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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 李明學(Ming-Shyue Lee) | |
| dc.contributor.author | Ya-Yun Lin | en |
| dc.contributor.author | 林雅筠 | zh_TW |
| dc.date.accessioned | 2021-06-15T05:19:12Z | - |
| dc.date.available | 2010-09-09 | |
| dc.date.copyright | 2010-09-09 | |
| dc.date.issued | 2010 | |
| dc.date.submitted | 2010-07-20 | |
| dc.identifier.citation | 1. Jemal, A., Thun, M. J., Ries, L. A., Howe, H. L., Weir, H. K., Center, M. M., Ward, E., Wu, X. C., Eheman, C., Anderson, R., Ajani, U. A., Kohler, B., and Edwards, B. K. (2008) J Natl Cancer Inst 100, 1672-1694
2. 中華民國行政院衛生署. (2010) 3. Denis, L. J., and Griffiths, K. (2000) Semin Surg Oncol 18, 52-74 4. Denmeade, S. R., and Isaacs, J. T. (2002) Nat Rev Cancer 2, 389-396 5. Feldman, B. J., and Feldman, D. (2001) Nat Rev Cancer 1, 34-45 6. Kiuchi, F., Goto, Y., Sugimoto, N., Akao, N., Kondo, K., and Tsuda, Y. (1993) Chem Pharm Bull (Tokyo) 41, 1640-1643 7. Aggarwal, B. B., Kumar, A., and Bharti, A. C. (2003) Anticancer Res 23, 363-398 8. Shen, L., and Ji, H. F. (2007) Spectrochim Acta A Mol Biomol Spectrosc 67, 619-623 9. Tonnesen, H. H., and Karlsen, J. (1985) Z Lebensm Unters Forsch 180, 402-404 10. Wang, Y. J., Pan, M. H., Cheng, A. L., Lin, L. I., Ho, Y. S., Hsieh, C. Y., and Lin, J. K. (1997) J Pharm Biomed Anal 15, 1867-1876 11. Eigner, D., and Scholz, D. (1999) J Ethnopharmacol 67, 1-6 12. Ammon, H. P., and Wahl, M. A. (1991) Planta Med 57, 1-7 13. Grant, K. L., and Schneider, C. D. (2000) Am J Health Syst Pharm 57, 1121-1122 14. Sreejayan, and Rao, M. N. (1997) J Pharm Pharmacol 49, 105-107 15. Huang, M. T., Lysz, T., Ferraro, T., Abidi, T. F., Laskin, J. D., and Conney, A. H. (1991) Cancer Res 51, 813-819 16. Menon, V. P., and Sudheer, A. R. (2007) Adv Exp Med Biol 595, 105-125 17. Bhandarkar, S. S., and Arbiser, J. L. (2007) Adv Exp Med Biol 595, 185-195 18. Lopez-Lazaro, M. (2008) Mol Nutr Food Res 52 Suppl 1, S103-127 19. Kunnumakkara, A. B., Anand, P., and Aggarwal, B. B. (2008) Cancer Lett 269, 199-225 20. Karin, M. (2006) Nature 441, 431-436 21. Kang, G., Kong, P. J., Yuh, Y. J., Lim, S. Y., Yim, S. V., Chun, W., and Kim, S. S. (2004) J Pharmacol Sci 94, 325-328 22. Bachmeier, B. E., Mohrenz, I. V., Mirisola, V., Schleicher, E., Romeo, F., Hohneke, C., Jochum, M., Nerlich, A. G., and Pfeffer, U. (2008) Carcinogenesis 29, 779-789 23. Tsui, K. H., Feng, T. H., Lin, C. M., Chang, P. L., and Juang, H. H. (2008) J Androl 29, 661-668 24. Gururaj, A. E., Belakavadi, M., Venkatesh, D. A., Marme, D., and Salimath, B. P. (2002) Biochem Biophys Res Commun 297, 934-942 25. Lin, L. I., Ke, Y. F., Ko, Y. C., and Lin, J. K. (1998) Oncology 55, 349-353 26. Yodkeeree, S., Chaiwangyen, W., Garbisa, S., and Limtrakul, P. (2009) J Nutr Biochem 20, 87-95 27. Raffo, A. J., Perlman, H., Chen, M. W., Day, M. L., Streitman, J. S., and Buttyan, R. (1995) Cancer Res 55, 4438-4445 28. Craft, N., Chhor, C., Tran, C., Belldegrun, A., DeKernion, J., Witte, O. N., Said, J., Reiter, R. E., and Sawyers, C. L. (1999) Cancer Res 59, 5030-5036 29. Shah, R. B., Ghosh, D., and Elder, J. T. (2006) Prostate 66, 1437-1444 30. Wang, X., Jones, T. D., Zhang, S., Eble, J. N., Bostwick, D. G., Qian, J., Lopez-Beltran, A., Montironi, R., Harris, J. J., and Cheng, L. (2007) Mod Pathol 20, 175-182 31. Fu, M., Wang, C., Li, Z., Sakamaki, T., and Pestell, R. G. (2004) Endocrinology 145, 5439-5447 32. Liu, X. H., Yao, S., Kirschenbaum, A., and Levine, A. C. (1998) Cancer Res 58, 4245-4249 33. Nakamura, K., Yasunaga, Y., Segawa, T., Ko, D., Moul, J. W., Srivastava, S., and Rhim, J. S. (2002) Int J Oncol 21, 825-830 34. Mukhopadhyay, A., Banerjee, S., Stafford, L. J., Xia, C., Liu, M., and Aggarwal, B. B. (2002) Oncogene 21, 8852-8861 35. Shi, Q., Shih, C. C., and Lee, K. H. (2009) Anticancer Agents Med Chem 9, 904-912 36. Hong, J. H., Ahn, K. S., Bae, E., Jeon, S. S., and Choi, H. Y. (2006) Prostate Cancer Prostatic Dis 9, 147-152 37. Shankar, T. N., Shantha, N. V., Ramesh, H. P., Murthy, I. A., and Murthy, V. S. (1980) Indian J Exp Biol 18, 73-75 38. Vareed, S. K., Kakarala, M., Ruffin, M. T., Crowell, J. A., Normolle, D. P., Djuric, Z., and Brenner, D. E. (2008) Cancer Epidemiol Biomarkers Prev 17, 1411-1417 39. Teiten, M. H., Gaascht, F., Eifes, S., Dicato, M., and Diederich, M. (2009) Genes Nutr 5, 61-74 40. Parkin, D. M., Bray, F., Ferlay, J., and Pisani, P. (2005) CA Cancer J Clin 55, 74-108 41. Cheng, A. L., Hsu, C. H., Lin, J. K., Hsu, M. M., Ho, Y. F., Shen, T. S., Ko, J. Y., Lin, J. T., Lin, B. R., Ming-Shiang, W., Yu, H. S., Jee, S. H., Chen, G. S., Chen, T. M., Chen, C. A., Lai, M. K., Pu, Y. S., Pan, M. H., Wang, Y. J., Tsai, C. C., and Hsieh, C. Y. (2001) Anticancer Res 21, 2895-2900 42. Li, L., Aggarwal, B. B., Shishodia, S., Abbruzzese, J., and Kurzrock, R. (2004) Cancer 101, 2351-2362 43. Dhillon, N., Aggarwal, B. B., Newman, R. A., Wolff, R. A., Kunnumakkara, A. B., Abbruzzese, J. L., Ng, C. S., Badmaev, V., and Kurzrock, R. (2008) Clin Cancer Res 14, 4491-4499 44. Garcea, G., Berry, D. P., Jones, D. J., Singh, R., Dennison, A. R., Farmer, P. B., Sharma, R. A., Steward, W. P., and Gescher, A. J. (2005) Cancer Epidemiol Biomarkers Prev 14, 120-125 45. Garcea, G., Jones, D. J., Singh, R., Dennison, A. R., Farmer, P. B., Sharma, R. A., Steward, W. P., Gescher, A. J., and Berry, D. P. (2004) Br J Cancer 90, 1011-1015 46. Anand, P., Kunnumakkara, A. B., Newman, R. A., and Aggarwal, B. B. (2007) Mol Pharm 4, 807-818 47. Shaikh, J., Ankola, D. D., Beniwal, V., Singh, D., and Kumar, M. N. (2009) Eur J Pharm Sci 37, 223-230 48. Cho, E. G., Kim, M. G., Kim, C., Kim, S. R., Seong, I. S., Chung, C., Schwartz, R. H., and Park, D. (2001) J Biol Chem 276, 44581-44589 49. Tanimoto, H., Underwood, L. J., Wang, Y., Shigemasa, K., Parmley, T. H., and O'Brien, T. J. (2001) Tumour Biol 22, 104-114 50. Tanimoto, H., Shigemasa, K., Tian, X., Gu, L., Beard, J. B., Sawasaki, T., and O'Brien, T. J. (2005) Br J Cancer 92, 278-283 51. Lin, C. Y., Anders, J., Johnson, M., and Dickson, R. B. (1999) J Biol Chem 274, 18237-18242 52. Lin, C. Y., Anders, J., Johnson, M., Sang, Q. A., and Dickson, R. B. (1999) J Biol Chem 274, 18231-18236 53. Shi, Y. E., Torri, J., Yieh, L., Wellstein, A., Lippman, M. E., and Dickson, R. B. (1993) Cancer Res 53, 1409-1415 54. Lin, C. Y., Wang, J. K., Torri, J., Dou, L., Sang, Q. A., and Dickson, R. B. (1997) J Biol Chem 272, 9147-9152 55. MS, L. (2006) Journal of Cancer Molecules 2, 183-190 56. Takeuchi, T., Harris, J. L., Huang, W., Yan, K. W., Coughlin, S. R., and Craik, C. S. (2000) J Biol Chem 275, 26333-26342 57. Oberst, M. D., Williams, C. A., Dickson, R. B., Johnson, M. D., and Lin, C. Y. (2003) J Biol Chem 278, 26773-26779 58. Kojima, K., Tsuzuki, S., Fushiki, T., and Inouye, K. (2009) J Biochem 145, 783-790 59. Friedrich, R., Fuentes-Prior, P., Ong, E., Coombs, G., Hunter, M., Oehler, R., Pierson, D., Gonzalez, R., Huber, R., Bode, W., and Madison, E. L. (2002) J Biol Chem 277, 2160-2168 60. Miyake, Y., Yasumoto, M., Tsuzuki, S., Fushiki, T., and Inouye, K. (2009) J Biochem 146, 273-282 61. Cho, E. G., Schwartz, R. H., and Kim, M. G. (2005) Biochem Biophys Res Commun 327, 328-334 62. Kim C, C. Y., Kang CH, Kim MG, Lee H, Cho EG, Park D. (2005) EMBO Rep. 6, 1045-1051 63. Oberst, M. D., Chen, L. Y., Kiyomiya, K., Williams, C. A., Lee, M. S., Johnson, M. D., Dickson, R. B., and Lin, C. Y. (2005) Am J Physiol Cell Physiol 289, C462-470 64. Benaud, C., Dickson, R. B., and Lin, C. Y. (2001) Eur J Biochem 268, 1439-1447 65. Kiyomiya, K., Lee, M. S., Tseng, I. C., Zuo, H., Barndt, R. J., Johnson, M. D., Dickson, R. B., and Lin, C. Y. (2006) Am J Physiol Cell Physiol 291, C40-49 66. List, K., Szabo, R., Molinolo, A., Nielsen, B. S., and Bugge, T. H. (2006) Am J Pathol 168, 1513-1525 67. Oberst, M. D., Singh, B., Ozdemirli, M., Dickson, R. B., Johnson, M. D., and Lin, C. Y. (2003) J Histochem Cytochem 51, 1017-1025 68. List, K., Haudenschild, C. C., Szabo, R., Chen, W., Wahl, S. M., Swaim, W., Engelholm, L. H., Behrendt, N., and Bugge, T. H. (2002) Oncogene 21, 3765-3779 69. Satomi, S., Yamasaki, Y., Tsuzuki, S., Hitomi, Y., Iwanaga, T., and Fushiki, T. (2001) Biochem Biophys Res Commun 287, 995-1002 70. Netzel-Arnett, S., Currie, B. M., Szabo, R., Lin, C. Y., Chen, L. M., Chai, K. X., Antalis, T. M., Bugge, T. H., and List, K. (2006) J Biol Chem 281, 32941-32945 71. List, K., Kosa, P., Szabo, R., Bey, A. L., Wang, C. B., Molinolo, A., and Bugge, T. H. (2009) Am J Pathol 175, 1453-1463 72. List, K., Szabo, R., Wertz, P. W., Segre, J., Haudenschild, C. C., Kim, S. Y., and Bugge, T. H. (2003) J Cell Biol 163, 901-910 73. Forbs, D., Thiel, S., Stella, M. C., Sturzebecher, A., Schweinitz, A., Steinmetzer, T., Sturzebecher, J., and Uhland, K. (2005) Int J Oncol 27, 1061-1070 74. Riddick, A. C., Shukla, C. J., Pennington, C. J., Bass, R., Nuttall, R. K., Hogan, A., Sethia, K. K., Ellis, V., Collins, A. T., Maitland, N. J., Ball, R. Y., and Edwards, D. R. (2005) Br J Cancer 92, 2171-2180 75. Kang, J. Y., Dolled-Filhart, M., Ocal, I. T., Singh, B., Lin, C. Y., Dickson, R. B., Rimm, D. L., and Camp, R. L. (2003) Cancer Res 63, 1101-1105 76. Zeng, L., Cao, J., and Zhang, X. (2005) World J Gastroenterol 11, 6202-6207 77. Santin, A. D., Zhan, F., Bellone, S., Palmieri, M., Cane, S., Bignotti, E., Anfossi, S., Gokden, M., Dunn, D., Roman, J. J., O'Brien, T. J., Tian, E., Cannon, M. J., Shaughnessy, J., Jr., and Pecorelli, S. (2004) Int J Cancer 112, 14-25 78. Jin, J. S., Chen, A., Hsieh, D. S., Yao, C. W., Cheng, M. F., and Lin, Y. F. (2006) Int J Surg Pathol 14, 65-72 79. Saleem, M., Adhami, V. M., Zhong, W., Longley, B. J., Lin, C. Y., Dickson, R. B., Reagan-Shaw, S., Jarrard, D. F., and Mukhtar, H. (2006) Cancer Epidemiol Biomarkers Prev 15, 217-227 80. Ding, K. F., Sun, L. F., Ge, W. T., Hu, H. G., Zhang, S. Z., and Zheng, S. (2005) World J Gastroenterol 11, 5651-5654 81. Uhland, K. (2006) Cell Mol Life Sci 63, 2968-2978 82. Lee, S. L., Dickson, R. B., and Lin, C. Y. (2000) J Biol Chem 275, 36720-36725 83. List, K., Szabo, R., Molinolo, A., Sriuranpong, V., Redeye, V., Murdock, T., Burke, B., Nielsen, B. S., Gutkind, J. S., and Bugge, T. H. (2005) Genes Dev 19, 1934-1950 84. Shimomura, T., Denda, K., Kitamura, A., Kawaguchi, T., Kito, M., Kondo, J., Kagaya, S., Qin, L., Takata, H., Miyazawa, K., and Kitamura, N. (1997) J Biol Chem 272, 6370-6376 85. Oberst, M. D., Johnson, M. D., Dickson, R. B., Lin, C. Y., Singh, B., Stewart, M., Williams, A., al-Nafussi, A., Smyth, J. F., Gabra, H., and Sellar, G. C. (2002) Clin Cancer Res 8, 1101-1107 86. Kaighn, M. E., Narayan, K. S., Ohnuki, Y., Lechner, J. F., and Jones, L. W. (1979) Invest Urol 17, 16-23 87. Cao, J., Liu, Y., Jia, L., Zhou, H. M., Kong, Y., Yang, G., Jiang, L. P., Li, Q. J., and Zhong, L. F. (2007) Free Radic Biol Med 43, 968-975 88. Lokeshwar, B. L. (1999) Ann N Y Acad Sci 878, 271-289 89. Miyake, H., Hara, I., Yamanaka, K., Gohji, K., Arakawa, S., and Kamidono, S. (1999) Prostate 39, 123-129 90. Benaud, C., Oberst, M., Hobson, J. P., Spiegel, S., Dickson, R. B., and Lin, C. Y. (2002) J Biol Chem 277, 10539-10546 91. Thiery, J. P. (2002) Nat Rev Cancer 2, 442-454 92. Carles, J., Lloreta, J., Salido, M., Font, A., Suarez, M., Baena, V., Nogue, M., Domenech, M., and Fabregat, X. (2004) Clin Cancer Res 10, 4742-4745 93. Osman, I., Scher, H. I., Drobnjak, M., Verbel, D., Morris, M., Agus, D., Ross, J. S., and Cordon-Cardo, C. (2001) Clin Cancer Res 7, 2643-2647 94. Engelsen, I. B., Stefansson, I. M., Beroukhim, R., Sellers, W. R., Meyerson, M., Akslen, L. A., and Salvesen, H. B. (2008) Int J Oncol 32, 307-316 95. Morin, D., Barthelemy, S., Zini, R., Labidalle, S., and Tillement, J. P. (2001) FEBS Lett 495, 131-136 96. Tarin, D. (1985) Biochim Biophys Acta 780, 227-235 97. Duffy, M. J., McGowan, P. M., and Gallagher, W. M. (2008) J Pathol 214, 283-293 98. Masterson, J., and O'Dea, S. (2007) Cells Tissues Organs 185, 175-179 99. Chambers, A. F., and Matrisian, L. M. (1997) J Natl Cancer Inst 89, 1260-1270 100. Kalluri, R. (2003) Nat Rev Cancer 3, 422-433 101. Fingleton, B. (2006) Front Biosci 11, 479-491 102. Egeblad, M., and Werb, Z. (2002) Nat Rev Cancer 2, 161-174 103. Sternlicht, M. D., and Werb, Z. (2001) Annu Rev Cell Dev Biol 17, 463-516 104. Andreasen, P. A., Egelund, R., and Petersen, H. H. (2000) Cell Mol Life Sci 57, 25-40 105. Mazar, A. P., Henkin, J., and Goldfarb, R. H. (1999) Angiogenesis 3, 15-32 106. Liotta, L. A., Goldfarb, R. H., Brundage, R., Siegal, G. P., Terranova, V., and Garbisa, S. (1981) Cancer Res 41, 4629-4636 107. Odekon, L. E., Blasi, F., and Rifkin, D. B. (1994) J Cell Physiol 158, 398-407 108. Park, J. E., Keller, G. A., and Ferrara, N. (1993) Mol Biol Cell 4, 1317-1326 109. Mazzieri, R., Masiero, L., Zanetta, L., Monea, S., Onisto, M., Garbisa, S., and Mignatti, P. (1997) EMBO J 16, 2319-2332 110. Murphy, G., Ward, R., Gavrilovic, J., and Atkinson, S. (1992) Matrix Suppl 1, 224-230 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/46620 | - |
| dc.description.abstract | 攝護腺癌的癌症致死率在西方男性世界中排名第二位；在台灣，攝護腺癌的發生率以及死亡率亦有逐年提升的現象。攝護腺癌的高致死率主要是由於癌症的病程發展到癌細胞具有較高移動、侵襲和轉移能力或變成雄激素非依賴型的徵狀。薑黃素 (Curcumin) 是由中草藥和薑黃萃取出來的多酚類物質，近年研究指出薑黃素具有抗氧化、抗發炎、抗癌以及預防癌症產生 (chemoprevention) 的能力，然而，薑黃素是如何抑制攝護腺癌細胞侵襲的分子機制尚未清楚了解。在本篇研究裡，我檢測了薑黃素對於攝護腺癌細胞 (PC-3) 的生長、移動與侵襲的影響。實驗結果指出薑黃素可有效地抑制攝護腺癌細胞的生長、移動與侵襲的能力。為了更進一步研究薑黃素抑制攝護腺癌細胞移動與侵襲的分子機制，我檢測了薑黃素對於間質蛋白酶 (Matriptase) 的影響。間質蛋白酶是第二型嵌膜絲胺酸蛋白酶，近年來研究指出不正常活化的間質蛋白酶可能參與了許多癌症的演進，包括攝護腺癌。而實驗結果指出，薑黃素可以降低間質蛋白酶的表現量及活化，但不影響其基因的表現。此外，薑黃素可以促進已活化的間質蛋白酶釋出到細胞外。更進一步地，我們建立了攝護腺癌細胞侵襲能力進化的細胞模式 (PC-3 以及M2I1 PC-3 cells)，並檢驗了薑黃素對此 PC-3 侵襲細胞模式的侵襲能力之影響。 M2I1 細胞比起 PC-3 細胞具有大約多達一倍的侵襲能力。而薑黃素可抑制M2I1細胞侵襲能力，其原因可能是藉由抑制了活化的間質蛋白酶，而非透過影響上皮-間質轉化 (Epithelial-mesenchymal transitions) 的過程。此外，我也檢驗了薑黃素對於過量表達間質蛋白酶的細胞其侵襲能力的影響，透過建立大量穩定表現間質蛋白酶的 CWR22Rv1 細胞，發現大量表現間質蛋白酶的CWR22Rv1細胞可提升高達一倍的侵襲能力。而薑黃素亦可抑制這些大量表現間質蛋白酶的 CWR22Rv1 細胞之侵襲能力，且抑制的現象隨著薑黃素的濃度上升而增加。此外，實驗結果也顯示出薑黃素可以抑制因表皮生長因子 (EGF和Heregulin) 所刺激而增加的PC-3 細胞侵襲能力。整體來說，實驗結果指出薑黃素具有抑制間質蛋白酶功能而達到壓抑攝護腺癌細胞侵襲的能力。 | zh_TW |
| dc.description.abstract | Prostate cancer is the second leading cause of cancer-related death in men of the western world. In Taiwan, the incidence and mortality of prostate cancer have been rising progressively in recent years. The high mortality of prostate cancer is mainly due to the cancer progression to an androgen-independent state and/or high cancer cell migration, invasion and metastasis. Curcumin, a polyphenol substance derived from the herbal remedy and dietary spice turmeric, has been shown with potent antioxidant, anti-inflammatory, anti-carcinogenic, and chemopreventive effects. However, the molecular mechanism how curcumin suppresses prostate cancer cell invasion is not well understood. In this study, I examined the effect of natural compound curcumin on cell proliferation, migration and invasion in human prostate cancer PC3 cells. The results showed that curcumin could significantly suppress prostate cancer cell proliferation, migration and invasion. To further investigate the molecular mechanism in which curcumin was able to inhibit prostate cancer cell migration and invasion, I examined the effect of curcumin on a tumor-promoting, membrane-anchored serine protease, matriptase, since recent studies have shown that dysregulation of matriptase activation can promote the progression of many cancers including prostate cancer. The data showed that curcumin was able to reduce the activated levels with no effect on its gene expression of matriptase. Moreover, the reduction of activated matriptase by curcumin was partly due to the curcumin promoting the shedding of activated matriptase into extracellular environment. Furthermore, we established a PC-3 cell invasion progression model (parental and M2I1 PC-3 cells) with an increasing cell invasion capability and examined the effect of curcumin on different PC-3 cell invasion. The invasive ability of M2I1 cells was enhanced by approximate one fold, compared to the parental PC-3 cells. Curcumin-decreased M2I1 cell invasion was partly due to suppressing the level of activated matriptase but not via altering EMT process. I also examined the effect of curcumin on the cell invasion of those cells with matriptase overexpresion. I established the stable pools of CWR22Rv1 cells with matriptase overexpression and found that expression of matriptase in CWR22Rv1 cells enhanced their invasive ability approximately one fold. With curcumin treatment, the invasive ability induced by matriptase overexpression was suppressed in a dose-dependent manner. In addition, our data also showed that curcumin was able to suppress EGF- or heregulin-stimulated PC-3 cell invasion. In summary, the data indicated that curcumin exhibits a suppressive effect on prostate cancer cell invasion, at least in part by down-regulating matriptase function. | en |
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| dc.description.tableofcontents | 致謝 i
中文摘要 iii Abstract iv Chapter 1. Introduction 1 1.1 Prostate cancer 2 1.2 Curcumin 2 1.3 Matriptase 8 1.4 Research motivation 15 Chapter 2. Materials and methods 16 2.1 Materials 17 2.2 Methods 21 2.3 Buffer 30 Chapter 3. Results 32 3.1 Effect of curcumin on the cytotoxicity of PC-3 cells 33 3.2 Growth-inhibitory effects of curcumin on PC-3 cell viability and proliferation. 33 3.3 Curcumin inhibited the motility and invasion of PC-3 cells. 35 3.4 Curcumin-decreased PC-3 cell invasion potentially via inhibiting serine protease(s). 36 3.5 Curcumin decreased MMPs activity in PC-3 cells. 37 3.6 Curcumin reduced protein levels of matriptase and HAI-1 but with no effects on its gene expression in PC-3 cells. 37 3.7 Curcumin promoted matriptase shedding in PC-3 cells. 38 3.8 Involvement of MMPs and serine protease in the shedding of matriptase 40 3.9 Inhibitory effects of curcumin on the cell invasion of different PC-3 cells. 41 3.10 Inhibitory effect of curcumin on matriptase-overexpressing CWR22Rv1 cell invasion. 43 3.11 Inhibitory effect of curcumin on ErbB signaling induced cell invasion. 44 Chapter 4. Discussion 45 Chapter 5. Figures 51 Figure 1. Effect of curcumin on the cytotoxicity of PC-3 cells. 52 Figure 2. Analysis of curcumin effect on PC-3 cell viability and proliferation. 53 Figure 4. Analysis of broad MMPs inhibitor (GM6001), serine protease inhibitor (AEBSF) and curcumin effects on PC-3 cell invasion. 57 Figure 6. Effect of curcumin on protein and gene expression of matriptase and HAI-1 in PC-3 cells. 59 Figure 7. Effect of curcumin on matriptase shedding in PC-3 cells. 63 Chapter 6. References 75 | |
| dc.language.iso | en | |
| dc.title | 探討薑黃素在攝護腺癌細胞移動、侵襲以及間質蛋白酶活化的影響 | zh_TW |
| dc.title | Suppression of prostate cancer cell migration and invasion by curcumin through down-regulating matriptase activity | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 98-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 呂紹俊(Shao-Chun Lu),張智芬(Zee-Fen Chang),楊家榮(Chia-Ron Yang),王正康(Jehng-Kang Wang) | |
| dc.subject.keyword | 薑黃素,攝護腺癌,侵襲,間質蛋白酶, | zh_TW |
| dc.subject.keyword | curcumin,prostate cancer,invasion,matriptase, | en |
| dc.relation.page | 81 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2010-07-21 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 生物化學暨分子生物學研究所 | zh_TW |
| 顯示於系所單位： | 生物化學暨分子生物學科研究所 | |
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