請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/23363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 | Chang-Szu Cho | en |
| dc.contributor.author | 卓昶思 | zh_TW |
| dc.date.accessioned | 2021-06-08T04:59:48Z | - |
| dc.date.copyright | 2010-08-19 | |
| dc.date.issued | 2010 | |
| dc.date.submitted | 2010-08-17 | |
| dc.identifier.citation | 1. Bizzozero, G. (1893) Ueber die schlauchfo¨rmigen Dru¨sen des Magendarmkanals und die Beziehungen ihres Epithels zu dem Oberfla¨chenepithel der Schleimhaut., Dritte mitteilung. Archiv Mikroskopische Anat 43, 82-152.
2. Kusters, J. G., van Vliet, A. H., and Kuipers, E. J. (2006) Pathogenesis of Helicobacter pylori infection, Clin Microbiol Rev 19, 449-490. 3. Krienitz, W. (1906) Ueber das auftreten von mageninhalt bei carcinoma ventriculi., Dtsch. Med. Wochenschr 22, 872. 4. Luger, A. (1917) Ueber spirochaeten und fusiforme bazillen im darm, miteiner beitrag zur frage der lamblien-enteritis. , Wiein. Klin. Wochenschr. 52, 1643-1647. 5. Warren, J. R., and B. J. Marshall. (1983) Unidentified curved bacilli on gastric epithelium in active chronic gastritis, Lancet 1, 1273-1275. 6. Marshall, B. J., J. A. Armstrong, D. B. McGechie, and R. J. Glancy. . (1985) Attempt to fulfil Koch’s postulates for pyloric Campylobacter. , Med. J. Austr. 142, 436-439. 7. Morris, A., and Nicholson, G. (1987) Ingestion of Campylobacter pyloridis causes gastritis and raised fasting gastric pH, Am J Gastroenterol 82, 192-199. 8. Kusters, J. G., Gerrits, M. M., Van Strijp, J. A., and Vandenbroucke-Grauls, C. M. (1997) Coccoid forms of Helicobacter pylori are the morphologic manifestation of cell death, Infect Immun 65, 3672-3679. 9. Enroth, H., Wreiber, K., Rigo, R., Risberg, D., Uribe, A., and Engstrand, L. (1999) In vitro aging of Helicobacter pylori: changes in morphology, intracellular composition and surface properties, Helicobacter 4, 7-16. 10. O'Toole, P. W., Lane, M. C., and Porwollik, S. (2000) Helicobacter pylori motility, Microbes Infect 2, 1207-1214. 11. Scott, D. R., E. A. Marcus, D. L. Weeks, and G. Sachs. (2002) Mechanisms of acid resistance due to the urease system of Helicobacter pylori., Gastroenterology 123, 187-195. 12. Alm, R. A., Ling, L. S., Moir, D. T., King, B. L., Brown, E. D., Doig, P. C., Smith, D. R., Noonan, B., Guild, B. C., deJonge, B. L., Carmel, G., Tummino, P. J., Caruso, A., Uria-Nickelsen, M., Mills, D. M., Ives, C., Gibson, R., Merberg, D., Mills, S. D., Jiang, Q., Taylor, D. E., Vovis, G. F., and Trust, T. J. (1999) Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori, Nature 397, 176-180. 13. Boneca, I. G., de Reuse, H., Epinat, J. C., Pupin, M., Labigne, A., and Moszer, I. (2003) A revised annotation and comparative analysis of Helicobacter pylori genomes, Nucleic Acids Res 31, 1704-1714. 14. Tomb, J. F., White, O., Kerlavage, A. R., Clayton, R. A., Sutton, G. G., Fleischmann, R. D., Ketchum, K. A., Klenk, H. P., Gill, S., Dougherty, B. A., Nelson, K., Quackenbush, J., Zhou, L., Kirkness, E. F., Peterson, S., Loftus, B., Richardson, D., Dodson, R., Khalak, H. G., Glodek, A., McKenney, K., Fitzegerald, L. M., Lee, N., Adams, M. D., Hickey, E. K., Berg, D. E., Gocayne, J. D., Utterback, T. R., Peterson, J. D., Kelley, J. M., Cotton, M. D., Weidman, J. M., Fujii, C., Bowman, C., Watthey, L., Wallin, E., Hayes, W. S., Borodovsky, M., Karp, P. D., Smith, H. O., Fraser, C. M., and Venter, J. C. (1997) The complete genome sequence of the gastric pathogen Helicobacter pylori, Nature 388, 539-547. 15. Achtman, M., and Suerbaum, S. (2000) Sequence variation in Helicobacter pylori, Trends Microbiol 8, 57-58. 16. Falush, D., Wirth, T., Linz, B., Pritchard, J. K., Stephens, M., Kidd, M., Blaser, M. J., Graham, D. Y., Vacher, S., Perez-Perez, G. I., Yamaoka, Y., Megraud, F., Otto, K., Reichard, U., Katzowitsch, E., Wang, X., Achtman, M., and Suerbaum, S. (2003) Traces of human migrations in Helicobacter pylori populations, Science 299, 1582-1585. 17. Suerbaum, S., and Achtman, M. (2004) Helicobacter pylori: recombination, population structure and human migrations, Int J Med Microbiol 294, 133-139. 18. Falush, D., Kraft, C., Taylor, N. S., Correa, P., Fox, J. G., Achtman, M., and Suerbaum, S. (2001) Recombination and mutation during long-term gastric colonization by Helicobacter pylori: estimates of clock rates, recombination size, and minimal age, Proc Natl Acad Sci U S A 98, 15056-15061. 19. Suerbaum, S., and Achtman, M. (1999) Evolution of Helicobacter pylori: the role of recombination, Trends Microbiol 7, 182-184. 20. Algood, H. M., and Cover, T. L. (2006) Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defenses, Clin Microbiol Rev 19, 597-613. 21. Parsonnet, J. (1998) Helicobacter pylori, Infect Dis Clin North Am 12, 185-197. 22. Taylor, D. N., and Blaser, M. J. (1991) The epidemiology of Helicobacter pylori infection, Epidemiol Rev 13, 42-59. 23. Perez-Perez, G. I., Rothenbacher, D., and Brenner, H. (2004) Epidemiology of Helicobacter pylori infection, Helicobacter 9 Suppl 1, 1-6. 24. Pounder, R. E., and Ng, D. (1995) The prevalence of Helicobacter pylori infection in different countries, Aliment Pharmacol Ther 9 Suppl 2, 33-39. 25. Fiedorek, S. C., Malaty, H. M., Evans, D. L., Pumphrey, C. L., Casteel, H. B., Evans, D. J., Jr., and Graham, D. Y. (1991) Factors influencing the epidemiology of Helicobacter pylori infection in children, Pediatrics 88, 578-582. 26. Lin, C. W., Chang, Y. S., Wu, S. C., and Cheng, K. S. (1998) Helicobacter pylori in gastric biopsies of Taiwanese patients with gastroduodenal diseases, Jpn J Med Sci Biol 51, 13-23. 27. Teh, B. H., Lin, J. T., Pan, W. H., Lin, S. H., Wang, L. Y., Lee, T. K., and Chen, C. J. (1994) Seroprevalence and associated risk factors of Helicobacter pylori infection in Taiwan, Anticancer Res 14, 1389-1392. 28. Brown, L. M. (2000) Helicobacter pylori: epidemiology and routes of transmission, Epidemiol Rev 22, 283-297. 29. Ernst, P. B., and Gold, B. D. (2000) The disease spectrum of Helicobacter pylori: the immunopathogenesis of gastroduodenal ulcer and gastric cancer, Annu Rev Microbiol 54, 615-640. 30. Kuipers, E. J. (1999) Review article: exploring the link between Helicobacter pylori and gastric cancer., Aliment. Pharmacol. Ther. 13, 3-12. 31. Kuipers, E. J., Thijs, J. C., and Festen, H. P. (1995) The prevalence of Helicobacter pylori in peptic ulcer disease, Aliment Pharmacol Ther 9 Suppl 2, 59-69. 32. Armstrong, J. A., Wee, S. H., Goodwin, C. S., and Wilson, D. H. (1987) Response of Campylobacter pyloridis to antibiotics, bismuth and an acid-reducing agent in vitro--an ultrastructural study, J Med Microbiol 24, 343-350. 33. Lambert, J. R., and Midolo, P. (1997) The actions of bismuth in the treatment of Helicobacter pylori infection, Aliment Pharmacol Ther 11 Suppl 1, 27-33. 34. Vogt, K., M. Warrelmann, and H. Hahn. (1989) The minimum inhibitory concentrations of various bismuth salts against Campylobacter pylori., Zentbl. Bakteriol. 271, 304-308. 35. Johansson, E. L., Bergquist, C., Edebo, A., Johansson, C., and Svennerholm, A. M. (2004) Comparison of different routes of vaccination for eliciting antibody responses in the human stomach, Vaccine 22, 984-990. 36. Keller, W. C., and Michetti, P. (2001) Vaccination against Helicobacter pylori --an old companion of man, Expert Opin Biol Ther 1, 795-802. 37. Kreiss, C., Buclin, T., Cosma, M., Corthesy-Theulaz, I., and Michetti, P. (1996) Safety of oral immunisation with recombinant urease in patients with Helicobacter pylori infection, Lancet 347, 1630-1631. 38. Voland, P., Zeitner, M., Hafsi, N., and Prinz, C. (2006) Human immune response towards recombinant Helicobacter pylori urease and cellular fractions, Vaccine 24, 3832-3839. 39. Midolo, P. D., Lambert, J. R., Hull, R., Luo, F., and Grayson, M. L. (1995) In vitro inhibition of Helicobacter pylori NCTC 11637 by organic acids and lactic acid bacteria, J Appl Bacteriol 79, 475-479. 40. Lorca, G. L., Wadstrom, T., Valdez, G. F., and Ljungh, A. (2001) Lactobacillus acidophilus autolysins inhibit Helicobacter pylori in vitro, Curr Microbiol 42, 39-44. 41. Armuzzi, A., Cremonini, F., Bartolozzi, F., Canducci, F., Candelli, M., Ojetti, V., Cammarota, G., Anti, M., De Lorenzo, A., Pola, P., Gasbarrini, G., and Gasbarrini, A. (2001) The effect of oral administration of Lactobacillus GG on antibiotic-associated gastrointestinal side-effects during Helicobacter pylori eradication therapy, Aliment Pharmacol Ther 15, 163-169. 42. Burne, R. A., and Chen, Y. Y. (2000) Bacterial ureases in infectious diseases, Microbes Infect 2, 533-542. 43. Bijlsma, J. J., Lie, A. L. M., Nootenboom, I. C., Vandenbroucke-Grauls, C. M., and Kusters, J. G. (2000) Identification of loci essential for the growth of Helicobacter pylori under acidic conditions, J Infect Dis 182, 1566-1569. 44. Stingl, K., K. Altendorf, and E. P. Bakker. (2002) Acid survival of Helicobacter pylori: how does urease activity trigger cytoplasmic pH homeostasis?, Trends Microbiol. 10, 70-74. 45. Scott, D. R., Weeks, D., Hong, C., Postius, S., Melchers, K., and Sachs, G. (1998) The role of internal urease in acid resistance of Helicobacter pylori, Gastroenterology 114, 58-70. 46. Tummuru, M. K., Cover, T. L., and Blaser, M. J. (1993) Cloning and expression of a high-molecular-mass major antigen of Helicobacter pylori: evidence of linkage to cytotoxin production, Infect Immun 61, 1799-1809. 47. Miehlke, S., Go, M. F., Kim, J. G., Graham, D. Y., and Figura, N. (1998) Serologic detection of Helicobacter pylori infection with cagA-positive strains in duodenal ulcer, gastric cancer, and asymptomatic gastritis, J Gastroenterol 33 Suppl 10, 18-21. 48. Cover, T. L., Glupczynski, Y., Lage, A. P., Burette, A., Tummuru, M. K., Perez-Perez, G. I., and Blaser, M. J. (1995) Serologic detection of infection with cagA+ Helicobacter pylori strains, J Clin Microbiol 33, 1496-1500. 49. Christie, P. J., and Vogel, J. P. (2000) Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells, Trends Microbiol 8, 354-360. 50. Covacci, A., Censini, S., Bugnoli, M., Petracca, R., Burroni, D., Macchia, G., Massone, A., Papini, E., Xiang, Z., Figura, N., and et al. (1993) Molecular characterization of the 128-kDa immunodominant antigen of Helicobacter pylori associated with cytotoxicity and duodenal ulcer, Proc Natl Acad Sci U S A 90, 5791-5795. 51. Fischer, W., Puls, J., Buhrdorf, R., Gebert, B., Odenbreit, S., and Haas, R. (2001) Systematic mutagenesis of the Helicobacter pylori cag pathogenicity island: essential genes for CagA translocation in host cells and induction of interleukin-8, Mol Microbiol 42, 1337-1348. 52. Stein, M., Rappuoli, R., and Covacci, A. (2000) Tyrosine phosphorylation of the Helicobacter pylori CagA antigen after cag-driven host cell translocation, Proc Natl Acad Sci U S A 97, 1263-1268. 53. Selbach, M., S. Moese, C. R. Hauck, T. F. Meyer, and S. Backert. (2002) Src is the kinase of the Helicobacter pylori CagA protein in vitro and in vivo., J. Biol. Chem. 277, 6775-6778. 54. Stein, M., F. Bagnoli, R. Halenbeck, R. Rappuoli, W. J. Fantl, and A. Covacci. (2002) c-Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs., Mol. Microbiol. 43, 971-981. 55. Moese, S., Selbach, M., Kwok, T., Brinkmann, V., Konig, W., Meyer, T. F., and Backert, S. (2004) Helicobacter pylori induces AGS cell motility and elongation via independent signaling pathways, Infect Immun 72, 3646-3649. 56. Selbach, M., Moese, S., Backert, S., Jungblut, P. R., and Meyer, T. F. (2004) The Helicobacter pylori CagA protein induces tyrosine dephosphorylation of ezrin, Proteomics 4, 2961-2968. 57. Argent, R. H., Kidd, M., Owen, R. J., Thomas, R. J., Limb, M. C., and Atherton, J. C. (2004) Determinants and consequences of different levels of CagA phosphorylation for clinical isolates of Helicobacter pylori, Gastroenterology 127, 514-523. 58. Higashi, H., R. Tsutsumi, A. Fujita, S. Yamazaki, M. Asaka, T. Azuma, and M. Hatakeyama. (2002) Biological activity of the Helicobacter pylori virulence factor CagA is determined by variation in the tyrosine phosphorylation sites., Proc. Natl. Acad. Sci. USA 99, 14428-14433. 59. Viala, J., Chaput, C., Boneca, I. G., Cardona, A., Girardin, S. E., Moran, A. P., Athman, R., Memet, S., Huerre, M. R., Coyle, A. J., DiStefano, P. S., Sansonetti, P. J., Labigne, A., Bertin, J., Philpott, D. J., and Ferrero, R. L. (2004) Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island, Nat Immunol 5, 1166-1174. 60. Azuma, T., A. Yamakawa, S. Yamazaki, K. Fukuta, M. Ohtani, Y. Ito, M. Dojo, Y. Yamazaki, and M. Kuriyama. (2002) Correlation between variation of the 3'- region of the cagA gene in Helicobacter pylori and disease outcome in Japan. , J. Infect. Dis. 186, 1621-1630. 61. Yamazaki, S., A. Yamakawa, Y. Ito, M. Ohtani, H. Higashi, M. Hatakeyama, and T. Azuma. (2003) The CagA protein of Helicobacter pylori is translocated into epithelial cells and binds to SHP-2 in human gastric mucosa., J. Infect. Dis. 187, 334-337. 62. Cover, T. L., and Blaser, M. J. (1992) Purification and characterization of the vacuolating toxin from Helicobacter pylori, J Biol Chem 267, 10570-10575. 63. Cover, T. L., and Blanke, S. R. (2005) Helicobacter pylori VacA, a paradigm for toxin multifunctionality, Nat Rev Microbiol 3, 320-332. 64. Hennig, E. E., Godlewski, M. M., Butruk, E., and Ostrowski, J. (2005) Helicobacter pylori VacA cytotoxin interacts with fibronectin and alters HeLa cell adhesion and cytoskeletal organization in vitro, FEMS Immunol Med Microbiol 44, 143-150. 65. Atherton, J. C., Cao, P., Peek, R. M., Jr., Tummuru, M. K., Blaser, M. J., and Cover, T. L. (1995) Mosaicism in vacuolating cytotoxin alleles of Helicobacter pylori. Association of specific vacA types with cytotoxin production and peptic ulceration, J Biol Chem 270, 17771-17777. 66. van Doorn, L. J., Figueiredo, C., Sanna, R., Pena, S., Midolo, P., Ng, E. K., Atherton, J. C., Blaser, M. J., and Quint, W. G. (1998) Expanding allelic diversity of Helicobacter pylori vacA, J Clin Microbiol 36, 2597-2603. 67. Suerbaum, S., Josenhans, C., Sterzenbach, T., Drescher, B., Brandt, P., Bell, M., Droge, M., Fartmann, B., Fischer, H. P., Ge, Z., Horster, A., Holland, R., Klein, K., Konig, J., Macko, L., Mendz, G. L., Nyakatura, G., Schauer, D. B., Shen, Z., Weber, J., Frosch, M., and Fox, J. G. (2003) The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus, Proc Natl Acad Sci U S A 100, 7901-7906. 68. Ando, T., Peek, R. M., Pride, D., Levine, S. M., Takata, T., Lee, Y. C., Kusugami, K., van der Ende, A., Kuipers, E. J., Kusters, J. G., and Blaser, M. J. (2002) Polymorphisms of Helicobacter pylori HP0638 reflect geographic origin and correlate with cagA status, J Clin Microbiol 40, 239-246. 69. Yamaoka, Y., Kikuchi, S., el-Zimaity, H. M., Gutierrez, O., Osato, M. S., and Graham, D. Y. (2002) Importance of Helicobacter pylori oipA in clinical presentation, gastric inflammation, and mucosal interleukin 8 production, Gastroenterology 123, 414-424. 70. Boren, T., Falk, P., Roth, K. A., Larson, G., and Normark, S. (1993) Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens, Science 262, 1892-1895. 71. Guruge, J. L., Falk, P. G., Lorenz, R. G., Dans, M., Wirth, H. P., Blaser, M. J., Berg, D. E., and Gordon, J. I. (1998) Epithelial attachment alters the outcome of Helicobacter pylori infection, Proc Natl Acad Sci U S A 95, 3925-3930. 72. Rad, R., Gerhard, M., Lang, R., Schoniger, M., Rosch, T., Schepp, W., Becker, I., Wagner, H., and Prinz, C. (2002) The Helicobacter pylori blood group antigen-binding adhesin facilitates bacterial colonization and augments a nonspecific immune response, J Immunol 168, 3033-3041. 73. Gerhard, M., Lehn, N., Neumayer, N., Boren, T., Rad, R., Schepp, W., Miehlke, S., Classen, M., and Prinz, C. (1999) Clinical relevance of the Helicobacter pylori gene for blood-group antigen-binding adhesin, Proc Natl Acad Sci U S A 96, 12778-12783. 74. 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., and Boren, T. (2002) Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation, Science 297, 573-578. 75. Roche, N., Angstrom, J., Hurtig, M., Larsson, T., Boren, T., and Teneberg, S. (2004) Helicobacter pylori and complex gangliosides, Infect Immun 72, 1519-1529. 76. Walsh, E. J., and Moran, A. P. (1997) Influence of medium composition on the growth and antigen expression of Helicobacter pylori, J Appl Microbiol 83, 67-75. 77. D.J. Evans Jr., D. G. E., T. Takemura, H. Nakano, H.C. Lampert, D.Y. Graham, D.N. Granger, P.R. Kvietys. (1995) Characterization of a Helicobacter pylori neutrophil activating protein., Infect. Immun. 63, 213-2220. 78. F. Tonello, W. G. D., B. Satin, M. Molinari, G. Tognon, G. Grandi, G. Del Giudice, R. Rappuoli, C. Montecucco. (1999) The Helicobacter pylori neutrophilactivating protein is an iron-binding protein with dodecameric structure., Mol. Microbiol. 34, 238-246. 79. G. Zanotti, E. P., W. Dundon, R. Battistutta, M. Seveso, G. Del Giudice, R. Rappuoli, C. Montecucco. (2002) Structure of the neutrophil-activating protein from Helicobacter pylori., J. Mol. Biol. 323, 125-130. 80. B. Satin, G. D. G., V. Della Bianca, S. Dusi, C. Laudanna, F. Tonello, D., and Kelleher, R. R., C. Montecucco, F. Rossi. (2000) The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a protective antigen and a major virulence factor, J. Exp. Med. 191, 1467-1476. 81. Namavar, F., Sparrius, M., Veerman, E. C., Appelmelk, B. J., and Vandenbroucke-Grauls, C. M. (1998) Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin, Infect Immun 66, 444-447. 82. Montemurro, P., Nishioka, H., Dundon, W. G., de Bernard, M., Del Giudice, G., Rappuoli, R., and Montecucco, C. (2002) The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a potent stimulant of mast cells, Eur J Immunol 32, 671-676. 83. Nilsson, C., Skoglund, A., Moran, A. P., Annuk, H., Engstrand, L., and Normark, S. (2008) Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases, PLoS One 3, e3811. 84. Moran, A. P. (2007) Lipopolysaccharide in bacterial chronic infection: insights from Helicobacter pylori lipopolysaccharide and lipid A, Int J Med Microbiol 297, 307-319. 85. Moran, A. P., Helander, I. M., and Kosunen, T. U. (1992) Compositional analysis of Helicobacter pylori rough-form lipopolysaccharides, J Bacteriol 174, 1370-1377. 86. Moran, A. P. (2008) Relevance of fucosylation and Lewis antigen expression in the bacterial gastroduodenal pathogen Helicobacter pylori, Carbohydr Res 343, 1952-1965. 87. Moran, A. P., Knirel, Y. A., Senchenkova, S. N., Widmalm, G., Hynes, S. O., and Jansson, P. E. (2002) Phenotypic variation in molecular mimicry between Helicobacter pylori lipopolysaccharides and human gastric epithelial cell surface glycoforms. Acid-induced phase variation in Lewis(x) and Lewis(y) expression by H. Pylori lipopolysaccharides, J Biol Chem 277, 5785-5795. 88. Sandhoff, K., and Wassle, W. (1971) Enrichment and characterization of 2 forms of human N-acetyl-beta-D-hexosaminidase, Hoppe Seylers Z Physiol Chem 352, 1119-1133. 89. Hou, Y., Vocadlo, D., Withers, S., and Mahuran, D. (2000) Role of beta Arg211 in the active site of human beta-hexosaminidase B, Biochemistry 39, 6219-6227. 90. Mahuran, D. J. (1995) Beta-hexosaminidase: biosynthesis and processing of the normal enzyme, and identification of mutations causing Jewish Tay-Sachs disease, Clin Biochem 28, 101-106. 91. Mahuran, D. J., Neote, K., Klavins, M. H., Leung, A., and Gravel, R. A. (1988) Proteolytic processing of pro-alpha and pro-beta precursors from human beta-hexosaminidase. Generation of the mature alpha and beta a beta b subunits, J Biol Chem 263, 4612-4618. 92. Weitz, G., and Proia, R. L. (1992) Analysis of the glycosylation and phosphorylation of the alpha-subunit of the lysosomal enzyme, beta-hexosaminidase A, by site-directed mutagenesis, J Biol Chem 267, 10039-10044. 93. Sonderfeld-Fresko, S., and Proia, R. L. (1989) Analysis of the glycosylation and phosphorylation of the lysosomal enzyme, beta-hexosaminidase B, by site-directed mutagenesis, J Biol Chem 264, 7692-7697. 94. Mahuran, D. J. (1999) Biochemical consequences of mutations causing the GM2 gangliosidoses, Biochim Biophys Acta 1455, 105-138. 95. Olszewska, E., Olszewski, S., Borzym-Kluczyk, M., and Zwierz, K. (2007) Role of N-acetyl-beta-D-hexosaminidase in cholesteatoma tissue, Acta Biochim Pol 54, 365-370. 96. Bazzi, C., Petrini, C., Rizza, V., Arrigo, G., Napodano, P., Paparella, M., and D'Amico, G. (2002) Urinary N-acetyl-beta-glucosaminidase excretion is a marker of tubular cell dysfunction and a predictor of outcome in primary glomerulonephritis, Nephrol Dial Transplant 17, 1890-1896. 97. Popko, J., Zalewska, A., Golaszewska, Z., Marciniak, J., Sierakowski, S., Worowski, K., and Zwierz, K. (2005) Comparative analysis of hexosaminidase and cathepsin D expression in synovial fluid of patients with rheumatoid arthritis and traumatized joints, Clin Exp Rheumatol 23, 725-726. 98. Popko, J., Zalewska, A., Olszewski, S., Gorska, A., Sierakowski, S., Zwierz, K., and Urban, M. (2003) Activity of N-acetyl-beta hexosaminidase in serum and joint fluid of the knees of patients with juvenile idiopatic arthritis, Clin Exp Rheumatol 21, 675. 99. Liu, J., Numa, M. M., Liu, H., Huang, S. J., Sears, P., Shikhman, A. R., and Wong, C. H. (2004) Synthesis and high-throughput screening of N-acetyl-beta-hexosaminidase inhibitor libraries targeting osteoarthritis, J Org Chem 69, 6273-6283. 100. Perez-Blanco, F. J., Ruiz-Martin, A., Moreno-Terribas, G., and Cantero-Hinojosa, J. (1996) Urinary activity of N-acetyl-beta-glycosaminidase (NAG) in arterial hypertension, Clin Nephrol 45, 65-66. 101. Lugering, N., Stoll, R., Siekmann, A., Faulhaber, J., Heese, C., Dietrich, O., Kucharzik, T., Busch, H., Hasilik, A., and Domschke, W. (1995) Elevated levels of activities of beta-hexosaminidase and alpha-mannosidase in human immunodeficiency virus-infected patients, J Infect Dis 171, 683-686. 102. Lo, C. H., and Kritchevsky, D. (1978) Human serum hexosaminidase: elevated B form isozyme in cancer patients, J Med 9, 313-336. 103. Pretlow, T. G., 2nd, Harris, B. E., Bradley, E. L., Jr., Bueschen, A. J., Lloyd, K. L., and Pretlow, T. P. (1985) Enzyme activities in prostatic carcinoma related to Gleason grades, Cancer Res 45, 442-446. 104. Tomasiak, M. M., Tomasiak, M., Zietkowski, Z., Skiepko, R., and Bodzenta-Lukaszyk, A. (2008) N-acetyl-beta-hexosaminidase activity in asthma, Int Arch Allergy Immunol 146, 133-137. 105. Shikhman, A. R., Brinson, D. C., and Lotz, M. (2000) Profile of glycosaminoglycan-degrading glycosidases and glycoside sulfatases secreted by human articular chondrocytes in homeostasis and inflammation, Arthritis Rheum 43, 1307-1314. 106. Liu, J., Shikhman, A. R., Lotz, M. K., and Wong, C. H. (2001) Hexosaminidase inhibitors as new drug candidates for the therapy of osteoarthritis, Chem Biol 8, 701-711. 107. Ho, C. W., Popat, S. D., Liu, T. W., Tsai, K. C., Ho, M. J., Chen, W. H., Yang, A. S., and Lin, C. H. (2010) Development of GlcNAc-inspired iminocyclitiols as potent and selective N-acetyl-beta-hexosaminidase inhibitors, ACS Chem Biol 5, 489-497. 108. Batista, L., Miller, F., Clave, C., Arfi, A., Douillard-Guilloux, G., Couraud, P. O., and Caillaud, C. (2010) Induced secretion of beta-hexosaminidase by human brain endothelial cells: a novel approach in Sandhoff disease?, Neurobiol Dis 37, 656-660. 109. Koo, I. C., Ohol, Y. M., Wu, P., Morisaki, J. H., Cox, J. S., and Brown, E. J. (2008) Role for lysosomal enzyme beta-hexosaminidase in the control of mycobacteria infection, Proc Natl Acad Sci U S A 105, 710-715. 110. 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. 111. Kawakubo, M., Ito, Y., Okimura, Y., Kobayashi, M., Sakura, K., Kasama, S., Fukuda, M. N., Fukuda, M., Katsuyama, T., and Nakayama, J. (2004) Natural antibiotic function of a human gastric mucin against Helicobacter pylori infection, Science 305, 1003-1006. 112. Hase, K., Murakami, M., Iimura, M., Cole, S. P., Horibe, Y., Ohtake, T., Obonyo, M., Gallo, R. L., Eckmann, L., and Kagnoff, M. F. (2003) Expression of LL-37 by human gastric epithelial cells as a potential host defense mechanism against Helicobacter pylori, Gastroenterology 125, 1613-1625. 113. Pennybacker, M., Liessem, B., Moczall, H., Tifft, C. J., Sandhoff, K., and Proia, R. L. (1996) Identification of domains in human beta-hexosaminidase that determine substrate specificity, J Biol Chem 271, 17377-17382. 114. Yi, E. C., and Hackett, M. (2000) Rapid isolation method for lipopolysaccharide and lipid A from gram-negative bacteria, Analyst 125, 651-656. 115. Darveau, R. P., and Hancock, R. E. (1983) Procedure for isolation of bacterial lipopolysaccharides from both smooth and rough Pseudomonas aeruginosa and Salmonella typhimurium strains, J Bacteriol 155, 831-838. 116. Tsai, C. M., and Frasch, C. E. (1982) A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels, Anal Biochem 119, 115-119. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/23363 | - |
| dc.description.abstract | 全球約有50%人口身上帶有胃幽門螺旋桿菌感染。在相關醫學研究中，已確立胃幽門桿菌之感染為導致腸胃道疾病如胃炎、胃潰瘍及胃癌的主要原因之一，雖然已有許多研究揭露胃幽門桿菌的致病機制，但對於在感染中宿主細胞與胃幽門桿菌之間詳細的互動機制仍不甚清楚。先前本實驗室發現胃幽門桿菌之感染會促使宿主細胞分泌出第二型岩藻醣水解酶，且此酵素可加強胃幽門桿菌附著於宿主細胞的能力，在感染及致病過程中扮演重要角色。本研究中進一步發現，另一種糖解酵素-乙醯胺基葡萄糖水解酶亦存在於胃幽門桿菌感染宿主細胞的狀況下。與未感染的對照組比較，不論是以原生型或是由臨床病人身上分離的胃幽門桿菌感染宿主細胞，共同培養液中的乙醯胺基葡萄糖水解酶活性都會顯著提高。此外，乙醯胺基葡萄糖水解酶於實驗中具有抑制胃幽門桿菌生長之作用。雖目前尚未釐清何種因子會造成此酵素的釋放，以及此酵素透過何種機制影響胃幽門桿菌的存活，這些發現仍進一步地揭露了胃幽門桿菌與宿主細胞於感染過程中的交互作用。 | zh_TW |
| dc.description.abstract | Infection about one half of the global population, the bacterial pathogen H. pylori is the primary cause of gastritis, duodenal ulcer and gastric cancer. Despite the well-known infection mechanism, the interactions between H. pylori and the host during infection are not fully understood. We previously identified α-L-fucosidase to be secreted from host cells upon H. pylori infection. The enzyme is connected to the bacterial adhesion, growth and pathogenicity of the pathogen. Here we report the presence of another glycosidase, N-acetyl-β-D-hexosaminidase, under co-culture conditions, but with a different scenario. In comparison with a negative control (no infection, the level of β-hexosaminidase activity was greatly enhanced upon the infection of H. pylori strains, including wild type and other clinical isolates. In addition, the presence of β-hexosaminidase significantly reduced the viability of H. pylori in vitro. Although it still remain unclear about what factors contribute to the release of β-hexosaminidase, and how the enzyme affects the bacterial survival, this study provides another example of host-pathogen interaction. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-08T04:59:48Z (GMT). No. of bitstreams: 1 ntu-99-R97b46012-1.pdf: 2366111 bytes, checksum: 37b458674752fba7efe2b3f8cd4cadbe (MD5) Previous issue date: 2010 | en |
| dc.description.tableofcontents | Acknowledgement I
Abbreviations II 中文摘要 III Abstract IIII Chapter 1 Introduction 1 1.1 Helicobacter pylori 1 1.2 Major virulence and colonization factors of Helicobacter pylori 11 1.3 N-acetyl-β-D-hexosaminidase 18 1.4 Research motivation 23 Chapter 2 Results 25 2.1 Glycoside hydrolase activities in AGS/H. pylori co-culture medium 25 2.2 Increased activity of β-hexosaminidase in co-culture medium 25 2.3 Identification of human N-acetyl-β-D-hexosaminidase in co-culture medium 27 2.4 β-hexosaminidase could have bactericidal effect on H. pylori in vitro 28 2.5 Effect of virulence and other factors on β-hexosaminidase secretion 28 2.6 Effect of human β-hexosaminidase on H. pylori LPS 30 Chapter 3 Discussion 31 3.1 Role of β-hexosaminidase in the infection of H. pylori to gastric cancer cells 31 3.2 Secretion of glycosidases as a host defense mechanism in H. pylori infection 33 Chapter 4 Materials and Methods 35 4.1 H. pylori strains and cell lines 35 4.2 H. pylori co-culture condition 35 4.3 Enzyme activity assay 36 4.4 Immunoblotting 37 4.5 In-gel digestion 38 4.6 Mass spectrometry analysis 40 4.7 Cloning, expression and purification of recombinant human β-hexosaminidase 41 4.8 Colony-forming assay 41 4.9 H. pylori LPS extraction by Tri-reagent® method 42 4.10 Modified silver-staining method for LPS 43 4.11 Purification of β-hexosaminidase by immunoprecipitation 44 Chapter 5 Conclusion 45 Chapter 6 References 46 Chapter 7 Legends of table and figures 67 | |
| dc.language.iso | en | |
| dc.title | 乙醯基胺葡萄糖水解酶於胃幽門桿菌感染胃癌細胞扮演之角色 | zh_TW |
| dc.title | Role of N-acetyl-beta-D-hexosaminidase in the infection of Helicobacter pylori to gastric cancer cells | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 98-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 吳明賢(Ming-Shiang Wu),賈景山(Jean-San Chia),吳世雄(Shih-Hsiung Wu) | |
| dc.subject.keyword | 胃幽門桿菌,岩藻醣水解酶,乙醯胺基葡萄糖水解酶,腸胃道疾病, | zh_TW |
| dc.subject.keyword | H. pylori,α-L-fucosidase,N-acetyl-β-D-hexosaminidase,gastric diseases, | en |
| dc.relation.page | 80 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2010-08-18 | |
| 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-99-1.pdf 目前未授權公開取用 | 2.31 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。