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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 吳漢忠(Han-Chung Wu) | |
dc.contributor.author | Kuo-Hua Tung | en |
dc.contributor.author | 董國華 | zh_TW |
dc.date.accessioned | 2021-06-07T17:49:44Z | - |
dc.date.copyright | 2013-03-04 | |
dc.date.issued | 2013 | |
dc.date.submitted | 2013-01-29 | |
dc.identifier.citation | Adams, G.P., Schier, R., Marshall, K., Wolf, E.J., McCall, A.M., Marks, J.D., and Weiner, L.M. (1998). Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies. Cancer Res. 58, 485-490.
Adams, G.P., and Weiner, L.M. (2005). Monoclonal antibody therapy of cancer. Nat. Biotechnol. 23, 1147-1157. Argani, P., Lui, M.Y., Couturier, J., Bouvier, R., Fournet, J.C., and Ladanyi, M. (2003). A novel CLTC-TFE3 gene fusion in pediatric renal adenocarcinoma with t(X;17)(p11.2;q23). Oncogene 22, 5374-5378. Bao, B., Ali, S., Ahmad, A., Azmi, A.S., Li, Y., Banerjee, S., Kong, D., Sethi, S., Aboukameel, A., Padhye, S.B., et al. (2012). Hypoxia-Induced Aggressiveness of Pancreatic Cancer Cells Is Due to Increased Expression of VEGF, IL-6 and miR-21, Which Can Be Attenuated by CDF Treatment. PLoS One 7, e50165. Bardeesy, N., and DePinho, R.A. (2002). Pancreatic cancer biology and genetics. Nat. Rev. Cancer 2, 897-909. Beattie, E.C., Howe, C.L., Wilde, A., Brodsky, F.M., and Mobley, W.C. (2000). NGF signals through TrkA to increase clathrin at the plasma membrane and enhance clathrin-mediated membrane trafficking. J. Neurosci. 20, 7325-7333. Blixt, M.K., and Royle, S.J. (2011). Clathrin heavy chain gene fusions expressed in human cancers: analysis of cellular functions. Traffic 12, 754-761. Bonazzi, M., Spano, S., Turacchio, G., Cericola, C., Valente, C., Colanzi, A., Kweon, H.S., Hsu, V.W., Polishchuck, E.V., Polishchuck, R.S., et al. (2005). CtBP3/BARS drives membrane fission in dynamin-independent transport pathways. Nat. Cell Biol. 7, 570-580. Bonner, J.A., Harari, P.M., Giralt, J., Azarnia, N., Shin, D.M., Cohen, R.B., Jones, C.U., Sur, R., Raben, D., Jassem, J., et al. (2006). Radiotherapy plus cetuximab for squamous-cell carcinoma of the head and neck. N. Engl. J. Med. 354, 567-578. Brodsky, F.M. (2012). Diversity of clathrin function: new tricks for an old protein. Annu. Rev. Cell Dev. Biol. 28, 309-336. Burgos, L., and Burgos, M.E. (2004). [Pancreatic neuroendocrine tumors]. Rev. Med. Chil. 132, 627-634. Burns, W.R., and Edil, B.H. (2012). Neuroendocrine pancreatic tumors: guidelines for management and update. Curr. Treat. Options Oncol. 13, 24-34. Burris, H.A., 3rd, Moore, M.J., Andersen, J., Green, M.R., Rothenberg, M.L., Modiano, M.R., Cripps, M.C., Portenoy, R.K., Storniolo, A.M., Tarassoff, P., et al. (1997). Improvements in survival and clinical benefit with gemcitabine as first-line therapy for patients with advanced pancreas cancer: a randomized trial. J. Clin. Oncol. 15, 2403-2413. Burstein, H.J., Harris, L.N., Marcom, P.K., Lambert-Falls, R., Havlin, K., Overmoyer, B., Friedlander, R.J., Jr., Gargiulo, J., Strenger, R., Vogel, C.L., et al. (2003). Trastuzumab and vinorelbine as first-line therapy for HER2-overexpressing metastatic breast cancer: multicenter phase II trial with clinical outcomes, analysis of serum tumor markers as predictive factors, and cardiac surveillance algorithm. J. Clin. Oncol. 21, 2889-2895. Carter, P. (2001). Improving the efficacy of antibody-based cancer therapies. Nat. Rev. Cancer 1, 118-129. Cascinu, S., Berardi, R., Labianca, R., Siena, S., Falcone, A., Aitini, E., Barni, S., Di Costanzo, F., Dapretto, E., Tonini, G., et al. (2008). Cetuximab plus gemcitabine and cisplatin compared with gemcitabine and cisplatin alone in patients with advanced pancreatic cancer: a randomised, multicentre, phase II trial. Lancet Oncol. 9, 39-44. Chang, D.K., Chiu, C.Y., Kuo, S.Y., Lin, W.C., Lo, A., Wang, Y.P., Li, P.C., and Wu, H.C. (2009). Antiangiogenic targeting liposomes increase therapeutic efficacy for solid tumors. J. Biol. Chem. 284, 12905-12916. Chang, Q., Jurisica, I., Do, T., and Hedley, D.W. (2011). Hypoxia predicts aggressive growth and spontaneous metastasis formation from orthotopically grown primary xenografts of human pancreatic cancer. Cancer Res. 71, 3110-3120. Chu, Y.W., Yang, P.C., Yang, S.C., Shyu, Y.C., Hendrix, M.J., Wu, R., and Wu, C.W. (1997). Selection of invasive and metastatic subpopulations from a human lung adenocarcinoma cell line. Am. J. Respir. Cell Mol. Biol. 17, 353-360. Cinar, P., and Tempero, M.A. (2012). Monoclonal antibodies and other targeted therapies for pancreatic cancer. Cancer J. 18, 653-664. Duffy, J.P., and Reber, H.A. (2003). Pancreatic neoplasms. Curr. Opin. Gastroenterol. 19, 458-466. Conner, S.D., and Schmid, S.L. (2003). Regulated portals of entry into the cell. Nature 422, 37-44. Costello, E., Greenhalf, W., and Neoptolemos, J.P. (2012). New biomarkers and targets in pancreatic cancer and their application to treatment. Nat. Rev. Gastroenterol. Hepatol. 9, 435-444. Cunningham, D., Humblet, Y., Siena, S., Khayat, D., Bleiberg, H., Santoro, A., Bets, D., Mueser, M., Harstrick, A., Verslype, C., et al. (2004). Cetuximab monotherapy and cetuximab plus irinotecan in irinotecan-refractory metastatic colorectal cancer. N. Engl. J. Med. 351, 337-345. Detre, S., Saclani Jotti, G., and Dowsett, M. (1995). A 'quickscore' method for immunohistochemical semiquantitation: validation for oestrogen receptor in breast carcinomas. J. Clin. Pathol. 48, 876-878. Di Tommaso, L., Destro, A., Fabbris, V., Spagnuolo, G., Laura Fracanzani, A., Fargion, S., Maggioni, M., Patriarca, C., Maria Macchi, R., Quagliuolo, M., et al. (2011). Diagnostic accuracy of clathrin heavy chain staining in a marker panel for the diagnosis of small hepatocellular carcinoma. Hepatology 53, 1549-1557. Edge SB, Byrd DR, Compton CC, et al. (2010) Exocrine and endocrine pancreas. AJCC Cancer Staging Manual. 7th ed. New York, NY: Springer. 241-249. Enari, M., Ohmori, K., Kitabayashi, I., and Taya, Y. (2006). Requirement of clathrin heavy chain for p53-mediated transcription. Genes Dev. 20, 1087-1099. Escudier, B., Bellmunt, J., Negrier, S., Bajetta, E., Melichar, B., Bracarda, S., Ravaud, A., Golding, S., Jethwa, S., and Sneller, V. (2010). Phase III trial of bevacizumab plus interferon alfa-2a in patients with metastatic renal cell carcinoma (AVOREN): final analysis of overall survival. J. Clin. Oncol. 28, 2144-2150. Feng, Y., Zhu, H., Ling, T., Hao, B., Zhang, G., and Shi, R. (2011). Effects of YC-1 targeting hypoxia-inducible factor 1 alpha in oesophageal squamous carcinoma cell line Eca109 cells. Cell Biol. Int. 35, 491-497. Ferrara, N., Hillan, K.J., Gerber, H.P., and Novotny, W. (2004). Discovery and development of bevacizumab, an anti-VEGF antibody for treating cancer. Nat. Rev. Drug Discov. 3, 391-400. Folkman, J. (1971). Tumor angiogenesis: therapeutic implications. N. Engl. J. Med. 285, 1182-1186. Forsythe, J.A., Jiang, B.H., Iyer, N.V., Agani, F., Leung, S.W., Koos, R.D., and Semenza, G.L. (1996). Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1. Mol. Cell Biol. 16, 4604-4613. Fotin, A., Cheng, Y., Sliz, P., Grigorieff, N., Harrison, S.C., Kirchhausen, T., and Walz, T. (2004). Molecular model for a complete clathrin lattice from electron cryomicroscopy. Nature 432, 573-579. Friedman, G.D., and van den Eeden, S.K. (1993). Risk factors for pancreatic cancer: an exploratory study. Int. J. Epidemiol. 22, 30-37. Goh, L.K., Huang, F., Kim, W., Gygi, S., and Sorkin, A. (2010). Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor. J. Cell Biol. 189, 871-883. Greenberger, L.M., Horak, I.D., Filpula, D., Sapra, P., Westergaard, M., Frydenlund, H.F., Albaek, C., Schroder, H., and Orum, H. (2008). A RNA antagonist of hypoxia-inducible factor-1alpha, EZN-2968, inhibits tumor cell growth. Mol. Cancer Ther. 7, 3598-3608. Hanahan, D., and Weinberg, R.A. (2011). Hallmarks of cancer: the next generation. Cell 144, 646-674. Harding, J., and Burtness, B. (2005). Cetuximab: an epidermal growth factor receptor chemeric human-murine monoclonal antibody. Drugs Today (Barc) 41, 107-127. Harris, M. (2004). Monoclonal antibodies as therapeutic agents for cancer. Lancet Oncol. 5, 292-302. Hingorani, S.R., Petricoin, E.F., Maitra, A., Rajapakse, V., King, C., Jacobetz, M.A., Ross, S., Conrads, T.P., Veenstra, T.D., Hitt, B.A., et al. (2003). Preinvasive and invasive ductal pancreatic cancer and its early detection in the mouse. Cancer Cell 4, 437-450. Hruban, R.H., Goggins, M., Parsons, J., and Kern, S.E. (2000). Progression model for pancreatic cancer. Clin. Cancer Res. 6, 2969-2972. Hung, J.J., Yang, M.H., Hsu, H.S., Hsu, W.H., Liu, J.S., and Wu, K.J. (2009). Prognostic significance of hypoxia-inducible factor-1alpha, TWIST1 and Snail expression in resectable non-small cell lung cancer. Thorax 64, 1082-1089. Hurwitz, H., Fehrenbacher, L., Novotny, W., Cartwright, T., Hainsworth, J., Heim, W., Berlin, J., Baron, A., Griffing, S., Holmgren, E., et al. (2004). Bevacizumab plus irinotecan, fluorouracil, and leucovorin for metastatic colorectal cancer. N. Engl. J. Med. 350, 2335-2342. Iovanna, J., Mallmann, M.C., Goncalves, A., Turrini, O., and Dagorn, J.C. (2012). Current knowledge on pancreatic cancer. Front. Oncol. 2, 6. Isaacs, J.S., Jung, Y.J., Mimnaugh, E.G., Martinez, A., Cuttitta, F., and Neckers, L.M. (2002). Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. J. Biol. Chem. 277, 29936-29944. Ischenko, I., Seeliger, H., Jauch, K.W., and Bruns, C.J. (2009). Metastatic activity and chemotherapy resistance in human pancreatic cancer--influence of cancer stem cells. Surgery 146, 430-434. Ishikawa, O., Ohigashi, H., Imaoka, S., Furukawa, H., Sasaki, Y., Fujita, M., Kuroda, C., and Iwanaga, T. (1992). Preoperative indications for extended pancreatectomy for locally advanced pancreas cancer involving the portal vein. Ann. Surg. 215, 231-236. Jain, R.K. (1999). Transport of molecules, particles, and cells in solid tumors. Annu. Rev. Biomed. Eng. 1, 241-263. Jalanko, H., Kuusela, P., Roberts, P., Sipponen, P., Haglund, C.A., and Makela, O. (1984). Comparison of a new tumour marker, CA 19-9, with alpha-fetoprotein and carcinoembryonic antigen in patients with upper gastrointestinal diseases. J. Clin. Pathol. 37, 218-222. Joffre, C., Barrow, R., Menard, L., Calleja, V., Hart, I.R., and Kermorgant, S. (2011). A direct role for Met endocytosis in tumorigenesis. Nat. Cell Biol. 13, 827-837. Jones, D.T., Trowbridge, I.S., and Harris, A.L. (2006). Effects of transferrin receptor blockade on cancer cell proliferation and hypoxia-inducible factor function and their differential regulation by ascorbate. Cancer Res. 66, 2749-2756. Kaelin, W.G., Jr., and Ratcliffe, P.J. (2008). Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol. Cell 30, 393-402. Kasibhatla, S., Jessen, K.A., Maliartchouk, S., Wang, J.Y., English, N.M., Drewe, J., Qiu, L., Archer, S.P., Ponce, A.E., Sirisoma, N., et al. (2005). A role for transferrin receptor in triggering apoptosis when targeted with gambogic acid. Proc. Natl. Acad. Sci. U. S. A. 102, 12095-12100. Kim, M.L., Sorg, I., and Arrieumerlou, C. (2011). Endocytosis-independent function of clathrin heavy chain in the control of basal NF-kappaB activation. PLoS One 6, e17158. Kindler, H.L., Niedzwiecki, D., Hollis, D., Sutherland, S., Schrag, D., Hurwitz, H., Innocenti, F., Mulcahy, M.F., O'Reilly, E., Wozniak, T.F., et al. (2010). Gemcitabine plus bevacizumab compared with gemcitabine plus placebo in patients with advanced pancreatic cancer: phase III trial of the Cancer and Leukemia Group B (CALGB 80303). J. Clin. Oncol. 28, 3617-3622. Kirchhausen, T. (2000). Clathrin. Annu. Rev. Biochem. 69, 699-727. Kirchhausen, T., Harrison, S.C., Chow, E.P., Mattaliano, R.J., Ramachandran, K.L., Smart, J., and Brosius, J. (1987). Clathrin heavy chain: molecular cloning and complete primary structure. Proc. Natl. Acad. Sci. U. S. A. 84, 8805-8809. Kohler, G., and Milstein, C. (1975). Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495-497. Kong, X., Lin, Z., Liang, D., Fath, D., Sang, N., and Caro, J. (2006). Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha. Mol. Cell. Biol. 26, 2019-2028. Koukourakis, M.I., Simopoulos, C., Polychronidis, A., Perente, S., Botaitis, S., Giatromanolaki, A., and Sivridis, E. (2003). The effect of trastuzumab/docatexel combination on breast cancer angiogenesis: dichotomus effect predictable by the HIFI alpha/VEGF pre-treatment status? Anticancer Res. 23, 1673-1680. Labianca, R., Merelli, B., and Mosconi, S. (2012). Treatment of advanced pancreatic cancer. Ann. Oncol. 23 Suppl 10, x139-140. Lai, H.C., Tsai, I.J., Chen, P.C., Muo, C.H., Chou, J.W., Peng, C.Y., Lai, S.W., Sung, F.C., Lyu, S.Y., and Morisky, D.E. (2012). Gallstones, a cholecystectomy, chronic pancreatitis, and the risk of subsequent pancreatic cancer in diabetic patients: a population-based cohort study. J. Gastroenterol. Lampugnani, M.G., Orsenigo, F., Gagliani, M.C., Tacchetti, C., and Dejana, E. (2006). Vascular endothelial cadherin controls VEGFR-2 internalization and signaling from intracellular compartments. J. Cell Biol. 174, 593-604. Laskin, J.J., and Sandler, A.B. (2004). Epidermal growth factor receptor: a promising target in solid tumours. Cancer Treat. Rev. 30, 1-17. Laughner, E., Taghavi, P., Chiles, K., Mahon, P.C., and Semenza, G.L. (2001). HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1alpha (HIF-1alpha) synthesis: novel mechanism for HIF-1-mediated vascular endothelial growth factor expression. Mol. Cell. Biol. 21, 3995-4004. Lee, T.Y., Wu, H.C., Tseng, Y.L., and Lin, C.T. (2004). A novel peptide specifically binding to nasopharyngeal carcinoma for targeted drug delivery. Cancer Res. 64, 8002-8008. Li, D., Xie, K., Wolff, R., and Abbruzzese, J.L. (2004). Pancreatic cancer. Lancet 363, 1049-1057. Li, S., Schmitz, K.R., Jeffrey, P.D., Wiltzius, J.J., Kussie, P., and Ferguson, K.M. (2005). Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell 7, 301-311. Lieu, P.T., Heiskala, M., Peterson, P.A., and Yang, Y. (2001). The roles of iron in health and disease. Mol. Aspects Med. 22, 1-87. Lin, C.W., Liao, M.Y., Lin, W.W., Wang, Y.P., Lu, T.Y., and Wu, H.C. (2012). Epithelial Cell Adhesion Molecule Regulates Tumor Initiation and Tumorigenesis via Activating Reprogramming Factors and Epithelial-Mesenchymal Transition Gene Expression in Colon Cancer. J. Biol. Chem. 287, 39449-39459. Liu, I.J., Chiu, C.Y., Chen, Y.C., and Wu, H.C. (2011). Molecular mimicry of human endothelial cell antigen by autoantibodies to nonstructural protein 1 of dengue virus. J. Biol. Chem. 286, 9726-9736. Liu, S.H., Towler, M.C., Chen, E., Chen, C.Y., Song, W., Apodaca, G., and Brodsky, F.M. (2001). A novel clathrin homolog that co-distributes with cytoskeletal components functions in the trans-Golgi network. EMBO J. 20, 272-284. Lowenfels, A.B., and Maisonneuve, P. (2005). Risk factors for pancreatic cancer. J. Cell. Biochem. 95, 649-656. Lowenfels, A.B., and Maisonneuve, P. (2006). Epidemiology and risk factors for pancreatic cancer. Best Pract. Res. Clin. Gastroenterol. 20, 197-209. Lu, T.Y., Kao, C.F., Lin, C.T., Huang, D.Y., Chiu, C.Y., Huang, Y.S., and Wu, H.C. (2009). DNA methylation and histone modification regulate silencing of OPG during tumor progression. J. Cell Biochem. 108, 315-325. Lu, T.Y., Lu, R.M., Liao, M.Y., Yu, J., Chung, C.H., Kao, C.F., and Wu, H.C. (2010). Epithelial cell adhesion molecule regulation is associated with the maintenance of the undifferentiated phenotype of human embryonic stem cells. J. Biol. Chem. 285, 8719-8732. Lundgren, K., Holm, C., and Landberg, G. (2007). Hypoxia and breast cancer: prognostic and therapeutic implications. Cell Mol. Life Sci. 64, 3233-3247. Marks, B., Stowell, M.H., Vallis, Y., Mills, I.G., Gibson, A., Hopkins, C.R., and McMahon, H.T. (2001). GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Nature 410, 231-235. Mayerhofer, M., Valent, P., Sperr, W.R., Griffin, J.D., and Sillaber, C. (2002). BCR/ABL induces expression of vascular endothelial growth factor and its transcriptional activator, hypoxia inducible factor-1alpha, through a pathway involving phosphoinositide 3-kinase and the mammalian target of rapamycin. Blood 100, 3767-3775. Maynard, J., and Georgiou, G. (2000). Antibody engineering. Annu. Rev. Biomed. Eng. 2, 339-376. McMahon, H.T., and Boucrot, E. (2011). Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 12, 517-533. Mersmann, M., Schmidt, A., Rippmann, J.F., Wuest, T., Brocks, B., Rettig, W.J., Garin-Chesa, P., Pfizenmaier, K., and Moosmayer, D. (2001). Human antibody derivatives against the fibroblast activation protein for tumor stroma targeting of carcinomas. Int. J. Cancer 92, 240-248. Mini, E., Nobili, S., Caciagli, B., Landini, I., and Mazzei, T. (2006). Cellular pharmacology of gemcitabine. Ann. Oncol. 17 Suppl 5, v7-12. Miura, F., Takada, T., Amano, H., Yoshida, M., Furui, S., and Takeshita, K. (2006). Diagnosis of pancreatic cancer. HPB (Oxford) 8, 337-342. Molina, M.A., Codony-Servat, J., Albanell, J., Rojo, F., Arribas, J., and Baselga, J. (2001). Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells. Cancer Res. 61, 4744-4749. Monti, E., and Gariboldi, M.B. (2011). HIF-1 as a target for cancer chemotherapy, chemosensitization and chemoprevention. Curr. Mol. Pharmacol. 4, 62-77. Moore, M.J., Goldstein, D., Hamm, J., Figer, A., Hecht, J.R., Gallinger, S., Au, H.J., Murawa, P., Walde, D., Wolff, R.A., et al. (2007). Erlotinib plus gemcitabine compared with gemcitabine alone in patients with advanced pancreatic cancer: a phase III trial of the National Cancer Institute of Canada Clinical Trials Group. J. Clin. Oncol. 25, 1960-1966. Morris, S.W., Kirstein, M.N., Valentine, M.B., Dittmer, K.G., Shapiro, D.N., Saltman, D.L., and Look, A.T. (1994). Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma. Science 263, 1281-1284. Moskowitz, H.S., Yokoyama, C.T., and Ryan, T.A. (2005). Highly cooperative control of endocytosis by clathrin. Mol. Biol. Cell 16, 1769-1776. Mousavi, S.A., Malerod, L., Berg, T., and Kjeken, R. (2004). Clathrin-dependent endocytosis. Biochem. J. 377, 1-16. Ng, P.P., Dela Cruz, J.S., Sorour, D.N., Stinebaugh, J.M., Shin, S.U., Shin, D.S., Morrison, S.L., and Penichet, M.L. (2002). An anti-transferrin receptor-avidin fusion protein exhibits both strong proapoptotic activity and the ability to deliver various molecules into cancer cells. Proc. Natl. Acad. Sci. U. S. A. 99, 10706-10711. Ohara, T., Noma, K., Urano, S., Watanabe, S., Nishitani, S., Tomono, Y., Kimura, F., Kagawa, S., Shirakawa, Y., and Fujiwara, T. (2012). A novel synergistic effect of iron depletion on anti-angiogenic cancer therapy. Int. J. Cancer. Ohata, H., Ota, N., Shirouzu, M., Yokoyama, S., Yokota, J., Taya, Y., and Enari, M. (2009). Identification of a function-specific mutation of clathrin heavy chain (CHC) required for p53 transactivation. J. Mol. Biol. 394, 460-471. Onnis, B., Rapisarda, A., and Melillo, G. (2009). Development of HIF-1 inhibitors for cancer therapy. J. Cell Mol. Med. 13, 2780-2786. Pan, S., Chen, R., Crispin, D.A., May, D., Stevens, T., McIntosh, M.W., Bronner, M.P., Ziogas, A., Anton-Culver, H., and Brentnall, T.A. (2011). Protein alterations associated with pancreatic cancer and chronic pancreatitis found in human plasma using global quantitative proteomics profiling. J. Proteome Res. 10, 2359-2376. Papageorgio, C., and Perry, M.C. (2007). Epidermal growth factor receptor-targeted therapy for pancreatic cancer. Cancer Invest. 25, 647-657. Pearse, B.M. (1976). Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles. Proc. Natl. Acad. Sci. U. S. A. 73, 1255-1259. Pietras, R.J., Fendly, B.M., Chazin, V.R., Pegram, M.D., Howell, S.B., and Slamon, D.J. (1994). Antibody to HER-2/neu receptor blocks DNA repair after cisplatin in human breast and ovarian cancer cells. Oncogene 9, 1829-1838. Pleskow, D.K., Berger, H.J., Gyves, J., Allen, E., McLean, A., and Podolsky, D.K. (1989). Evaluation of a serologic marker, CA19-9, in the diagnosis of pancreatic cancer. Ann. Intern. Med. 110, 704-709. Provenzano, P.P., Cuevas, C., Chang, A.E., Goel, V.K., Von Hoff, D.D., and Hingorani, S.R. (2012). Enzymatic targeting of the stroma ablates physical barriers to treatment of pancreatic ductal adenocarcinoma. Cancer Cell 21, 418-429. Raimondi, S., Maisonneuve, P., and Lowenfels, A.B. (2009). Epidemiology of pancreatic cancer: an overview. Nat. Rev. Gastroenterol. Hepatol. 6, 699-708. Royle, S.J. (2012). The role of clathrin in mitotic spindle organisation. J Cell Sci 125, 19-28. Royle, S.J., Bright, N.A., and Lagnado, L. (2005). Clathrin is required for the function of the mitotic spindle. Nature 434, 1152-1157. Saaristo, A., Karpanen, T., and Alitalo, K. (2000). Mechanisms of angiogenesis and their use in the inhibition of tumor growth and metastasis. Oncogene 19, 6122-6129. Saif, M.W. (2011). Pancreatic neoplasm in 2011: an update. JOP 12, 316-321. Sakorafas, G.H., and Sarr, M.G. (2005). Cystic neoplasms of the pancreas; what a clinician should know. Cancer Treat. Rev. 31, 507-535. Schmid, S.L. (1997). Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66, 511-548. Schmid, S.L. (2010). Clathrin-mediated endocytosis: a universe of new questions. Mol. Biol. Cell 21, 3818-3819. Schrama, D., Reisfeld, R.A., and Becker, J.C. (2006). Antibody targeted drugs as cancer therapeutics. Nat. Rev. Drug Discov. 5, 147-159. Scita, G., and Di Fiore, P.P. (2010). The endocytic matrix. Nature 463, 464-473. Seimiya, M., Tomonaga, T., Matsushita, K., Sunaga, M., Oh-Ishi, M., Kodera, Y., Maeda, T., Takano, S., Togawa, A., Yoshitomi, H., et al. (2008). Identification of novel immunohistochemical tumor markers for primary hepatocellular carcinoma; clathrin heavy chain and formiminotransferase cyclodeaminase. Hepatology 48, 519-530. Semenza, G.L. (2003). Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer 3, 721-732. Semenza, G.L. (2006). Development of novel therapeutic strategies that target HIF-1. Expert Opin. Ther. Targets 10, 267-280. Siegel, R., Naishadham, D., and Jemal, A. (2012). Cancer statistics, 2012. CA Cancer J. Clin. 62, 10-29. Sorkin, A., and Von Zastrow, M. (2002). Signal transduction and endocytosis: close encounters of many kinds. Nat. Rev. Mol. Cell Biol. 3, 600-614. Sorkin, A., and Von Zastrow, M. (2009). Endocytosis and signalling: intertwining molecular networks. Nat. Rev. Mol. Cell Biol. 10, 609-622. Starling, N., Watkins, D., Cunningham, D., Thomas, J., Webb, J., Brown, G., Thomas, K., Oates, J., and Chau, I. (2009). Dose finding and early efficacy study of gemcitabine plus capecitabine in combination with bevacizumab plus erlotinib in advanced pancreatic cancer. J. Clin. Oncol. 27, 5499-5505. Toyokuni, S. (2009). Role of iron in carcinogenesis: cancer as a ferrotoxic disease. Cancer Sci. 100, 9-16. Trail, P.A., King, H.D., and Dubowchik, G.M. (2003). Monoclonal antibody drug immunoconjugates for targeted treatment of cancer. Cancer Immunol. Immunother. 52, 328-337. Trowbridge, I.S., and Domingo, D.L. (1981). Anti-transferrin receptor monoclonal antibody and toxin-antibody conjugates affect growth of human tumour cells. Nature 294, 171-173. Van Cutsem, E., Vervenne, W.L., Bennouna, J., Humblet, Y., Gill, S., Van Laethem, J.L., Verslype, C., Scheithauer, W., Shang, A., Cosaert, J., et al. (2009). Phase III trial of bevacizumab in combination with gemcitabine and erlotinib in patients with metastatic pancreatic cancer. J. Clin. Oncol. 27, 2231-2237. Vassilopoulos, S., Esk, C., Hoshino, S., Funke, B.H., Chen, C.Y., Plocik, A.M., Wright, W.E., Kucherlapati, R., and Brodsky, F.M. (2009). A role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism. Science 324, 1192-1196. Von Hoff, D.D. (2006). What's new in pancreatic cancer treatment pipeline? Best Pract. Res. Clin. Gastroenterol. 20, 315-326. Wang, G.L., and Semenza, G.L. (1993). Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction. Blood 82, 3610-3615. Wang, Z., Sengupta, R., Banerjee, S., Li, Y., Zhang, Y., Rahman, K.M., Aboukameel, A., Mohammad, R., Majumdar, A.P., Abbruzzese, J.L., et al. (2006). Epidermal growth factor receptor-related protein inhibits cell growth and invasion in pancreatic cancer. Cancer Res. 66, 7653-7660. Wu, H.C., Jung, M.Y., Chiu, C.Y., Chao, T.T., Lai, S.C., Jan, J.T., and Shaio, M.F. (2003). Identification of a dengue virus type 2 (DEN-2) serotype-specific B-cell epitope and detection of DEN-2-immunized animal serum samples using an epitope-based peptide antigen. J. Gen. Virol. 84, 2771-2779. Wu, S.R., Cheng, T.S., Chen, W.C., Shyu, H.Y., Ko, C.J., Huang, H.P., Teng, C.H., Lin, C.H., Johnson, M.D., Lin, C.Y., et al. (2010). Matriptase is involved in ErbB-2-induced prostate cancer cell invasion. Am. J. Pathol. 177, 3145-3158. Yarden, Y., and Ullrich, A. (1988). Growth factor receptor tyrosine kinases. Annu. Rev. Biochem. 57, 443-478. Yeo, E.J., Chun, Y.S., Cho, Y.S., Kim, J., Lee, J.C., Kim, M.S., and Park, J.W. (2003). YC-1: a potential anticancer drug targeting hypoxia-inducible factor 1. J. Natl. Cancer Inst. 95, 516-525. Yoshida, N., Yoshida, S., Koishi, K., Masuda, K., and Nabeshima, Y. (1998). Cell heterogeneity upon myogenic differentiation: down-regulation of MyoD and Myf-5 generates 'reserve cells'. J. Cell Sci. 111 ( Pt 6), 769-779. Yu, Y., Gutierrez, E., Kovacevic, Z., Saletta, F., Obeidy, P., Suryo Rahmanto, Y., and Richardson, D.R. (2012). Iron chelators for the treatment of cancer. Curr. Med. Chem. 19, 2689-2702. Zhang, Q., Chen, G., Liu, X., and Qian, Q. (2007). Monoclonal antibodies as therapeutic agents in oncology and antibody gene therapy. Cell Res. 17, 89-99. Zhang, D., Li, J., Costa, M., Gao, J., and Huang, C. (2010). JNK1 mediates degradation HIF-1alpha by a VHL-independent mechanism that involves the chaperones Hsp90/Hsp70. Cancer Res. 70, 813-823. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/15669 | - |
dc.description.abstract | 胰腺癌是一種惡性以及高度致死的疾病,目前尚未有療效的治療方式提供選擇,為了提升胰腺癌的治療成效,本研究利用單株抗體技術生產Pa65-2抗體,其能專一的辨認胰腺癌細胞及腫瘤血管,並具有不辨認正常細胞的特性。Pa65-2的標靶蛋白經鑑定為人類網格重鏈蛋白 (human clathrin heavy chain, CHC)。我們發現使用小髮夾型核醣核酸(Short hairpin RNA,shRNA) 減少CHC表現的胰腺癌細胞,不僅可以減少了腫瘤細胞的增殖 (proliferation)、集落形成 (colony formation) 和侵襲 (invasion) 能力,同時也會誘導腫瘤細胞凋亡的產生。過去研究證實CHC主要功能是與細胞內吞作用有關,而透過Pa65-2處理後的胰腺癌細胞,可以抑制表皮生長因子(epidermal growth factor, EGF) 及運鐵蛋白 (transferrin, Tf) 的吞入作用,進而抑制腫瘤細胞的生長作用。在異體移植人類腫瘤的動物實驗也顯示,透過shRNA減少CHC的表現或利用Pa65-2治療,可以抑制腫瘤的生長和血管新生。本研究我們證實CHC在調控血管新生扮演了重要的角色,當細胞於缺氧情況下,CHC會與缺氧誘導因子(HIF)-1alpha蛋白結合,並幫助HIF-1alpha蛋白的穩定,促進其核轉位與其下游基因的調控子缺氧反應元件結合 (hypoxia responsive element , HRE) 進而調控血管內皮生長因子(vascular endothelial growth factor , VEGF)的表達。當透過shRNA減少CHC表現的結果,可以觀察減少了HIF-1alpha的蛋白以及下游基因,例如:VEGF, 紅血球生成素 (erythropoietin, EPO) 以及血小板生長因子-B(platelet-derived growth factor-B,PDGF-B)的表現量。綜合上述研究證實, CHC在腫瘤血管新生及腫瘤生成的過程扮演重要的角色。利用Pa65-2單株抗體或是CHC shRNA治療,未來有潛力發展為胰臟癌的治療策略。 | zh_TW |
dc.description.abstract | Pancreatic adenocarcinoma is an aggressive disease with a high mortality rate. Currently, treatment options are limited. In an effort to improve the efficacy of treatments for pancreatic adenocarcinoma, we have newly generated a monoclonal antibody (mAb), Pa65-2, which specifically binds to pancreatic cancer cells and tumor blood vessels but not to normal cells. The target protein of Pa65-2 is identified as human clathrin heavy chain (CHC). We found that knockdown of CHC not only reduced cancer cell proliferation, colony formation and invasion, but it also induced cancer cell apoptosis. Additionally, treatment of Pa65-2 blocked cancer cells’ uptake of epidermal growth factor (EGF) and transferrin (Tf), following the inhibition of cancer cell growth. In vivo study showed that suppression of CHC either by shRNA or by Pa65-2 inhibited tumor growth and angiogenesis. In this study, we demonstrated that CHC plays an important role in the regulation of angiogenesis. Under hypoxia, CHC was to bind with the hypoxia-inducing factor (HIF)-1alpha protein, increasing the stability of this protein, facilitating its nuclear translocation and hypoxia responsive element (HRE) promoter binding and thereby regulating the expression of vascular endothelial growth factor (VEGF). Knockdown of CHC results in downregulations of both HIF-1alpha | en |
dc.description.provenance | Made available in DSpace on 2021-06-07T17:49:44Z (GMT). No. of bitstreams: 1 ntu-102-D93444001-1.pdf: 9596432 bytes, checksum: 44e014a4cd342d27896844570935fc59 (MD5) Previous issue date: 2013 | en |
dc.description.tableofcontents | List of Abbreviations 1
中文摘要 4 Abstract 5 Chapter 1. Introduction 7 1-1 Pancreas 7 1-2 Pancreatic cancer 7 1-2-1 Pancreatic adenocarcinoma 9 1-2-2 Epidemiology of pancreatic cancer 9 1-2-3 Diagnosis of pancreatic cancer 10 1-2-4 Staging for pancreatic cancer 11 1-2-5 Current treatments 12 1-3 Monoclonal antibody (mAb) 13 1-4 Clathrin Heavy chain (CHC) 16 1-4-1 Clathrin genes 16 1-4-2 The structure of clathrin 17 1-4-3 The function of clathrin 18 1-5 Hypoxia inducible factor-1a (HIF-1alpha) 21 Chapter 2. Materials and methods 24 2-1 Cell lines and culture 24 2-2 Generation of monoclonal antibodies 24 2-3 Enzyme-linked immunosorbent assay and flow cytometric analysis 25 2-4 Identification of the target protein of Pa65-2 26 2-5 Immunoprecipitation and immunoblotting assay 26 2-6 Cell proliferation analysis and invasion assays 27 2-7 Short hairpin RNA (shRNA) transfection and luciferase reporter gene assays 27 2-8 Quantitative reverse transcription polymerase chain reaction (RT-PCR) 29 2-9 Hypoxia assay 29 2-10 Chromatin immunoprecipitation (ChIP) 29 2-11 Immuno-electron microscopy 30 2-12 Inhibition of cell internalization by Pa65-2 31 2-13 Immunofluorescent staining 31 2-14 Apoptosis assay 32 2-15 Animal models 32 2-16 CD31 staining and terminal deoxynucleotidyl transferase-mediated dUTP nick end Labeling (TUNEL) assay 33 2-17 Analysis of tissue samples 34 2-18 Statistical analyses 35 Chapter 3. Results 36 3-1 Generation and characterization of mAbs against pancreatic cancer 36 3-2 Identification of Pa65-2 target protein 37 3-3 Suppressing CHC expression inhibits pancreatic cancer growth 38 3-4 CHC regulates VEGF expression in pancreatic cancer 39 3-5 CHC interaction stabilizes HIF-1alpha protein in MIA PaCa-2 cells 40 3-6 Inhibition of pancreatic cancer growth and angiogenesis by Pa65-2 42 Chapter 4. Discussion 44 Chapter 5. Conclusion 50 References 51 List of Tables Table 1. Staging of pancreatic cancer 77 Table 2. List of primers 78 List of primers for cloning 78 Table 3a. CHC expression in human pancreas cancer tissue arrays 79 Table 3b. CHC expression in human pancreas cancer tissue arrays 80 List of Figures Fig. 1. ELISA determination of the titer of hyperimmune sera against MIA PaCa-2 cells. 81 Fig. 2. Determination of the binding activities of Pa65-2 on MIA PaCa-2 cells. 82 Fig. 3. Pa65-2 antibody recognized a single band of Mr 190 kDa protein on the MIA PaCa-2 by Western blotting. 83 Fig. 4. Pa65-2 shows high affinity against MIA PaCa-2 cell membrane and cytosol by labeling immuno-electron microscopy. 84 Fig. 5. Analysis of Pa65-2 localization in intact MIA PaCa-2 cells using confocal microscopy. 85 Fig. 6. Generation and characterization of mAbs against pancreatic cancer. 86 Fig. 7. Immunohistochemistry analysis of Pa65-2 in human pancreatic cancer tissue array. 87 Fig. 8. Immunofluorescent staining of Pa65-2 and Ulex europeus agglutinin-1 (UEA-1), the endothelial cell marker, show that they are co-localized 88 Fig. 9. Binding activity of Pa65-2 against various cancer cell lines. 89 Fig. 10. Purification of Pa65-2-targeted protein 90 Fig. 11. Pa65-2 specifically recognized CHC.. 91 Fig. 12. Suppressing CHC expression inhibits pancreatic cancer cell growth in vitro. 92 Fig. 13. Suppression of CHC expression had no effect on human skin fibroblast cell growth. 93 Fig. 14. Suppressing CHC expression inhibits pancreatic cancer growth in vivo. 94 Fig. 15. Suppression of CHC expression inhibits lung cancer growth and invasion. 95 Fig. 16. Suppressing CHC expression inhibits pancreatic cancer angiogenesis in vivo. 96 Fig. 17. Suppressing CHC expression inhibits VEGF expression in pancreatic cancer. 97 Fig. 18. CHC regulates VEGF expression in pancreatic cancer cells.. 98 Fig. 19. Colocalization of CHC and HIF-1alpha in MIA PaCa-2 cells by immunofluorescence. 99 Fig. 20. Colocalization of CHC and HIF-1alpha, shown by immunofluorescence, in CL1-5 cells 100 Fig. 21. CHC interacts with HIF-1alpha in MIA PaCa-2 cells.. 101 Fig. 22. CHC knockdown decreased HIF-1alpha protein expression but not mRNA level in MIA PaCa cells.. 102 Fig. 23. CHC knockdown facilitated HIF-1alpha protein degradation in MIA PaCa cells. 103 Fig. 24. CHC knockdown decreased HIF-1alpha-dependent genes expression. 104 Fig. 25. Inhibition of ligand internalization by Pa65-2. 105 Fig. 26. Inhibition of pancreatic cancer cells growth by Pa65-2.. 106 Fig. 27. Inhibition of endothelial cells growth in vitro by Pa65-2.. 107 Fig. 28. Pa65-2 suppression of pancreatic xenograft tumor growth.. 109 Fig. 29. Schematic representation of the proposed mechanism of CHC mediation of tumorigenesis. 111 | |
dc.language.iso | en | |
dc.title | 網格重鏈蛋白透過調控缺氧誘發因子-1α及血管新生因子之訊息傳遞以促進腫瘤生長及血管的新生 | zh_TW |
dc.title | Clathrin Heavy Chain Promotes Tumor Growth and Angiogenesis through Regulation of HIF-1alpha and VEGF Signaling | en |
dc.type | Thesis | |
dc.date.schoolyear | 101-1 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 林中梧(Chung-Wu Lin),周綠蘋(Lu-Ping Chow),蘇燦隆(Tsann-Long Su),高承福(Cheng-Fu Kao),沈家寧(Chia-Ning Shen) | |
dc.subject.keyword | 胰臟癌,胰臟腺癌,單株抗體,網格蛋白重鏈,缺氧誘導因子-1,血管內皮生長因子,血管新生, | zh_TW |
dc.subject.keyword | pancreatic cancer,pancreatic adenocarcinoma,monoclonal antibody,clathrin heavy chain,HIF-1alpha,VEGF,angiogenesis, | en |
dc.relation.page | 111 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2013-01-29 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 病理學研究所 | zh_TW |
顯示於系所單位: | 病理學科所 |
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