheng, L., Zhong, F., Zhong, W., Zhu, S., Zhao, S., Gilbert, D., Baumhueter, S., Spier, G., Carter, C., Cravchik, A., Woodage, T., Ali, F., An, H., Awe, A., Baldwin, D., Baden, H., Barnstead, M., Barrow, I., Beeson, K., Busam, D., Carver, A., Center, A., Cheng, M. L., Curry, L., Danaher, S., Davenport, L., Desilets, R., Dietz, S., Dodson, K., Doup, L., Ferriera, S., Garg, N., Gluecksmann, A., Hart, B., Haynes, J., Haynes, C., Heiner, C., Hladun, S., Hostin, D., Houck, J., Howland, T., Ibegwam, C., Johnson, J., Kalush, F., Kline, L., Koduru, S., Love, A., Mann, F., May, D., McCawley, S., McIntosh, T., McMullen, I., Moy, M., Moy, L., Murphy, B., Nelson, K., Pfannkoch, C., Pratts, E., Puri, V., Qureshi, H., Reardon, M., Rodriguez, R., Rogers, Y. H., Romblad, D., Ruhfel, B., Scott, R., Sitter, C., Smallwood, M., Stewart, E., Strong, R., Suh, E., Thomas, R., Tint, N. N., Tse, S., Vech, C., Wang, G., Wetter, J., Williams, S., Williams, M., Windsor, S., Winn-Deen, E., Wolfe, K., Zaveri, J., Zaveri, K., Abril, J. F., Guigo, R., Campbell, M. J., Sjolander, K. V., Karlak, B., Kejariwal, A., Mi, H., Lazareva, B., Hatton, T., Narechania, A., Diemer, K., Muruganujan, A., Guo, N., Sato, S., Bafna, V., Istrail, S., Lippert, R., Schwartz, R., Walenz, B., Yooseph, S., Allen, D., Basu, A., Baxendale, J., Blick, L., Caminha, M., Carnes-Stine, J., Caulk, P., Chiang, Y. H., Coyne, M., Dahlke, C., Mays, A., Dombroski, M., Donnelly, M., Ely, D., Esparham, S., Fosler, C., Gire, H., Glanowski, S., Glasser, K., Glodek, A., Gorokhov, M., Graham, K., Gropman, B., Harris, M., Heil, J., Henderson, S., Hoover, J., Jennings, D., Jordan, C., Jordan, J., Kasha, J., Kagan, L., Kraft, C., Levitsky, A., Lewis, M., Liu, X., Lopez, J., Ma, D., Majoros, W., McDaniel, J., Murphy, S., Newman, M., Nguyen, T., Nguyen, N., Nodell, M., Pan, S., Peck, J., Peterson, M., Rowe, W., Sanders, R., Scott, J., Simpson, M., Smith, T., Sprague, A., Stockwell, T., Turner, R., Venter, E., Wang, M., Wen, M., Wu, D., Wu, M., Xia, A., Zandieh, A. & Zhu, X. The sequence of the human genome. Science 291, 1304-1351,(2001). 59 Alhadeff, J. A. & Janowsky, A. J. Human serum alpha-L-fucosidase. Clin Chim Acta 82, 133-140,(1978). 60 Beem, E. P., Lisman, J. J. W., Vansteijn, G. J., Vanderwal, C. J., Trippelvitz, L. A. W., Overdijk, B., Vanhalbeek, H., Mutsaers, J. H. G. M. & Vliegenthart, J. F. G. Structural-Analysis of the Carbohydrate Moieties of Alpha-L-Fucosidase from Human-Liver. Glycoconjugate J 4, 33-42,(1987). 61 Alhadeff, J. A. & Freeze, H. Carbohydrate composition of purified human liver alpha-L-fucosidase. Mol Cell Biochem 18, 33-37,(1977). 62 Argade, S. P., Hopfer, R. L., Strang, A. M., van Halbeek, H. & Alhadeff, J. A. Structural studies on the carbohydrate moieties of human liver alpha-L-fucosidase. Arch Biochem Biophys 266, 227-247,(1988). 63 Fisher, K. J. & Aronson, N. N., Jr. Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase. Biochem J 264, 695-701,(1989). 64 Piesecki, S. & Alhadeff, J. A. The effect of carbohydrate removal on the properties of human liver alpha-L-fucosidase. Biochim Biophys Acta 1119, 194-200,(1992). 65 Lloyd, K. O. Philip Levine award lecture. Blood group antigens as markers for normal differentiation and malignant change in human tissues. Am J Clin Pathol 87, 129-139,(1987). 66 Sakamoto, S., Watanabe, T., Tokumaru, T., Takagi, H., Nakazato, H. & Lloyd, K. O. Expression of Lewisa, Lewisb, Lewisx, Lewisy, siayl-Lewisa, and sialyl-Lewisx blood group antigens in human gastric carcinoma and in normal gastric tissue. Cancer Res 49, 745-752,(1989). 67 Saadi, A. T., Blackwell, C. C., Raza, M. W., James, V. S., Stewart, J., Elton, R. A. & Weir, D. M. Factors enhancing adherence of toxigenic Staphylococcus aureus to epithelial cells and their possible role in sudden infant death syndrome. Epidemiol Infect 110, 507-517,(1993). 68 Heneghan, M. A., Moran, A. P., Feeley, K. M., Egan, E. L., Goulding, J., Connolly, C. E. & McCarthy, C. F. Effect of host Lewis and ABO blood group antigen expression on Helicobacter pylori colonisation density and the consequent inflammatory response. FEMS Immunol Med Microbiol 20, 257-266,(1998). 69 Norman, K. E., Anderson, G. P., Kolb, H. C., Ley, K. & Ernst, B. Sialyl Lewis(x) (sLe(x)) and an sLe(x) mimetic, CGP69669A, disrupt E-selectin-dependent leukocyte rolling in vivo. Blood 91, 475-483,(1998). 70 Zhang, B. H., Chen, H., Yao, X. P., Cong, W. M. & Wu, M. C. E-selectin and its ligand-sLeX in the metastasis of hepatocellular carcinoma. Hepatobiliary Pancreat Dis Int 1, 80-82,(2002). 71 Linden, S., Boren, T., Dubois, A. & Carlstedt, I. Rhesus monkey gastric mucins: oligomeric structure, glycoforms and Helicobacter pylori binding. Biochem J 379, 765-775,(2004). 72 Boren, T., Falk, P., Roth, K. A., Larson, G. & Normark, S. Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens. Science 262, 1892-1895,(1993). 73 Mahdavi, J., Sonden, B., Hurtig, M., Olfat, F. O., Forsberg, L., Roche, N., Angstrom, J., Larsson, T., Teneberg, S., Karlsson, K. A., Altraja, S., Wadstrom, T., Kersulyte, D., Berg, D. E., Dubois, A., Petersson, C., Magnusson, K. E., Norberg, T., Lindh, F., Lundskog, B. B., Arnqvist, A., Hammarstrom, L. & Boren, T. Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation. Science 297, 573-578,(2002). 74 Sell, S. Cancer-associated carbohydrates identified by monoclonal antibodies. Hum. Pathol. 21, 1003-1019,(1990). 75 Taylor-Papadimitriou, J. & Epenetos, A. A. Exploiting altered glycosylation patterns in cancer: progress and challenges in diagnosis and therapy. Trends. Biotechnol. 12, 227-233,(1994). 76 Michie, S. A., Streeter, P. R., Bolt, P. A., Butcher, E. C. & Picker, L. J. The human peripheral lymph node vascular addressin. An inducible endothelial antigen involved in lymphocyte homing. Am. J. Pathol. 143, 1688-1698,(1993). 77 Salmi, M., Granfors, K., MacDermott, R. & Jalkanen, S. Aberrant binding of lamina propria lymphocytes to vascular endothelium in inflammatory bowel diseases. Gastroenterology 106, 596-605,(1994). 78 Hanninen, A., Taylor, C., Streeter, P. R., Stark, L. S., Sarte, J. M., Shizuru, J. A., Simell, O. & Michie, S. A. Vascular addressins are induced on islet vessels during insulitis in nonobese diabetic mice and are involved in lymphoid cell binding to islet endothelium. J. Clin. Invest. 92, 2509-2515,(1993). 79 Dube, D. H. & Bertozzi, C. R. Glycans in cancer and inflammation--potential for therapeutics and diagnostics. Nat. Rev. Drug. Discov. 4, 477-488,(2005). 80 Monteiro, M. A., Zheng, P., Ho, B., Yokota, S., Amano, K., Pan, Z., Berg, D. E., Chan, K. H., MacLean, L. L. & Perry, M. B. Expression of histo-blood group antigens by lipopolysaccharides of Helicobacter pylori strains from asian hosts: the propensity to express type 1 blood-group antigens. Glycobiology 10, 701-713,(2000). 81 Monteiro, M. A., Chan, K. H., Rasko, D. A., Taylor, D. E., Zheng, P. Y., Appelmelk, B. J., Wirth, H. P., Yang, M., Blaser, M. J., Hynes, S. O., Moran, A. P. & Perry, M. B. Simultaneous expression of type 1 and type 2 Lewis blood group antigens by Helicobacter pylori lipopolysaccharides. Molecular mimicry between h. pylori lipopolysaccharides and human gastric epithelial cell surface glycoforms. J Biol Chem 273, 11533-11543,(1998). 82 Rasko, D. A., Wilson, T. J., Zopf, D. & Taylor, D. E. Lewis antigen expression and stability in Helicobacter pylori isolated from serial gastric biopsies. J Infect Dis 181, 1089-1095,(2000). 83 Zheng, P. Y., Hua, J., Yeoh, K. G. & Ho, B. Association of peptic ulcer with increased expression of Lewis antigens but not cagA, iceA, and vacA in Helicobacter pylori isolates in an Asian population. Gut 47, 18-22,(2000). 84 Weis, W. I., Taylor, M. E. & Drickamer, K. The C-type lectin superfamily in the immune system. Immunol Rev 163, 19-34,(1998). 85 Heneghan, M. A., McCarthy, C. F. & Moran, A. P. Relationship of blood group determinants on Helicobacter pylori lipopolysaccharide with host lewis phenotype and inflammatory response. Infect Immun 68, 937-941,(2000). 86 Martin, S. L., McColm, A. A. & Appelmelk, B. J. H. pylori adhesion and Lewis X. Gastroenterology 119, 1414-1416,(2000). 87 Edwards, N. J., Monteiro, M. A., Faller, G., Walsh, E. J., Moran, A. P., Roberts, I. S. & High, N. J. Lewis X structures in the O antigen side-chain promote adhesion of Helicobacter pylori to the gastric epithelium. Mol Microbiol 35, 1530-1539,(2000). 88 Guruge, J. L., Falk, P. G., Lorenz, R. G., Dans, M., Wirth, H. P., Blaser, M. J., Berg, D. E. & Gordon, J. I. Epithelial attachment alters the outcome of Helicobacter pylori infection. Proc Natl Acad Sci U S A 95, 3925-3930,(1998). 89 Covacci, A. & Rappuoli, R. Tyrosine-phosphorylated bacterial proteins: Trojan horses for the host cell. J Exp Med 191, 587-592,(2000). 90 Wirth, H. P., Yang, M., Karita, M. & Blaser, M. J. Expression of the human cell surface glycoconjugates Lewis x and Lewis y by Helicobacter pylori isolates is related to cagA status. Infect Immun 64, 4598-4605,(1996). 91 Chang, C. F., Ho, C. W., Wu, C. Y., Chao, T. A., Wong, C. H. & Lin, C. H. Discovery of picomolar slow tight-binding inhibitors of alpha-fucosidase. Chem Biol 11, 1301-1306,(2004). 92 Bethell, G. S., Ayers, J. S., Hancock, W. S. & Hearn, M. T. A novel method of activation of cross-linked agaroses with 1,1'-carbonyldiimidazole which gives a matrix for affinity chromatography devoid of additional charged groups. J Biol Chem 254, 2572-2574,(1979). 93 Hase, S., Ikenaka, T. & Matsushima, Y. Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fluorescent compound. Biochem Biophys Res Commun 85, 257-263,(1978). 94 Hase, S., Natsuka, S., Oku, H. & Ikenaka, T. Identification method for twelve oligomannose-type sugar chains thought to be processing intermediates of glycoproteins. Anal Biochem 167, 321-326,(1987). 95 Hase, S., Ikenaka, T. & Matsushima, Y. A highly sensitive method for analyses of sugar moieties of glycoproteins by fluorescence labeling. J Biochem 90, 407-414,(1981). 96 Hase, S. Pyridylamination as a means of analyzing complex sugar chains. Proc Jpn Acad Ser B Phys Biol Sci 86, 378-390,(2010). 97 Ishimizu, T., Sasaki, A., Okutani, S., Maeda, M., Yamagishi, M. & Hase, S. Endo-beta-mannosidase, a plant enzyme acting on N-glycan: purification, molecular cloning, and characterization. J Biol Chem 279, 38555-38562,(2004). 98 Jensen, P. H., Karlsson, N. G., Kolarich, D. & Packer, N. H. Structural analysis of N- and O-glycans released from glycoproteins. Nat Protoc 7, 1299-1310,(2012). 99 Wang, S. H., Wu, S. W. & Khoo, K. H. MS-based glycomic strategies for probing the structural details of polylactosaminoglycan chain on N-glycans and glycoproteomic identification of its protein carriers. Proteomics 11, 2812-2829,(2011). 100 Ceroni, A., Maass, K., Geyer, H., Geyer, R., Dell, A. & Haslam, S. M. GlycoWorkbench: a tool for the computer-assisted annotation of mass spectra of glycans. J Proteome Res 7, 1650-1659,(2008). 101 Shih, Y. P., Kung, W. M., Chen, J. C., Yeh, C. H., Wang, A. H. & Wang, T. F. High-throughput screening of soluble recombinant proteins. Protein Sci 11, 1714-1719,(2002). 102 Van Hoof, F. & Hers, H. G. Mucopolysaccharidosis by absence of alpha-fucosidase. Lancet 1, 1198,(1968). 103 Pierce, R. J. & Price, R. G. The separation and characterization of marmoset kidney beta-D-galactosidase and beta-D-glucosidase. Biochem J 167, 765-773,(1977). 104 Pearce, R. D., Callahan, J. W., Little, P. B., Armstrong, D. T., Kiehm, D. & Clarke, J. T. Properties and prenatal ontogeny of beta-D-mannosidase in selected goat tissues. Biochem J 243, 603-609,(1987). 105 Dawson, G. & Tsay, G. Substrate specificity of human alpha-L-fucosidase. Arch Biochem Biophys 184, 12-23,(1977). 106 Kodar, K., Stadlmann, J., Klaamas, K., Sergeyev, B. & Kurtenkov, O. Immunoglobulin G Fc N-glycan profiling in patients with gastric cancer by LC-ESI-MS: relation to tumor progression and survival. Glycoconj J 29, 57-66,(2012). 107 Mizushima, T., Yagi, H., Takemoto, E., Shibata-Koyama, M., Isoda, Y., Iida, S., Masuda, K., Satoh, M. & Kato, K. Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans. Genes Cells 16, 1071-1080,(2011). 108 Krapp, S., Mimura, Y., Jefferis, R., Huber, R. & Sondermann, P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J Mol Biol 325, 979-989,(2003). 109 Marasco, W. A. & Sui, J. The growth and potential of human antiviral monoclonal antibody therapeutics. Nat Biotechnol 25, 1421-1434,(2007). 110 Conzelmann, E., Burg, J., Stephan, G. & Sandhoff, K. Complexing of glycolipids and their transfer between membranes by the activator protein for degradation of lysosomal ganglioside GM2. Eur J Biochem 123, 455-464,(1982). 111 Tappel, A. Lysosomal enzymes and initiation of breast cancer. Med Hypotheses 64, 288-289,(2005). 112 Tappel, A. Lysosomal and prostasomal hydrolytic enzymes and redox processes and initiation of prostate cancer. Med Hypotheses 64, 1170-1172,(2005). 113 Moriwaki, K., Noda, K., Furukawa, Y., Ohshima, K., Uchiyama, A., Nakagawa, T., Taniguchi, N., Daigo, Y., Nakamura, Y., Hayashi, N. & Miyoshi, E. Deficiency of GMDS leads to escape from NK cell-mediated tumor surveillance through modulation of TRAIL signaling. Gastroenterology 137, 188-198, 198 e181-182,(2009). 114 Moriwaki, K. & Miyoshi, E. Fucosylation and gastrointestinal cancer. World J Hepatol 2, 151-161,(2010). 115 Brooks, P. C. Cell adhesion molecules in angiogenesis. Cancer Metastasis Rev 15, 187-194,(1996). | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/64231 | - |
| dc.description.abstract | 岩藻醣水解酶 (α-L-Fucosidase) 是負責水解非還原端上各種含有岩藻糖修飾的醣類分子並釋放出L-fucose。人類有兩種岩藻醣水解酶 (EC 3.2.1.51) ，分別為第一型岩藻醣水解酶 (簡稱FucA1) 和第二型岩藻醣水解酶 (簡稱FucA2) 。諸多疾病會有岩藻醣水解酶活性異常的現象，先前本實驗室的研究發現，當人類癌症細胞受到胃幽門螺旋桿菌感染時，會促使FucA2分泌至細胞外。而FucA2在感染過程中所扮演的角色與生化性質目前仍不清楚。
為了瞭解FucA2的生理意義，探討其生化特性是很重要的一部份。本研究首次在大腸桿菌建構具有融合蛋白的FucA2質體，並成功表現出有活性且大量的FucA2，檢測其pH值對活性之影響、酵素動力學常數、受質專一性等性質，並與FucA1作比較。這二個酵素的pH 值活性分布有異，FucA1最佳活性落在pH 4.5 及pH 6.5而FucA2則落在pH 6.0。接著用含螢光的寡醣鏈與細胞萃取之醣鏈檢測受質專一性，發現FucA1可水解 Fuc α-1,2 Gal β-1,4、core Fuc α-1,6 bi/triantennary、Lea、Lex受質上的岩藻醣，而且FucA1對於細胞上萃取之後的醣鏈上之core Fucose有非常好的水解活性，FucA2則水解Fuc α-1,2 Gal β-1,4、core Fuc biantennary、Lex受質上的岩藻醣。 另外諸多研究報告癌症病人的血漿中含有高度的岩藻醣水解酶活性，為探究此生理現象的活性來源，本研究自萬芳醫院取得癌症病人的血漿進行分析，並利用實驗室合成的抑制劑層析管柱純化出岩藻醣水解酶，再以中研院單多株抗體生產中心所生產的專一性抗體來作確認。經實驗證實肝癌病人血漿中高度的岩藻醣水解酶活性來自於FucA1，而且發現其上具有轉譯後修飾作用，以凝集素微陣列分析發現該修飾為含有Fuc之N-glycosylation，而正常人血漿中岩藻醣水解酶則屬於FucA2，其修飾則偏向O-glycosylation。顯示FucA1有潛力作為腫瘤指標，而單多株抗體生產中心所製備的anti-FucA1 IgG則可應用於臨床研究並作為診斷工具。 | zh_TW |
| dc.description.abstract | There are two α-L-fucosidases (EC 3.2.1.51) in human, including α-L-fucosidase1 (FucA1) and α-L-fucosidase2 (FucA2). They are responsible for the removal of L-fucose residues from the non-reducing end of glycoconjugates. Abnormal fucosidase activity has been associated with many diseases, such as hepatocellular cancer and breast cancer. Previous study indicated that the infection of Helicobacter pylori triggers the release of FucA2 by gastric cancer cells. However, the role and physiological function of FucA2 still remain ambiguous. One of the prerequisites for further studies is to prepare FucA2 in a sufficient amount and to carry out their characterizations.
Previous preparation of FucA2 in our labotoary was restricted by the poor expression and extremely low activity. Herein we succesfully express recombinant FucA2 in E. coli.by incorporating 6x His, MBP and TEV protease recognition site to N-terminus of FucA2. Significant expression and activity were obtained after removal of the MBP-fusion tag with TEV protease, allowing the biochemical characterizations such as pH profile, kinetic parameters and substrate specificity. The results indicated that FucA2 is optimally active at pH 6.0, unlike FucA1 which has dual optimum at pH 4.5 and pH 6.5. To examine the substrate specificity, the glycoproteins extracted from human colon cancer cells line (Colo 205) and seven pyridylamino-conjugated sugars were used for the study. These glycoconjugates were subjected to the hydrolytic cleavage of either FucA1 or FucA2, followed by mass spectrometric and HPLC analyse, respectively the results indicate that FucA1 preferentially hydrolyzes L-fucose from Fuc α-1,2 Gal β-1,4, core Fuc α-1,6 bi/triantennary, Lea, Lex, while FUCA2 catalyzes the hydrolysis of Fuc α-1,2 Gal β-1,4, and Lex. Furthermore, both recombinant FucA1 and FucA2 were examined by the antibodies that were generated by immunization of the specific peptides correspounding to residues 404-444 of FucA1 and residues 404-445 of FucA2 (represent the major sequence differance). In conjunction with our developed inhibitor-based affinity column chromatography, the antibodies were used to examine and identify the serum fucosidase from the patients with liver and gastric cancers. The result indicated that high activity of FucA1 was found in the serum of liver cancer patients, while that of FucA2 in the serum of normal people. Further examination (such as the glycol-structure analysis) would be beneficial to use FucA1 as a biomarker. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-16T17:35:58Z (GMT). No. of bitstreams: 1 ntu-101-R99b46008-1.pdf: 8353940 bytes, checksum: a175750c5ed042861159f5e20ba1ebe2 (MD5) Previous issue date: 2012 | en |
| dc.description.tableofcontents | 誌謝 I
常用縮寫及中英對照表 II 中文摘要 IV ABSTRACT V 目錄 VII 圖目錄 XI 表目錄 XIII CHAPTER 1 緒論 1 1-1 岩藻醣水解酶概述 1 1-2 人類岩藻醣水解酶之功能與相關疾病 4 1-2-1 人類第一型岩藻醣水解酶 4 1-2-2 人類第二型岩藻醣水解酶 5 1-2-3 人類岩藻醣水解酶之醣基化現象 6 1-3 路易士抗原之角色 7 1-3-1 人類細胞表現之路易士抗原 7 1-3-2 幽門螺旋桿菌表現之路易士抗原 8 1-4 人類岩藻醣水解酶的之偵測 9 1-4-1 人類岩藻醣水解酶的活性偵測 9 1-4-2 人類岩藻醣水解酶受質專一性之偵測 10 1-5 論文研究動機 12 CHAPTER 2 結果 14 2-1 人類第二型岩藻醣水解酶重組蛋白之建構與生化特性 14 2-1-1 質體建構 14 2-1-2 質體轉殖後小量表現 15 2-1-3 MBP_FucA2大量表現與純化 16 2-1-4 rFucA2基本生化性質檢測 17 2-2 檢測人類岩藻醣水解酶的受質專一性 17 2-2-1 以各式PA-sugar當作受質 18 2-2-2 以細胞萃取之醣鏈當作受質 21 2-3 抗人類岩藻醣水解酶抗體的開發 34 2-3-1 抗FucA1抗體與抗FucA 2抗體之抗原決定區選取 34 2-3-2 抗FucA1抗體與抗FucA 2抗體之製備與純化 36 2-3-3 檢測抗FucA1抗體與抗FucA 2抗體之專一性及效價 36 2-4 鑑定血漿樣本內之人類岩藻醣水解酶 41 2-4-1 測定血漿樣本內岩藻醣水解酶含量 42 2-4-2 西方點墨轉漬法偵測以抑制性親和性管柱所純化出的岩藻醣水解酶 43 2-4-3 凝集素微陣列分析岩藻醣水解酶上之醣鏈修飾 46 CHAPTER 3 討論 50 3-1 人類第二型岩藻醣水解酶重組蛋白之建構與純化之比較 50 3-2 比較人類第一型及第二型岩藻醣水解酶之基本生化性質 52 3-2-1 人類第一型及第二型岩藻醣水解酶pH值活性分布異同比較 52 3-2-2 利用PA-sugar探討人類岩藻醣水解酶受質專一性 53 3-2-3 利用model protein探討人類岩藻醣水解酶受質專一性 54 3-2-4 利用whole cell glycan探討人類岩藻醣水解酶受質專一性 55 3-3 比較自製抗體與市售抗體之敏感性及特異性 56 3-4 血漿樣本內岩藻醣水解酶之生理意義探討 58 3-4-1探討血漿樣本內之岩藻醣水解酶種類 58 3-4-2探討血漿樣本內之岩藻醣水解酶之醣化現象 59 CHAPTER 4 結論 61 CHAPTER 5 材料與方法 62 5-1 人類第二型岩藻醣水解酶重組蛋白之基因轉殖 (Gene cloning) 62 5-1-1 人類第二型岩藻醣水解酶基因之取得 62 5-1-2 引子設計 (Primer design) 62 5-1-3 聚合酶鏈鎖反應 (Polymerase Chain Reaction，PCR) 63 5-1-4 黏合反應(Ligation) 64 5-1-5 轉殖作用(Transformation) 65 5-1-6 質體DNA之抽取 65 5-2人類第二型岩藻醣水解酶重組蛋白之表現與純化 66 5-2-1 重組蛋白之大量表現 66 5-2-2 重組蛋白之純化 66 5-3基因密碼子改造後的人類岩藻醣水解酶重組蛋白之表現與純化 67 5-4 岩藻醣水解酶重組蛋白之活性測定 68 5-5 岩藻醣水解酶之酵素動力分析 68 5-6 高效能液相層析法分析及氨基吡啶醣 69 5-7 凝集素微陣列分析 69 5-8 人類第一型岩藻醣水解酶重組蛋白之表現與純化 70 5-9 抗岩藻醣水解酶抗體之純化 70 5-10 利用蛋白質變性劑萃取細胞的醣蛋白 71 5-10-1 去除脂質 71 5-10-2 醣蛋白萃取 71 5-10-3 N-linked glycan釋出與純化 71 5-10-4 O-linked glycan釋出與純化 72 5-10-5 以質譜儀分析glycan的樣本前處理(Permethylation) 73 5-11銀染法 73 參考文獻 75 | |
| dc.language.iso | zh-TW | |
| dc.title | 人類岩藻醣水解酶之生化性質探討 | zh_TW |
| dc.title | Characterization of Human α-L-Fucosidase:
Large-scale preparation, substrate specificity | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 100-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 邱繼輝(Kay-Hooi Khoo),李耀坤(Yaw-Kuen Li),吳明賢(Ming-Shiang Wu) | |
| dc.subject.keyword | 岩藻醣水解酶,受質專一性,肝癌,腫瘤指標, | zh_TW |
| dc.subject.keyword | α-L-fucosidases,substrate specificity,liver cancer,biomarker, | en |
| dc.relation.page | 86 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2012-08-15 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科學研究所 | zh_TW |
| 顯示於系所單位： | 生化科學研究所 | |
文件中的檔案：
| 檔案 | 大小 | 格式 | |
|---|---|---|---|
| ntu-101-1.pdf 目前未授權公開取用 | 8.16 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。