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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 陳水田(Shui-Tein Chen) | |
| dc.contributor.author | Tz-Yun Huang | en |
| dc.contributor.author | 黃子昀 | zh_TW |
| dc.date.accessioned | 2021-06-15T04:28:04Z | - |
| dc.date.available | 2009-08-21 | |
| dc.date.copyright | 2009-08-21 | |
| dc.date.issued | 2009 | |
| dc.date.submitted | 2009-08-20 | |
| dc.identifier.citation | 1. Echan, L. A.; Tang, H. Y.; Ali-Khan, N.; Lee, K.; Speicher, D. W., Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma. Proteomics 2005, 5, (13), 3292-303.
2. Rifai, N.; Gillette, M. A.; Carr, S. A., Protein biomarker discovery and validation: the long and uncertain path to clinical utility. Nat Biotechnol 2006, 24, (8), 971-83. 3. Hu, S.; Loo, J. A.; Wong, D. T., Human body fluid proteome analysis. Proteomics 2006, 6, (23), 6326-53. 4. Liu, T.; Qian, W. J.; Gritsenko, M. A.; Xiao, W.; Moldawer, L. L.; Kaushal, A.; Monroe, M. E.; Varnum, S. M.; Moore, R. J.; Purvine, S. O.; Maier, R. V.; Davis, R. W.; Tompkins, R. G.; Camp, D. G., 2nd; Smith, R. D., High dynamic range characterization of the trauma patient plasma proteome. Mol Cell Proteomics 2006, 5, (10), 1899-913. 5. Shores, K. S.; Udugamasooriya, D. G.; Kodadek, T.; Knapp, D. R., Use of peptide analogue diversity library beads for increased depth of proteomic analysis: application to cerebrospinal fluid. J Proteome Res 2008, 7, (5), 1922-31. 6. Thulasiraman, V.; Lin, S.; Gheorghiu, L.; Lathrop, J.; Lomas, L.; Hammond, D.; Boschetti, E., Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands. Electrophoresis 2005, 26, (18), 3561-71. 7. Guerrier, L.; Thulasiraman, V.; Castagna, A.; Fortis, F.; Lin, S.; Lomas, L.; Righetti, P. G.; Boschetti, E., Reducing protein concentration range of biological samples using solid-phase ligand libraries. J Chromatogr B Analyt Technol Biomed Life Sci 2006, 833, (1), 33-40. 8. Righetti, P. G.; Boschetti, E.; Lomas, L.; Citterio, A., Protein Equalizer Technology : the quest for a 'democratic proteome'. Proteomics 2006, 6, (14), 3980-92. 9. Boschetti, E.; Righetti, P. G., The art of observing rare protein species in proteomes with peptide ligand libraries. Proteomics 2009, 9, (6), 1492-510. 10. Anderson, N. L.; Anderson, N. G., The human plasma proteome: history, character, and diagnostic prospects. Mol Cell Proteomics 2002, 1, (11), 845-67. 11. Hortin, G. L.; Sviridov, D.; Anderson, N. L., High-abundance polypeptides of the human plasma proteome comprising the top 4 logs of polypeptide abundance. Clin Chem 2008, 54, (10), 1608-16. 12. Qian, W. J.; Kaleta, D. T.; Petritis, B. O.; Jiang, H.; Liu, T.; Zhang, X.; Mottaz, H. M.; Varnum, S. M.; Camp, D. G., 2nd; Huang, L.; Fang, X.; Zhang, W. W.; Smith, R. D., Enhanced detection of low abundance human plasma proteins using a tandem IgY12-SuperMix immunoaffinity separation strategy. Mol Cell Proteomics 2008, 7, (10), 1963-73. 13. Fortis, F.; Guerrier, L.; Righetti, P. G.; Antonioli, P.; Boschetti, E., A new approach for the removal of protein impurities from purified biologicals using combinatorial solid-phase ligand libraries. Electrophoresis 2006, 27, (15), 3018-27. 14. Fortis, F.; Guerrier, L.; Areces, L. B.; Antonioli, P.; Hayes, T.; Carrick, K.; Hammond, D.; Boschetti, E.; Righetti, P. G., A new approach for the detection and identification of protein impurities using combinatorial solid phase ligand libraries. J Proteome Res 2006, 5, (10), 2577-85. 15. Hoving, S.; Voshol, H.; van Oostrum, J., Towards high performance two-dimensional gel electrophoresis using ultrazoom gels. Electrophoresis 2000, 21, (13), 2617-21. 16. Westbrook, J. A.; Yan, J. X.; Wait, R.; Welson, S. Y.; Dunn, M. J., Zooming-in on the proteome: very narrow-range immobilised pH gradients reveal more protein species and isoforms. Electrophoresis 2001, 22, (14), 2865-71. 17. Guerrier, L.; Lomas, L.; Boschetti, E., A new general approach to purify proteins from complex mixtures. J Chromatogr A 2007, 1156, (1-2), 188-95. 18. Garcia-Martin, F.; Quintanar-Audelo, M.; Garcia-Ramos, Y.; Cruz, L. J.; Gravel, C.; Furic, R.; Cote, S.; Tulla-Puche, J.; Albericio, F., ChemMatrix, a poly(ethylene glycol)-based support for the solid-phase synthesis of complex peptides. J Comb Chem 2006, 8, (2), 213-20. 19. Homma, S.; Satoh, H.; Kagohashi, K.; Fujiwara, M.; Kamma, H.; Sekizawa, K., Production of CA125 by human lung cancer cell lines. Clin Exp Med 2004, 4, (3), 139-41. 20. Pollan, M.; Varela, G.; Torres, A.; de la Torre, M.; Ludena, M. D.; Ortega, M. D.; Pac, J.; Freixenet, J.; Gomez, G.; Sebastian, F.; Diez, M.; Arrabal, R.; Canalis, E.; Garcia-Tirado, J.; Arnedillo, A.; Rivas, J. J.; Minguella, J.; Gomez, A.; Garcia, M.; Aragones, N.; Perez-Gomez, B.; Lopez-Abente, G.; Gonzalez-Sarmiento, R.; Rojas, J. M., Clinical value of p53, c-erbB-2, CEA and CA125 regarding relapse, metastasis and death in resectable non-small cell lung cancer. Int J Cancer 2003, 107, (5), 781-90. 21. Ando, S.; Kimura, H.; Iwai, N.; Yamamoto, N.; Iida, T., Positive reactions for both Cyfra21-1 and CA125 indicate worst prognosis in non-small cell lung cancer. Anticancer Res 2003, 23, (3C), 2869-74. 22. Gaspar, M. J.; Diez, M.; Rodriguez, A.; Ratia, T.; Martin Duce, A.; Galvan, M.; Granell, J.; Coca, C., Clinical value of CEA and CA125 regarding relapse and metastasis in resectable non-small cell lung cancer. Anticancer Res 2003, 23, (4), 3427-32. 23. Hu, Y.; Zhong, A.; Yang, X., [Prognostic value of serum CA125 level in patients with advanced non-small cell lung cancer]. Zhonghua Zhong Liu Za Zhi 2000, 22, (1), 30-1. 24. Diez, M.; Pollan, M.; Maestro, M. L.; Ortega, M. D.; Gomez, A.; Sanchez-Pernaute, A.; Torres, A.; Granell, J.; Balibrea, J. L., Concordance between serum and cytosolic levels of CEA, CA125 and SCC antigens in patients with non-small cell lung cancer. Anticancer Res 1995, 15, (6B), 2811-7. 25. Diez, M.; Gomez, A.; Hernando, F.; Ortega, M. D.; Maestro, M. L.; Torres, A.; Muguerza, J. M.; Gutierrez, A.; Granell, J.; Balibrea, J. L., Serum CEA, CA125, and SCC antigens and tumor recurrence in resectable non-small cell lung cancer. Int J Biol Markers 1995, 10, (1), 5-10. 26. Kimura, Y.; Fujii, T.; Hamamoto, K.; Miyagawa, N.; Kataoka, M.; Iio, A., Serum CA125 level is a good prognostic indicator in lung cancer. Br J Cancer 1990, 62, (4), 676-8. 27. Clarke, M. R.; Landreneau, R. J.; Resnick, N. M.; Crowley, R.; Dougherty, G. J.; Cooper, D. L.; Yousem, S. A., Prognostic significance of CD44 expression in adenocarcinoma of the lung. Clin Mol Pathol 1995, 48, (4), M200-M204. 28. Jeon, J. H.; Kim, S. K.; Kim, H. J.; Chang, J.; Ahn, C. M.; Chang, Y. S., Insulin-like growth factor-1 attenuates cisplatin-induced gammaH2AX formation and DNA double-strand breaks repair pathway in non-small cell lung cancer. Cancer Lett 2008, 272, (2), 232-41. 29. Dziadziuszko, R.; Camidge, D. R.; Hirsch, F. R., The insulin-like growth factor pathway in lung cancer. J Thorac Oncol 2008, 3, (8), 815-8. 30. Velcheti, V.; Govindan, R., Insulin-like growth factor and lung cancer. J Thorac Oncol 2006, 1, (7), 607-10. 31. Yu, H.; Spitz, M. R.; Mistry, J.; Gu, J.; Hong, W. K.; Wu, X., Plasma levels of insulin-like growth factor-I and lung cancer risk: a case-control analysis. J Natl Cancer Inst 1999, 91, (2), 151-6. 32. Matsuda, Y.; Yamamoto, T.; Kudo, M.; Kawahara, K.; Kawamoto, M.; Nakajima, Y.; Koizumi, K.; Nakazawa, N.; Ishiwata, T.; Naito, Z., Expression and roles of lumican in lung adenocarcinoma and squamous cell carcinoma. Int J Oncol 2008, 33, (6), 1177-85. 33. Higashiyama, M.; Doi, O.; Yokouchi, H.; Kodama, K.; Nakamori, S.; Tateishi, R., Alpha-1-antichymotrypsin expression in lung adenocarcinoma and its possible association with tumor progression. Cancer 1995, 76, (8), 1368-76. 34. Gaffar, S. A.; Princler, G. L.; McIntire, K. R.; Braatz, J. A., A human lung tumor-associated antigen cross-reactive with alpha 1-antichymotrypsin. J Biol Chem 1980, 255, (17), 8334-9. 35. Faca, V.; Pitteri, S. J.; Newcomb, L.; Glukhova, V.; Phanstiel, D.; Krasnoselsky, A.; Zhang, Q.; Struthers, J.; Wang, H.; Eng, J.; Fitzgibbon, M.; McIntosh, M.; Hanash, S., Contribution of protein fractionation to depth of analysis of the serum and plasma proteomes. J Proteome Res 2007, 6, (9), 3558-65. 36. Pieper, R.; Gatlin, C. L.; Makusky, A. J.; Russo, P. S.; Schatz, C. R.; Miller, S. S.; Su, Q.; McGrath, A. M.; Estock, M. A.; Parmar, P. P.; Zhao, M.; Huang, S. T.; Zhou, J.; Wang, F.; Esquer-Blasco, R.; Anderson, N. L.; Taylor, J.; Steiner, S., The human serum proteome: display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins. Proteomics 2003, 3, (7), 1345-64. 37. Tyan, Y. C.; Wu, H. Y.; Su, W. C.; Chen, P. W.; Liao, P. C., Proteomic analysis of human pleural effusion. Proteomics 2005, 5, (4), 1062-74. 38. Tyan, Y. C.; Wu, H. Y.; Lai, W. W.; Su, W. C.; Liao, P. C., Proteomic profiling of human pleural effusion using two-dimensional nano liquid chromatography tandem mass spectrometry. J Proteome Res 2005, 4, (4), 1274-86. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/45574 | - |
| dc.description.abstract | 大部分生物抽取液(譬如：血清、胸腔液)的組成蛋白質濃度差距非常大，差距可以超過1010，也因為這非常巨大的濃度差距，那些已經被發現而且研究的非常透徹的幾個主要組成蛋白質，會遮蔽在生物抽取液中其他濃度非常低的蛋白質，使得低濃度蛋白質不容易被偵測到，因此這些低濃度蛋白質的偵測和分離是現階段蛋白質體學中一個有待克服的障礙。近年來，一些用來減少生物抽取液中各蛋白質濃度差距的方法被發展出來，在此，我們利用aminomethyl-chemmatrix微珠，因為此微珠具有兩性端(疏水端及親水端)可以去抓取蛋白質，期望可以達到平衡胸腔液樣品中各蛋白質濃度差距。我們分析處理過後的胸腔液樣品，發現那些低濃度蛋白質比較容易被二維電泳偵測到，我們接著用此方式去處理正常人的胸腔液和癌症病人的胸腔液，那些在病人和正常人中表現有差異的低濃度蛋白質較容易用二維電泳區分，而在這些有表現差異的低濃度蛋白質中，我們希望能找到屬於癌症病人的生物標記。 | zh_TW |
| dc.description.abstract | Most of biological extracts (e.g., serum, pleural effusion) have an extremely wide dynamic concentration range of over ten orders of magnitude, so a few well-characterized, high-abundant proteins mask the signal of other low abundance proteins. The separation and detection of low abundant proteins in the proteome is still an obstacle to be solved. Many methods which can make the “hidden proteome” become easier to research are developed in recently. We report here the use of amiomethyl-chemmatrix beads to reduce the dynamic concentration range in pleural effusion (PE). The amiomethyl-chemmatrix beads have the amphiphilic nature to equalize the concentration of different protein species. After treatment with the bead, the low abundance proteins in PE are easier to detect by 2-DE PAGE. The differences in the treated PE from normal person and lung cancer person are easier determined by 2-DE PAGE and we expect that the cancer biomarkers will be discovered among the different proteomes between these two treated PE. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T04:28:04Z (GMT). No. of bitstreams: 1 ntu-98-R96b46005-1.pdf: 4878292 bytes, checksum: 62294385dbdc971c0114f71dec25a149 (MD5) Previous issue date: 2009 | en |
| dc.description.tableofcontents | 1. Introduction…………………………………………………………………………8
2. Materials and methods……………………………………………………...……15 2.1. Materials……………………………………………………………….…….15 2.2. Methods…………………………….………………………….……………..16 2.2.1. Protein equalization by using Aminomethyl-ChemMatrix bead…....…16 2.2.2. Desalting of the eluant………………………..………………………16 2.2.3. Two-dimensional electrophoresis……………………………..……….17 2.2.4. In-gel digestion………………………………………………………...18 2.2.5. In-solution digestion…………………………………………………...19 2.2.6. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) ………………………………………...………………...20 3. Results……………………………………………………………………………..21 3.1. The dynamic range of protein concentration in PE were decreasing after equalization technology……………………………………………………....21 3.2. The optimal loading capacity of this bead ……………………………..…......22 3.3. Application of this method to PE from normal person and lung cancer patient and compared the differences between PE…………………………………...22 3.4. Protein identification by LC MS/MS…………………………..……………..23 4. Discussion…………………………………………………………………………25 5. Conclusion…………………………………………………………………………27 6. References…………………….…….……………………………………………..28 7. Figures…………………………………………………………………………..…35 8. Tables………………………………………………………………………………42 | |
| dc.language.iso | en | |
| dc.title | 利用Aminomethyl-chemmatrix微珠達成蛋白質體中各蛋白質量的均等化 | zh_TW |
| dc.title | Using the aminomethyl-chemmatrix beads to achieve the purpose of protein equalization | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 97-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 曾銘仁(Min - Jen Tseng),施子弼(Daniel Tzi-Bi Shih),吳世雄(Shih-Hsiung Wu),羅禮強(Lo, Lee-Chiang) | |
| dc.subject.keyword | aminomethyl-chemmatrix微珠,蛋白質的均等化, | zh_TW |
| dc.subject.keyword | aminomethyl-chemmatrix bead,protein equalization, | en |
| dc.relation.page | 44 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2009-08-20 | |
| 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 | |
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