請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/64607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 | Yu-Chen Wei | en |
| dc.contributor.author | 魏妤真 | zh_TW |
| dc.date.accessioned | 2021-06-16T17:57:43Z | - |
| dc.date.available | 2017-08-28 | |
| dc.date.copyright | 2012-08-28 | |
| dc.date.issued | 2012 | |
| dc.date.submitted | 2012-08-10 | |
| dc.identifier.citation | Aoyagi, Y., Isemura, M., Suzuki, Y., Sekine, C., Soga, K., Ozaki, T., and Ichida, F. (1985). Fucosylated alpha-fetoprotein as marker of early hepatocellular carcinoma. Lancet 2, 1353-1354.
Aoyagi, Y., Isemura, M., Suzuki, Y., Sekine, C., Soga, K., Ozaki, T., and Ichida, F. (1986). Change in fucosylation of alpha-fetoprotein on malignant transformation of liver cells. Lancet 1, 210. Aspholm-Hurtig, M., Dailide, G., Lahmann, M., Kalia, A., Ilver, D., Roche, N., Vikstrom, S., Sjostrom, R., Linden, S., Backstrom, A., et al. (2004). Functional adaptation of BabA, the H. pylori ABO blood group antigen binding adhesin. Science 305, 519-522. Berg, E.L., Robinson, M.K., Mansson, O., Butcher, E.C., and Magnani, J.L. (1991). A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1. J Biol Chem 266, 14869-14872. Borzym-Kluczyk, M., Radziejewska, I., Olszewska, E., Szajda, S., Knas, M., and Zwierz, K. (2007). Statistical evaluation of the isoform patterns of N-acetyl-beta-hexosaminidase from human renal cancer tissue separated by isoelectrofocusing. Clin Biochem 40, 403-406. Dariusz Szajda, S., Waszkiewicz, N., Stypulkowska, A., Dadan, J., and Zwierz, K. (2010). Lysosomal exoglycosidases in serum and urine of patients with pancreatic adenocarcinoma. Folia Histochem Cytobiol 48, 351-357. De Bolos, C., Garrido, M., and Real, F.X. (1995). MUC6 apomucin shows a distinct normal tissue distribution that correlates with Lewis antigen expression in the human stomach. Gastroenterology 109, 723-734. Drumm, B., Perez-Perez, G.I., Blaser, M.J., and Sherman, P.M. (1990). Intrafamilial clustering of Helicobacter pylori infection. N Engl J Med 322, 359-363. Edwards, N.J., Monteiro, M.A., Faller, G., Walsh, E.J., Moran, A.P., Roberts, I.S., and High, N.J. (2000). Lewis X structures in the O antigen side-chain promote adhesion of Helicobacter pylori to the gastric epithelium. Mol Microbiol 35, 1530-1539. Fukushima, H., de Wet, J.R., and O'Brien, J.S. (1985). Molecular cloning of a cDNA for human alpha-L-fucosidase. Proc Natl Acad Sci U S A 82, 1262-1265. Hakomori, S. (1989). Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens. Adv Cancer Res 52, 257-331. Jain, R.K., Koenig, G.C., Dellian, M., Fukumura, D., Munn, L.L., and Melder, R.J. (1996). Leukocyte-endothelial adhesion and angiogenesis in tumors. Cancer Metastasis Rev 15, 195-204. Johnson, S.W., Piesecki, S., Wang, R.F., Damjanov, I., and Alhadeff, J.A. (1992). Analysis of purified human liver alpha-L-fucosidase by western-blotting with lectins and polyclonal and monoclonal antibodies. Biochem J 282, 829-834. Koda, Y., Soejima, M., and Kimura, H. (1997). Structure and expression of H-type GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase gene (FUT1). Two transcription start sites and alternative splicing generate several forms of FUT1 mRNA. J Biol Chem 272, 7501-7505. Kunishio, K., Okada, M., Matsumoto, Y., and Nagao, S. (2003). Matrix metalloproteinase-2 and -9 expression in astrocytic tumors. Brain Tumor Pathol 20, 39-45. Lau, K.S., Partridge, E.A., Grigorian, A., Silvescu, C.I., Reinhold, V.N., Demetriou, M., and Dennis, J.W. (2007). Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129, 123-134. Liu, T.W., Ho, C.W., Huang, H.H., Chang, S.M., Popat, S.D., Wang, Y.T., Wu, M.S., Chen, Y.J., and Lin, C.H. (2009). 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. Mahdavi, J., Sonden, B., Hurtig, M., Olfat, F.O., Forsberg, L., Roche, N., Angstrom, J., Larsson, T., Teneberg, S., Karlsson, K.A., et al. (2002). Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation. Science 297, 573-578. Murata, K., Egami, H., Shibata, Y., Sakamoto, K., Misumi, A., and Ogawa, M. (1992). Expression of blood group-related antigens, ABH, Lewis(a), Lewis(b), Lewis(x), Lewis(y), CA19-9, and CSLEX1 in early cancer, intestinal metaplasia, and uninvolved mucosa of the stomach. Am J Clin Pathol 98, 67-75. Nadimpalli, S.K., Padmanabhan, N., and Koduru, S. (2004). Biochemical and immunological characterization of a glycosylated alpha-fucosidase from the invertebrate Unio: interaction of the enzyme with its in vivo binding partners. Protein Expression Purif 37, 279-287. Nakajima, S., Krishnan, B., Ota, H., Segura, A.M., Hattori, T., Graham, D.Y., and Genta, R.M. (1997). Mast cell involvement in gastritis with or without Helicobacter pylori infection. Gastroenterology 113, 746-754. Okoli, C., Fornara, A., Qin, J., Toprak, M.S., Dalhammar, G., Muhammed, M., and Rajarao, G.K. (2011). Characterization of superparamagnetic iron oxide nanoparticles and its application in protein purification. Journal of nanoscience and nanotechnology 11, 10201-10206. Partridge, E.A., Le Roy, C., Di Guglielmo, G.M., Pawling, J., Cheung, P., Granovsky, M., Nabi, I.R., Wrana, J.L., and Dennis, J.W. (2004). Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Science 306, 120-124. Shomer, N.H., Dangler, C.A., Whary, M.T., and Fox, J.G. (1998). Experimental Helicobacter pylori infection induces antral gastritis and gastric mucosa-associated lymphoid tissue in guinea pigs. Infect Immun 66, 2614-2618. Skrzydlewska, E., Sulkowska, M., Koda, M., and Sulkowski, S. (2005). Proteolytic-antiproteolytic balance and its regulation in carcinogenesis. World J Gastroenterol 11, 1251-1266. Szajda, S.D., Borzym-Kluczyk, M., Snarska, J., Puchalski, Z., and Zwierz, K. (2009). N-acetyl-beta-D-hexosaminidase and its isoenzymes A and B in blood serum and urine, as a potential colon cancer markers. Hepatogastroenterology 56, 1287-1298. Szymendera, J.J. (1986). Clinical usefulness of three monoclonal antibody-defined tumor markers: CA 19-9, CA 50, and CA 125. Tumour Biol 7, 333-342. Takada, A., Ohmori, K., Yoneda, T., Tsuyuoka, K., Hasegawa, A., Kiso, M., and Kannagi, R. (1993). Contribution of carbohydrate antigens sialyl Lewis A and sialyl Lewis X to adhesion of human cancer cells to vascular endothelium. Cancer Res 53, 354-361. Tappel, A. (2005). Lysosomal enzymes and initiation of breast cancer. Med Hypotheses 64, 288-289. Thomsson, K.A., Hinojosa-Kurtzberg, M., Axelsson, K.A., Domino, S.E., Lowe, J.B., Gendler, S.J., and Hansson, G.C. (2002). Intestinal mucins from cystic fibrosis mice show increased fucosylation due to an induced Fucalpha1-2 glycosyltransferase. Biochem J 367, 609-616. Visa, M., Hammer, E., Volker, U., Koliwer-Brandl, H., Kelm, S., and Nadimpalli, S.K. (2012). Purification and biochemical characterization of a lysosomal alpha-fucosidase from the deuterostomia Asterias rubens. Biochimie 94, 1199-1205. Wang, X., Gu, J., Ihara, H., Miyoshi, E., Honke, K., and Taniguchi, N. (2006). Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling. J Biol Chem 281, 2572-2577. Zhao, Y., Itoh, S., Wang, X., Isaji, T., Miyoshi, E., Kariya, Y., Miyazaki, K., Kawasaki, N., Taniguchi, N., and Gu, J. (2006). Deletion of core fucosylation on alpha3beta1 integrin down-regulates its functions. J Biol Chem 281, 38343-38350. Zwierz, P., Szajda, S.D., Snarska, J., Supronowicz, Z.B., Zawadzki, P., Zwierz, K., and Kaminsk, F. (2006). Concentration of thyroid stimulating hormone and activity of N-acetyl-beta-D-hexosaminidase and its isoenzymes, in serum of patients with thyroid cancer. Polski merkuriusz lekarski 21, 439-442. Abdel-Aleem, H., Ahmed, A., Sabra, A.M., Zakhari, M., Soliman, M., and Hamed, H. (1996). Serum alpha L-fucosidase enzyme activity in ovarian and other female genital tract tumors. Int J Gynaecol Obstet 55, 273-279. Alam, T., and Balasubramanian, A.S. (1979). Affinity chromatography and separation of the molecular forms of monkey brain alpha-L-fucosidase on fucose-linked sepharose. Biochim Biophys Acta 566, 327-334. Ayude, D., Fernandez-Rodriguez, J., Rodriguez-Berrocal, F.J., Martinez-Zorzano, V.S., de Carlos, A., Gil, E., and Paez de La Cadena, M. (2000). Value of the serum alpha-L-fucosidase activity in the diagnosis of colorectal cancer. Oncology 59, 310-316. Ayude, D., Paez De La Cadena, M., Martinez-Zorzano, V.S., Fernandez-Briera, A., and Rodriguez-Berrocal, F.J. (2003). Preoperative serum alpha-L-fucosidase activity as a prognostic marker in colorectal cancer. Oncology 64, 36-45. Azarkan, M., Huet, J., Baeyens-Volant, D., Looze, Y., and Vandenbussche, G. (2007). Affinity chromatography: a useful tool in proteomics studies. J chromatography B 849, 81-90. Bach, S., Knockaert, M., Reinhardt, J., Lozach, O., Schmitt, S., Baratte, B., Koken, M., Coburn, S.P., Tang, L., Jiang, T., et al. (2005). Roscovitine targets, protein kinases and pyridoxal kinase. J Biol Chem 280, 31208-31219. Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S., Boesche, M., Hobson, S., Mathieson, T., Perrin, J., Raida, M., Rau, C., et al. (2007). Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat Biotechnol 25, 1035-1044. Beydoun, D., Amal, R., Low, G., and McEvoy, S. (2002). Occurrence and prevention of photodissolution at the phase junction of magnetite and titanium dioxide. J Mol Catal A: Chem 180, 193-200. Bukofzer, S., Stass, P.M., Kew, M.C., de Beer, M., and Groeneveld, H.T. (1989). Alpha-L-fucosidase as a serum marker of hepatocellular carcinoma in southern African blacks. Br J Cancer 59, 417-420. Chang, C.F., Ho, C.W., Wu, C.Y., Chao, T.A., Wong, C.H., and Lin, C.H. (2004). Discovery of picomolar slow tight-binding inhibitors of alpha-fucosidase. Chem Biol 11, 1301-1306. Cuatrecasas, P., Wilchek, M., and Anfinsen, C.B. (1968). Selective enzyme purification by affinity chromatography. Proc Natl Acad Sci U S A 61, 636-643. de Koning, H.W., Chamuleau, R.A., and Bantjes, A. (1984). Crosslinked agarose encapsulated sorbents resistant to steam sterilization. Preparation and mechanical properties. J Biomed Mater Res 18, 1-13. Deugnier, Y., David, V., Brissot, P., Mabo, P., Delamaire, D., Messner, M., Bourel, M., and Legall, J.Y. (1984). Serum alpha-L-fucosidase: a new marker for the diagnosis of primary hepatic carcinoma? Hepatology 4, 889-892. DiCioccio, R.A., Barlow, J.J., and Matta, K.L. (1982). Substrate specificity and other properties of alpha-L-fucosidase from human serum. J Biol Chem 257, 714-718. Elshemey, W.M., Desouky, O.S., Mohammed, M.S., Elsayed, A.A., and el-Houseini, M.E. (2003). Characterization of cirrhosis and hepatocellular carcinoma using low-angle x-ray scattering signatures of serum. Phys Med Biol 48, N239-246. Fernandez, J., Rodriguez-Berrocal, F.J., de Carlos, A., de Castro, G., and de la Cadena, M.P. (1996). Nonradioactive immunoquantification of alpha-L-fucosidase protein in human colon tissues. J Biochem Biophys Methods 31, 39-47. Giardina, M.G., Matarazzo, M., Morante, R., Lucariello, A., Varriale, A., Guardasole, V., and De Marco, G. (1998). Serum alpha-L-fucosidase activity and early detection of hepatocellular carcinoma: a prospective study of patients with cirrhosis. Cancer 83, 2468-2474. Giardina, M.G., Matarazzo, M., Varriale, A., Morante, R., Napoli, A., and Martino, R. (1992). Serum alpha-L-fucosidase. A useful marker in the diagnosis of hepatocellular carcinoma. Cancer 70, 1044-1048. Godl, K., Wissing, J., Kurtenbach, A., Habenberger, P., Blencke, S., Gutbrod, H., Salassidis, K., Stein-Gerlach, M., Missio, A., Cotten, M., et al. (2003). An efficient proteomics method to identify the cellular targets of protein kinase inhibitors. Proc Natl Acad Sci U S A 100, 15434-15439. Hage, D.S., Anguizola, J.A., Bi, C., Li, R., Matsuda, R., Papastavros, E., Pfaunmiller, E., Vargas, J., and Zheng, X. (2012). Pharmaceutical and biomedical applications of affinity chromatography: Recent trends and developments. J Pharm Biomed Anal. Ho, C.W., Lin, Y.N., Chang, C.F., Li, S.T., Wu, Y.T., Wu, C.Y., Liu, S.W., Li, Y.K., and Lin, C.H. (2006). Discovery of different types of inhibition between the human and thermotoga maritima alpha-fucosidases by fuconojirimycin-based derivatives. Biochemistry 45, 5695-5702. Ho, K.C., Tsai, P.J., Lin, Y.S., and Chen, Y.C. (2004). Using biofunctionalized nanoparticles to probe pathogenic bacteria. Anal Chem 76, 7162-7168. Intra, J., Perotti, M.E., Pavesi, G., and Horner, D. (2007). Comparative and phylogenetic analysis of alpha-L-fucosidase genes. Gene 392, 34-46. Ip, P., Goh, W., Chan, K.W., and Cheung, P.T. (2002). A novel FUCA1 mutation causing fucosidosis in a Chinese boy. J Inherited Metab Dis 25, 415-416. Jain, R.S., Binder, R.L., Levy-Benshimol, A., Buck, C.A., and Warren, L. (1977). Purification of alpha-L-fucosidase from various sources by affinity chromatography. J Chromatogr 139, 283-290. Johnson, S.W., and Alhadeff, J.A. (1991). Mammalian alpha-L-fucosidases. Comp Biochem Physiol B 99, 479-488. Khunsook, S., Alhadeff, J.A., and Bean, B.S. (2002). Purification and characterization of human seminal plasma alpha-L-fucosidase. Mol Human Reprod 8, 221-227. Khunsook, S., Bean, B.S., McGowan, S.R., and Alhadeff, J.A. (2003). Purification and characterization of plasma membrane-associated human sperm alpha-L-fucosidase. Biol Reprod 68, 709-716. Kim, J.S., Yoon, T.J., Yu, K.N., Kim, B.G., Park, S.J., Kim, H.W., Lee, K.H., Park, S.B., Lee, J.K., and Cho, M.H. (2006). Toxicity and tissue distribution of magnetic nanoparticles in mice. Toxicol Sci 89, 338-347. Kuester, M., Becker, G.L., Hardes, K., Lindberg, I., Steinmetzer, T., and Than, M.E. (2011). Purification of the proprotein convertase furin by affinity chromatography based on PC-specific inhibitors. Biol Chem 392, 973-981. Lammerts van Bueren, A., Ardevol, A., Fayers-Kerr, J., Luo, B., Zhang, Y., Sollogoub, M., Bleriot, Y., Rovira, C., and Davies, G.J. (2010). Analysis of the reaction coordinate of alpha-L-fucosidases: a combined structural and quantum mechanical approach. J Am Chem Soc 132, 1804-1806. Laurent, S., Forge, D., Port, M., Roch, A., Robic, C., Vander Elst, L., and Muller, R.N. (2008). Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem Rev 108, 2064-2110. Leray, G., Deugnier, Y., Jouanolle, A.M., Lehry, D., Bretagne, J.F., Campion, J.P., Brissot, P., and Le Treut, A. (1989). Biochemical aspects of alpha-L-fucosidase in hepatocellular carcinoma. Hepatology 9, 249-252. Li, C., Qian, J., and Lin, J.S. (2006). Purification and characterization of alpha-L-fucosidase from human primary hepatocarcinoma tissue. World J Gastroenterol 12, 3770-3775. Listinsky, J.J., Listinsky, C.M., Alapati, V., and Siegal, G.P. (2001). Cell surface fucose ablation as a therapeutic strategy for malignant neoplasms. Adv Anat Pathol 8, 330-337. Liu, Q., Xu, Z., Finch, J.A., and Egerton, R. (1998). A Novel Two-Step Silica-Coating Process for Engineering Magnetic Nanocomposites. Chem Mater 10, 3936-3940. Liu, S.W., Chen, C.S., Chang, S.S., Mong, K.K., Lin, C.H., Chang, C.W., Tang, C.Y., and Li, Y.K. (2009a). Identification of essential residues of human alpha-L-fucosidase and tests of its mechanism. Biochemistry 48, 110-120. Liu, T.W., Ho, C.W., Huang, H.H., Chang, S.M., Popat, S.D., Wang, Y.T., Wu, M.S., Chen, Y.J., and Lin, C.H. (2009b). 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. Liu, X., Ma, Z., Xing, J., and Liu, H. (2004). Preparation and characterization of amino–silane modified superparamagnetic silica nanospheres. J Magn Magn Mater 270, 1-6. Llovet, J.M., Burroughs, A., and Bruix, J. (2003). Hepatocellular carcinoma. The Lancet 362, 1907-1917. Ma, J., Gong, Q., Lin, M., Xi, Y., Wang, M., Chen, Z., Pei, Z., and Ma, W. (2000). Combined five tumor markers in detecting primary hepatic carcinoma. Chinese journal of surgery 38, 14-16. Malaguarnera, G., Giordano, M., Paladina, I., Berretta, M., Cappellani, A., and Malaguarnera, M. (2010). Serum markers of hepatocellular carcinoma. Dig Dis Sci 55, 2744-2755. Medvedev, A., Kopylov, A., Buneeva, O., Zgoda, V., and Archakov, A. (2012). Affinity-based proteomic profiling: problems and achievements. Proteomics 12, 621-637. Moriwaki, K., and Miyoshi, E. (2010). Fucosylation and gastrointestinal cancer. World J Hepatol 2, 151-161. Nagae, M., Tsuchiya, A., Katayama, T., Yamamoto, K., Wakatsuki, S., and Kato, R. (2007). Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum. J Biol Chem 282, 18497-18509. Nakatsura, T., Yoshitake, Y., Senju, S., Monji, M., Komori, H., Motomura, Y., Hosaka, S., Beppu, T., Ishiko, T., Kamohara, H., et al. (2003). Glypican-3, overexpressed specifically in human hepatocellular carcinoma, is a novel tumor marker. Biochem Biophys Res Commun 306, 16-25. Pinto, B.M., and Bundle, D.R. (1983). Preparation of glycoconjugates for use as artificial antigens: a simplified procedure. Carbohydr Res 124, 313-318. Rix, U., Hantschel, O., Durnberger, G., Remsing Rix, L.L., Planyavsky, M., Fernbach, N.V., Kaupe, I., Bennett, K.L., Valent, P., Colinge, J., et al. (2007). Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets. Blood 110, 4055-4063. Rosano, C., Zuccotti, S., Cobucci-Ponzano, B., Mazzone, M., Rossi, M., Moracci, M., Petoukhov, M.V., Svergun, D.I., and Bolognesi, M. (2004). Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchrotron small angle X-ray scattering. Biochem Biophys Res Commun 320, 176-182. Seandel, M., Butler, J., Lyden, D., and Rafii, S. (2008). A catalytic role for proangiogenic marrow-derived cells in tumor neovascularization. Cancer Cell 13, 181-183. Seo, H.C., Willems, P.J., Kretz, K.A., Martin, B.M., and O'Brien, J.S. (1993). Fucosidosis: four new mutations and a new polymorphism. Hum Mol Genet 2, 423-429. Shah, M., Telang, S., Raval, G., Shah, P., and Patel, P.S. (2008). Serum fucosylation changes in oral cancer and oral precancerous conditions: alpha-L-fucosidase as a marker. Cancer 113, 336-346. Shi, M., Zhang, C.Q., Zhang, Y.Q., Liang, X.M., and Li, J.Q. (2004). Micrometastases of solitary hepatocellular carcinoma and appropriate resection margin. World J Surg 28, 376-381. Sulzenbacher, G., Bignon, C., Nishimura, T., Tarling, C.A., Withers, S.G., Henrissat, B., and Bourne, Y. (2004). Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis. J Biol Chem 279, 13119-13128. Svensson, S.C., and Thiem, J. (1990). Purification of alpha-L-fucosidase by C-glycosylic affinity chromatography, and the enzymic synthesis of alpha-L-fucosyl disaccharides. Carbohydr Res 200, 391-402. Turney, K., Drake, T.J., Smith, J.E., Tan, W., and Harrison, W.W. (2004). Functionalized nanoparticles for liquid atmospheric pressure matrix-assisted laser desorption/ionization peptide analysis. Rapid Commun Mass Spectrom 18, 2367-2374. Valsasina, B., Kalisz, H.M., and Isacchi, A. (2004). Kinase selectivity profiling by inhibitor affinity chromatography. Expert review of proteomics 1, 303-315. Willems, P.J., Seo, H.C., Coucke, P., Tonlorenzi, R., and O'Brien, J.S. (1999). Spectrum of mutations in fucosidosis. Eur J Hum Genet 7, 60-67. Wu, C.Y., Chang, C.F., Chen, J.S., Wong, C.H., and Lin, C.H. (2003). Rapid diversity-oriented synthesis in microtiter plates for in situ screening: discovery of potent and selective alpha-fucosidase inhibitors. Angew Chem Int Ed 42, 4661-4664. Wu, H.J., Ho, C.W., Ko, T.P., Popat, S.D., Lin, C.H., and Wang, A.H. (2010). Structural basis of alpha-fucosidase inhibition by iminocyclitols with K(i) values in the micro- to picomolar range. Angew Chem Int Ed 49, 337-340. Yao, D.F., Dong, Z.Z., and Yao, M. (2007). Specific molecular markers in hepatocellular carcinoma. Hepato Pancr Dis Int 6, 241-247. Yoshima, H., Takasaki, S., Ito-Mega, S., and Kobata, A. (1979). Purification of almond emulsin alpha-L-fucosidase I by affinity chromatography. Arch Biochem Biophys 194, 394-398. Yuan, K., Kucik, D., Singh, R.K., Listinsky, C.M., Listinsky, J.J., and Siegal, G.P. (2008). 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. Ho, C.W., Lin, Y.N., Chang, C.F., Li, S.T., Wu, Y.T., Wu, C.Y., Liu, S.W., Li, Y.K., and Lin, C.H. (2006). Discovery of different types of inhibition between the human and thermotoga maritima alpha-fucosidases by fuconojirimycin-based derivatives. Biochemistry 45, 5695-5702. Kita, Y., Miura, Y., Furukawa, J., Nakano, M., Shinohara, Y., Ohno, M., Takimoto, A., and Nishimura, S. (2007). Quantitative glycomics of human whole serum glycoproteins based on the standardized protocol for liberating N-glycans. Mol Cell Proteomics 6, 1437-1445. Liu, T.W., Ho, C.W., Huang, H.H., Chang, S.M., Popat, S.D., Wang, Y.T., Wu, M.S., Chen, Y.J., and Lin, C.H. (2009). 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. Abdel-Aleem, H., Ahmed, A., Sabra, A.M., Zakhari, M., Soliman, M., and Hamed, H. (1996). Serum alpha L-fucosidase enzyme activity in ovarian and other female genital tract tumors. Int J Gynaecol Obstet 55, 273-279. Alam, T., and Balasubramanian, A.S. (1979). Affinity chromatography and separation of the molecular forms of monkey brain alpha-L-fucosidase on fucose-linked sepharose. Biochim Biophys Acta 566, 327-334. Ayude, D., Fernandez-Rodriguez, J., Rodriguez-Berrocal, F.J., Martinez-Zorzano, V.S., de Carlos, A., Gil, E., and Paez de La Cadena, M. (2000). Value of the serum alpha-L-fucosidase activity in the diagnosis of colorectal cancer. Oncology 59, 310-316. Ayude, D., Paez De La Cadena, M., Martinez-Zorzano, V.S., Fernandez-Briera, A., and Rodriguez-Berrocal, F.J. (2003). Preoperative serum alpha-L-fucosidase activity as a prognostic marker in colorectal cancer. Oncology 64, 36-45. Azarkan, M., Huet, J., Baeyens-Volant, D., Looze, Y., and Vandenbussche, G. (2007). Affinity chromatography: a useful tool in proteomics studies. J Chromatography B 849, 81-90. Bach, S., Knockaert, M., Reinhardt, J., Lozach, O., Schmitt, S., Baratte, B., Koken, M., Coburn, S.P., Tang, L., Jiang, T., et al. (2005). Roscovitine targets, protein kinases and pyridoxal kinase. J Biol Chem 280, 31208-31219. Balog, C.I., Stavenhagen, K., Fung, W.L., Koeleman, C.A., McDonnell, L.M., Verhoeven, A., Mesker, W.E., Tollenaar, R.A., Deelder, A.M., and Wuhrer, M. (2012). N-glycosylation of colorectal cancer tissues: a liquid chromatography and mass spectrometry-based investigation. Mol Cell Proteomics Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S., Boesche, M., Hobson, S., Mathieson, T., Perrin, J., Raida, M., Rau, C., et al. (2007). Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat Biotechnol 25, 1035-1044. Bethell, G.S., Ayers, J.S., Hancock, W.S., and Hearn, M.T. (1979). 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. Beydoun, D., Amal, R., Low, G., and McEvoy, S. (2002). Occurrence and prevention of photodissolution at the phase junction of magnetite and titanium dioxide. J Mol Catal A 180, 193-200. Brehmer, D., Godl, K., Zech, B., Wissing, J., and Daub, H. (2004). Proteome-wide identification of cellular targets affected by bisindolylmaleimide-type protein kinase C inhibitors. Mol Cell Proteomics 3, 490-500. Bukofzer, S., Stass, P.M., Kew, M.C., de Beer, M., and Groeneveld, H.T. (1989). Alpha-L-fucosidase as a serum marker of hepatocellular carcinoma in southern African blacks. Br J Cancer 59, 417-420. Chang, C.F., Ho, C.W., Wu, C.Y., Chao, T.A., Wong, C.H., and Lin, C.H. (2004). Discovery of picomolar slow tight-binding inhibitors of alpha-fucosidase. Chem Biol 11, 1301-1306. Chou, P.H., Chen, S.H., Liao, H.K., Lin, P.C., Her, G.R., Lai, A.C., Chen, J.H., Lin, C.C., and Chen, Y.J. (2005). Nanoprobe-based affinity mass spectrometry for selected protein profiling in human plasma. Anal Chem 77, 5990-5997. Cuatrecasas, P., Wilchek, M., and Anfinsen, C.B. (1968). Selective enzyme purification by affinity chromatography. Proc Natl Acad Sci U S A 61, 636-643. de Koning, H.W., Chamuleau, R.A., and Bantjes, A. (1984). Crosslinked agarose encapsulated sorbents resistant to steam sterilization. Preparation and mechanical properties. J Biomed Mater Res 18, 1-13. Deugnier, Y., David, V., Brissot, P., Mabo, P., Delamaire, D., Messner, M., Bourel, M., and Legall, J.Y. (1984). Serum alpha-L-fucosidase: a new marker for the diagnosis of primary hepatic carcinoma? Hepatology 4, 889-892. DiCioccio, R.A., Barlow, J.J., and Matta, K.L. (1982). Substrate specificity and other properties of alpha-L-fucosidase from human serum. J Biol Chem 257, 714-718. Elshemey, W.M., Desouky, O.S., Mohammed, M.S., Elsayed, A.A., and el-Houseini, M.E. (2003). Characterization of cirrhosis and hepatocellular carcinoma using low-angle x-ray scattering signatures of serum. Phys Med Biol 48, N239-246. Fernandez, J., Rodriguez-Berrocal, F.J., de Carlos, A., de Castro, G., and de la Cadena, M.P. (1996). Nonradioactive immunoquantification of alpha-L-fucosidase protein in human colon tissues. J Biochem Biophys Methods 31, 39-47. Giardina, M.G., Matarazzo, M., Morante, R., Lucariello, A., Varriale, A., Guardasole, V., and De Marco, G. (1998). Serum alpha-L-fucosidase activity and early detection of hepatocellular carcinoma: a prospective study of patients with cirrhosis. Cancer 83, 2468-2474. Giardina, M.G., Matarazzo, M., Varriale, A., Morante, R., Napoli, A., and Martino, R. (1992). Serum alpha-L-fucosidase. A useful marker in the diagnosis of hepatocellular carcinoma. Cancer 70, 1044-1048. Godl, K., Wissing, J., Kurtenbach, A., Habenberger, P., Blencke, S., Gutbrod, H., Salassidis, K., Stein-Gerlach, M., Missio, A., Cotten, M., et al. (2003). An efficient proteomics method to identify the cellular targets of protein kinase inhibitors. Proc Natl Acad Sci U S A 100, 15434-15439. Hage, D.S., Anguizola, J.A., Bi, C., Li, R., Matsuda, R., Papastavros, E., Pfaunmiller, E., Vargas, J., and Zheng, X. (2012). Pharmaceutical and biomedical applications of affinity chromatography: Recent trends and developments. J Pharm Biomed Anal. Hirschhorn, R., Huie, M.L., and Kasper, J.S. (2002). Computer assisted cloning of human neutral alpha-glucosidase C (GANC): a new paralog in the glycosyl hydrolase gene family 31. Proc Natl Acad Sci U S A 99, 13642-13646. Ho, C.W., Lin, Y.N., Chang, C.F., Li, S.T., Wu, Y.T., Wu, C.Y., Liu, S.W., Li, Y.K., and Lin, C.H. (2006). Discovery of different types of inhibition between the human and thermotoga maritima alpha-fucosidases by fuconojirimycin-based derivatives. Biochemistry 45, 5695-5702. Ho, K.C., Tsai, P.J., Lin, Y.S., and Chen, Y.C. (2004). Using biofunctionalized nanoparticles to probe pathogenic bacteria. Anal Chem 76, 7162-7168. Intra, J., Perotti, M.E., Pavesi, G., and Horner, D. (2007). Comparative and phylogenetic analysis of alpha-L-fucosidase genes. Gene 392, 34-46. Ip, P., Goh, W., Chan, K.W., and Cheung, P.T. (2002). A novel FUCA1 mutation causing fucosidosis in a Chinese boy. J Inherited Metab Dis 25, 415-416. Jain, R.S., Binder, R.L., Levy-Benshimol, A., Buck, C.A., and Warren, L. (1977). Purification of alpha-L-fucosidase from various sources by affinity chromatography. J Chromatogr 139, 283-290. Johnson, S.W., and Alhadeff, J.A. (1991). Mammalian alpha-L-fucosidases. Comp Biochem Physiol B 99, 479-488. Johnson, S.W., Piesecki, S., Wang, R.F., Damjanov, I., and Alhadeff, J.A. (1992). Analysis of purified human liver alpha-L-fucosidase by western-blotting with lectins and polyclonal and monoclonal antibodies. Biochem J 282, 829-834. Keefe, A.D., Wilson, D.S., Seelig, B., and Szostak, J.W. (2001). One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag. Protein Expression Purif 23, 440-446. Khunsook, S., Alhadeff, J.A., and Bean, B.S. (2002). Purification and characterization of human seminal plasma alpha-L-fucosidase. Mol Human Reprod 8, 221-227. Khunsook, S., Bean, B.S., McGowan, S.R., and Alhadeff, J.A. (2003). Purification and characterization of plasma membrane-associated human sperm alpha-L-fucosidase. Biol Reprod 68, 709-716. Kim, J.S., Yoon, T.J., Yu, K.N., Kim, B.G., Park, S.J., Kim, H.W., Lee, K.H., Park, S.B., Lee, J.K., and Cho, M.H. (2006). Toxicity and tissue distribution of magnetic nanoparticles in mice. Toxicol Sci 89, 338-347. Kita, Y., Miura, Y., Furukawa, J., Nakano, M., Shinohara, Y., Ohno, M., Takimoto, A., and Nishimura, S. (2007). Quantitative glycomics of human whole serum glycoproteins based on the standardized protocol for liberating N-glycans. Mol Cell Proteomics 6, 1437-1445. Knockaert, M., Gray, N., Damiens, E., Chang, Y.T., Grellier, P., Grant, K., Fergusson, D., Mottram, J., Soete, M., Dubremetz, J.F., et al. (2000). Intracellular targets of cyclin-dependent kinase inhibitors: identification by affinity chromatography using immobilised inhibitors. Chem Biol 7, 411-422. Kuester, M., Becker, G.L., Hardes, K., Lindberg, I., Steinmetzer, T., and Than, M.E. (2011). Purification of the proprotein convertase furin by affinity chromatography based on PC-specific inhibitors. Biol Chem 392, 973-981. Lammerts van Bueren, A., Ardevol, A., Fayers-Kerr, J., Luo, B., Zhang, Y., Sollogoub, M., Bleriot, Y., Rovira, C., and Davies, G.J. (2010a). Analysis of the reaction coordinate of alpha-L-fucosidases: a combined structural and quantum mechanical approach. J Am Chem Soc 132, 1804-1806. Lammerts van Bueren, A., Popat, S.D., Lin, C.H., and Davies, G.J. (2010b). Structural and thermodynamic analyses of alpha-L-fucosidase inhibitors. ChemBioChem 11, 1971-1974. Laurent, S., Forge, D., Port, M., Roch, A., Robic, C., Vander Elst, L., and Muller, R.N. (2008). Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem Rev 108, 2064-2110. Leray, G., Deugnier, Y., Jouanolle, A.M., Lehry, D., Bretagne, J.F., Campion, J.P., Brissot, P., and Le Treut, A. (1989). Biochemical aspects of alpha-L-fucosidase in hepatocellular carcinoma. Hepatology 9, 249-252. Li, C., Qian, J., and Lin, J.S. (2006). Purification and characterization of alpha-L-fucosidase from human primary hepatocarcinoma tissue. World J Gastroenterol 12, 3770-3775. Listinsky, J.J., Listinsky, C.M., Alapati, V., and Siegal, G.P. (2001). Cell surface fucose ablation as a therapeutic strategy for malignant neoplasms. Adv Anat Pathol 8, 330-337. Liu, Q., Xu, Z., Finch, J.A., and Egerton, R. (1998). A Novel Two-Step Silica-Coating Process for Engineering Magnetic Nanocomposites. Chem Mater 10, 3936-3940. Liu, S.W., Chen, C.S., Chang, S.S., Mong, K.K., Lin, C.H., Chang, C.W., Tang, C.Y., and Li, Y.K. (2009a). Identification of essential residues of human alpha-L-fucosidase and tests of its mechanism. Biochemistry 48, 110-120. Liu, T.W., Ho, C.W., Huang, H.H., Chang, S.M., Popat, S.D., Wang, Y.T., Wu, M.S., Chen, Y.J., and Lin, C.H. (2009b). 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. Liu, X., Ma, Z., Xing, J., and Liu, H. (2004). Preparation and | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/64607 | - |
| dc.description.abstract | 岩藻糖水解酶屬於醣苷酶,首先於溶酶體內發現,負責切除醣複合物非還原端的岩藻糖。岩藻糖水解酶不正常地自細胞內分泌至細胞外液,與許多疾病進程相關,例如結腸癌、子宮頸癌和肝癌。血清岩藻糖水解酶活性在肝癌病患顯著高於健康正常組,酵素活性被認為是肝癌早期診斷的生物標誌物候選蛋白質。
先前本實驗室報導1-amino-1-deoxymethyl fuconojirimycin (FNJ) 和其衍生物是岩藻糖水解酶的有效抑制劑,抑制常數在μM 至 pM 範圍。本論文建構了簡單快速的方法,用於純化鑑定肝癌血清中的岩藻糖水解酶。主要將 FNJ 與活化載體上的 carbonyl diimidazole 耦合形成醯胺鍵,我們使用兩種載體,分別為瓊脂醣和磁性奈米粒子。以高效液相層析儀定量耦合釋出的 imidazole,計算出耦合產率約 70%。珠體的酵素結合能力,由結合後剩餘的岩藻糖水解酶活性決定,最佳結合能力為磁性奈米粒子每微莫耳活化位,結合約 326.5 微克的岩藻糖水解酶。含 0.5% SDS 的溶離液具有岩藻糖水解酶最高回收效率約 90%。這個純化方法應用在純化大腸桿菌粗抽液中的岩藻糖水解酶,以及人類血清中的酵素。在肝癌病患血清,鑑定出其內岩藻糖水解酶活性異常增高的主要酵素為溶酶體的岩藻糖水解酶。根據凝集素微陣列分析,初步純化之病患血清岩藻糖水解酶,可能具有 Fuc 相關的 N- 醣基化後修飾。抑制劑為主的親和性層析方法,同時應用在闡述幽門螺旋桿菌感染胃腺癌細胞後,共培養液中活性大量表現的葡萄糖苷酶種類。本研究證實抑制劑親和性層析方法為快速經濟的純化方法,有效應用於不同的複雜生物樣本。 | zh_TW |
| dc.description.abstract | α-L-fucosidase (AFU) is a glycosidase first found in lysosomes. This enzyme catalyzes the hydrolysis of fucose-containing glycoconjugates. The release of abnormal AFU from cells to extracellular fluid is linked to several disease processes, including colorectal cancer, ovarian cancer and hepatocellular carcinoma (HCC). The level of AFU activity from the serum of HCC patients is higher than that of normal people, indicating that the serum AFU is a potential biomarker for early diagnosis.
We previously demonstrated that 1-amino-1-deoxymethyl fuconojirimycin (FNJ) and derivatives are potent inhibitors of AFU (Ki values in the range of micro- to pico- molar). Herein in this thesis study, a facile method was developed for purification and identification of the serum AFU. The key step was to immobilize FNJ to carbonyl diimidazole-activated agarose matrix or magnetic nanoparticle via amide bond formation. The optimal immobilization yield was about 70%. The binding capacity was optimized to be 326.5 μg AFU/μmol on magnetic nanoparticle. Furthermore, the 0.5% SDS-containing eluent was found to offer the highest recovery yield of AFU about 90%. The method is applicable for purifying the AFU from human sera. For patients of HCC, the purified AFU is the lysosomal enzyme (FucA1), suggesting that FucA1 could be highly upregulated. It is of interest that the FucA1 of HCC contains fucosylated N-glycosylation. Additionally, the culture medium of H. pylori-infected gastric cancer cells was subjected to one step, deoxynojirimycin-based affinity chromatographic purification, leading to identification of a lysosomal α-glucosidase. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-16T17:57:43Z (GMT). No. of bitstreams: 1 ntu-101-R99b46007-1.pdf: 9104965 bytes, checksum: 1193bcfa1d9e52fe0c2807721f0ae836 (MD5) Previous issue date: 2012 | en |
| dc.description.tableofcontents | 口試委員會審定書 #
誌謝 i 中文摘要 ii 英文摘要 iii 圖目錄 viii 表目錄 xi 第一章 緒論 1 1.1. 岩藻糖水解酶與其相關疾病 1 1.2. 親和性層析法概述 4 1.3. 岩藻糖水解酶抑制劑之開發與應用 8 1.4. 岩藻醣水解酶之於肝癌檢測 13 第二章 材料與方法 15 一、實驗材料 15 二、實驗方法 15 2.1. 以大腸桿菌誘導表現海棲熱袍菌岩藻糖水解酶 (Tm FA) 15 2.2. 海棲熱袍菌岩藻糖水解酶 (Tm FA) 標準品純化 15 2.3. 蛋白質定量-Bradford法 16 2.4. 岩藻糖水解酶之活性測定 16 2.5. 薄層層析法 (Thin layer chromatography, TLC) 17 2.6. 定量岩藻糖水解酶抑制劑耦合於瓊脂醣產率 17 2.7. 高效能液相層析法分析咪唑 18 2.8. 蛋白質膠體電泳分析 18 2.9. 銀染法 19 2.10. 西方墨點法 20 2.11. 蛋白質鑑定前處理 21 2.11.1 膠體內水解 (In-gel digestion) 21 2.11.2 去鹽 (de-salt) 21 2.12. LC/MS-MS資料庫搜尋與數據分析 22 2.13. 醣基肽酶 (N-glycosidase F , PNGaseF) 去除N-醣基化 22 2.14. 凝集素陣列分析 (Lectin array) 23 2.15. 酵素免疫連接吸附法 25 2.16. 共軛焦螢光顯微鏡與細胞成像 26 第三章 結果 27 3.1 岩藻糖水解酶抑制劑親和性層析管柱純化方法建構 27 3.1.1 岩藻糖水解酶抑制劑合成 27 3.1.2 定量岩藻糖水解酶抑制劑耦合於瓊脂醣產率 30 3.1.3 檢測岩藻糖水解酶抑制劑@瓊脂糖之結合岩藻糖水解酶能力 33 3.1.4 以岩藻糖水解酶抑制劑@瓊脂醣純化菌液中岩藻糖水解酶 37 3.1.4.1 沖洗非專一性結合蛋白質條件測試 37 3.1.4.2 沖堤岩藻糖水解酶條件測試 39 3.1.4.3 純化大腸桿菌破菌液內岩藻糖水解酶的純化倍率 44 3.2 以磁性奈米粒子建構岩藻糖水解酶抑制劑親和性層析法 47 3.2.1 岩藻糖水解酶抑制劑耦合磁性奈米粒子與定量耦合產率 47 3.2.2 檢測岩藻糖水解酶抑制劑@磁性奈米粒子之酵素結合能力 49 3.2.3 岩藻糖水解酶抑制劑@磁性奈米粒子之純化倍率 52 3.3 抑制劑親和性層析管柱方法應用 54 3.3.1 鑑定肝癌病患血清內岩藻糖水解酶 54 3.3.1.1 測定血清內岩藻糖水解酶活性 54 3.3.1.2 純化及鑑定血清內岩藻醣水解酶 58 3.3.1.3 血清內岩藻糖水解酶糖化修飾鑑定 70 3.3.2 幽門螺旋桿菌促使胃腺癌細胞分泌α-葡萄糖苷酶純化與鑑定 78 第四章 討論 88 4.1 抑制劑親和性純化配體選擇與純化策略 88 4.2 抑制劑親和性純化法載體選擇 89 4.3 肝癌病患血清內岩藻糖水解酶種類探討 89 4.4 人類血清岩藻糖水解酶醣化修飾探討 91 4.5 幽門螺旋桿菌促使胃腺癌細胞分泌溶酶體α-葡萄糖苷酶 92 第五章 結論 94 第六章 參考文獻 95 附錄一 儀器設備 113 附錄二 光譜數據 115 | |
| dc.language.iso | zh-TW | |
| dc.subject | 抑制劑親和層析法 | zh_TW |
| dc.subject | 岩藻糖水解酶 | zh_TW |
| dc.subject | 肝癌 | zh_TW |
| dc.subject | 葡萄糖苷 | zh_TW |
| dc.subject | inhibitor-based chromatography | en |
| dc.subject | α-glucosidase | en |
| dc.subject | α-L-fucosidase | en |
| dc.subject | hepatocellular carcinoma | en |
| dc.title | 開發抑制劑為主的親和性層析方法以快速純化岩藻糖水解酶 | zh_TW |
| dc.title | Rapid identification of α-L-fucosidase via inhibitor-based affinity chromatography | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 100-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 林俊成(Chun-Cheng Lin),陳玉如(Yu-Ju Chen) | |
| dc.subject.keyword | 岩藻糖水解酶,肝癌,抑制劑親和層析法,葡萄糖苷,酶, | zh_TW |
| dc.subject.keyword | α-L-fucosidase,hepatocellular carcinoma,inhibitor-based chromatography,α-glucosidase, | en |
| dc.relation.page | 122 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2012-08-13 | |
| 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 未授權公開取用 | 8.89 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。
