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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 郭彥彬 | |
dc.contributor.author | Tai-Sheng Wu | en |
dc.contributor.author | 吳泰昇 | zh_TW |
dc.date.accessioned | 2021-06-08T03:04:21Z | - |
dc.date.copyright | 2017-09-12 | |
dc.date.issued | 2017 | |
dc.date.submitted | 2017-07-11 | |
dc.identifier.citation | 1. Gupta B, Johnson NW, and Kumar N. Global Epidemiology of Head and Neck Cancers: A Continuing Challenge. Oncology. 2016;91(1):13-23.
2. Ferlay J, Soerjomataram I, Dikshit R, Eser S, Mathers C, Rebelo M, Parkin DM, Forman D, and Bray F. Cancer incidence and mortality worldwide: sources, methods and major patterns in GLOBOCAN 2012. International journal of cancer. 2015;136(5):E359-86. 3. Parkin DM, Bray F, Ferlay J, and Pisani P. Global cancer statistics, 2002. CA: a cancer journal for clinicians. 2005;55(2):74-108. 4. Ko YC, Huang YL, Lee CH, Chen MJ, Lin LM, and Tsai CC. Betel quid chewing, cigarette smoking and alcohol consumption related to oral cancer in Taiwan. Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology. 1995;24(10):450-3. 5. Holm LE, Lundquist PG, Ruden BI, Silfversward C, Sobin A, and Wersall J. Combined preoperative radiotherapy and surgery in the treatment of carcinoma of the anterior two-thirds of the tongue. The Laryngoscope. 1983;93(6):792-6. 6. Lo WL, Kao SY, Chi LY, Wong YK, and Chang RC. Outcomes of oral squamous cell carcinoma in Taiwan after surgical therapy: factors affecting survival. Journal of oral and maxillofacial surgery : official journal of the American Association of Oral and Maxillofacial Surgeons. 2003;61(7):751-8. 7. Willis TG, Jadayel DM, Du MQ, Peng H, Perry AR, Abdul-Rauf M, Price H, Karran L, Majekodunmi O, Wlodarska I, et al. Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types. Cell. 1999;96(1):35-45. 8. Ye H, Dogan A, Karran L, Willis TG, Chen L, Wlodarska I, Dyer MJ, Isaacson PG, and Du MQ. BCL10 expression in normal and neoplastic lymphoid tissue. Nuclear localization in MALT lymphoma. The American journal of pathology. 2000;157(4):1147-54. 9. Bertin J, Guo Y, Wang L, Srinivasula SM, Jacobson MD, Poyet JL, Merriam S, Du MQ, Dyer MJ, Robison KE, et al. CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B. The Journal of biological chemistry. 2000;275(52):41082-6. 10. Wang L, Guo Y, Huang WJ, Ke X, Poyet JL, Manji GA, Merriam S, Glucksmann MA, DiStefano PS, Alnemri ES, et al. Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B. The Journal of biological chemistry. 2001;276(24):21405-9. 11. Bertin J, Wang L, Guo Y, Jacobson MD, Poyet JL, Srinivasula SM, Merriam S, DiStefano PS, and Alnemri ES. CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B. The Journal of biological chemistry. 2001;276(15):11877-82. 12. Zhang Q, Siebert R, Yan M, Hinzmann B, Cui X, Xue L, Rakestraw KM, Naeve CW, Beckmann G, Weisenburger DD, et al. Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32). Nature genetics. 1999;22(1):63-8. 13. Lee SH, Shin MS, Kim HS, Park WS, Kim SY, Lee HK, Park JY, Oh RR, Jang JJ, Park KM, et al. Point mutations and deletions of the Bcl10 gene in solid tumors and malignant lymphomas. Cancer research. 1999;59(22):5674-7. 14. Holzmann K, Kohlhammer H, Schwaenen C, Wessendorf S, Kestler HA, Schwoerer A, Rau B, Radlwimmer B, Dohner H, Lichter P, et al. Genomic DNA-chip hybridization reveals a higher incidence of genomic amplifications in pancreatic cancer than conventional comparative genomic hybridization and leads to the identification of novel candidate genes. Cancer research. 2004;64(13):4428-33. 15. Yeh PY, Kuo SH, Yeh KH, Chuang SE, Hsu CH, Chang WC, Lin HI, Gao M, and Cheng AL. A pathway for tumor necrosis factor-alpha-induced Bcl10 nuclear translocation. Bcl10 is up-regulated by NF-kappaB and phosphorylated by Akt1 and then complexes with Bcl3 to enter the nucleus. The Journal of biological chemistry. 2006;281(1):167-75. 16. Wang D, You Y, Lin PC, Xue L, Morris SW, Zeng H, Wen R, and Lin X. Bcl10 plays a critical role in NF-kappaB activation induced by G protein-coupled receptors. Proceedings of the National Academy of Sciences of the United States of America. 2007;104(1):145-50. 17. Jiang T, Grabiner B, Zhu Y, Jiang C, Li H, You Y, Lang J, Hung MC, and Lin X. CARMA3 is crucial for EGFR-Induced activation of NF-kappaB and tumor progression. Cancer research. 2011;71(6):2183-92. 18. Martin D, Galisteo R, and Gutkind JS. CXCL8/IL8 stimulates vascular endothelial growth factor (VEGF) expression and the autocrine activation of VEGFR2 in endothelial cells by activating NFkappaB through the CBM (Carma3/Bcl10/Malt1) complex. The Journal of biological chemistry. 2009;284(10):6038-42. 19. Chang HH, Kuo MY, Cheng SJ, and Chiang CP. Expression of BCL10 is significantly associated with the progression and prognosis of oral squamous cell carcinomas in Taiwan. Oral oncology. 2009;45(7):589-93. 20. Handy DE, Castro R, and Loscalzo J. Epigenetic modifications: basic mechanisms and role in cardiovascular disease. Circulation. 2011;123(19):2145-56. 21. Liu X, Chen X, Yu X, Tao Y, Bode AM, Dong Z, and Cao Y. Regulation of microRNAs by epigenetics and their interplay involved in cancer. Journal of experimental & clinical cancer research : CR. 2013;32(96. 22. Yao HW, and Li J. Epigenetic modifications in fibrotic diseases: implications for pathogenesis and pharmacological targets. The Journal of pharmacology and experimental therapeutics. 2015;352(1):2-13. 23. Kouzarides T. Chromatin modifications and their function. Cell. 2007;128(4):693-705. 24. Martin C, and Zhang Y. The diverse functions of histone lysine methylation. Nature reviews Molecular cell biology. 2005;6(11):838-49. 25. Bernstein BE, Meissner A, and Lander ES. The mammalian epigenome. Cell. 2007;128(4):669-81. 26. Barski A, Cuddapah S, Cui K, Roh TY, Schones DE, Wang Z, Wei G, Chepelev I, and Zhao K. High-resolution profiling of histone methylations in the human genome. Cell. 2007;129(4):823-37. 27. Trerotola M, Relli V, Simeone P, and Alberti S. Epigenetic inheritance and the missing heritability. Human genomics. 2015;9(17. 28. Chen T, Zhang Y, Guo WH, Meng MB, Mo XM, and Lu Y. Effects of heterochromatin in colorectal cancer stem cells on radiosensitivity. Chinese journal of cancer. 2010;29(3):270-6. 29. Vokes EE, Weichselbaum RR, Lippman SM, and Hong WK. Head and neck cancer. The New England journal of medicine. 1993;328(3):184-94. 30. Haddad RI, and Shin DM. Recent advances in head and neck cancer. The New England journal of medicine. 2008;359(11):1143-54. 31. Negri E, La Vecchia C, Franceschi S, and Tavani A. Attributable risk for oral cancer in northern Italy. Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology. 1993;2(3):189-93. 32. Boyle P, Veronesi U, Tubiana M, Alexander FE, da Silva F, Denis LJ, Freire JM, Hakama M, Hirsch A, Kroes R, et al. European School of Oncology Advisory report to the European Commission for the 'Europe Against Cancer Programme' European Code Against Cancer. European journal of cancer. 1995;31A(9):1395-405. 33. Wutzl A, Ploder O, Kermer C, Millesi W, Ewers R, and Klug C. Mortality and causes of death after multimodality treatment for advanced oral and oropharyngeal cancer. Journal of oral and maxillofacial surgery : official journal of the American Association of Oral and Maxillofacial Surgeons. 2007;65(2):255-60. 34. Gupta GP, and Massague J. Cancer metastasis: building a framework. Cell. 2006;127(4):679-95. 35. Klemm S, Zimmermann S, Peschel C, Mak TW, and Ruland J. Bcl10 and Malt1 control lysophosphatidic acid-induced NF-kappaB activation and cytokine production. Proceedings of the National Academy of Sciences of the United States of America. 2007;104(1):134-8. 36. Arumugam T, Simeone DM, Schmidt AM, and Logsdon CD. S100P stimulates cell proliferation and survival via receptor for activated glycation end products (RAGE). The Journal of biological chemistry. 2004;279(7):5059-65. 37. Hayden MS, and Ghosh S. Shared principles in NF-kappaB signaling. Cell. 2008;132(3):344-62. 38. Hacker H, and Karin M. Regulation and function of IKK and IKK-related kinases. Science's STKE : signal transduction knowledge environment. 2006;2006(357):re13. 39. McAllister-Lucas LM, Ruland J, Siu K, Jin X, Gu S, Kim DS, Kuffa P, Kohrt D, Mak TW, Nunez G, et al. CARMA3/Bcl10/MALT1-dependent NF-kappaB activation mediates angiotensin II-responsive inflammatory signaling in nonimmune cells. Proceedings of the National Academy of Sciences of the United States of America. 2007;104(1):139-44. 40. Bhattacharyya S, Gill R, Chen ML, Zhang F, Linhardt RJ, Dudeja PK, and Tobacman JK. Toll-like receptor 4 mediates induction of the Bcl10-NFkappaB-interleukin-8 inflammatory pathway by carrageenan in human intestinal epithelial cells. The Journal of biological chemistry. 2008;283(16):10550-8. 41. Donato R. S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. The international journal of biochemistry & cell biology. 2001;33(7):637-68. 42. Salama I, Malone PS, Mihaimeed F, and Jones JL. A review of the S100 proteins in cancer. European journal of surgical oncology : the journal of the European Society of Surgical Oncology and the British Association of Surgical Oncology. 2008;34(4):357-64. 43. Cancemi P, Di Cara G, Albanese NN, Costantini F, Marabeti MR, Musso R, Lupo C, Roz E, and Pucci-Minafra I. Large-scale proteomic identification of S100 proteins in breast cancer tissues. BMC cancer. 2010;10(476. 44. Yao R, Davidson DD, Lopez-Beltran A, MacLennan GT, Montironi R, and Cheng L. The S100 proteins for screening and prognostic grading of bladder cancer. Histology and histopathology. 2007;22(9):1025-32. 45. Diederichs S, Bulk E, Steffen B, Ji P, Tickenbrock L, Lang K, Zanker KS, Metzger R, Schneider PM, Gerke V, et al. S100 family members and trypsinogens are predictors of distant metastasis and survival in early-stage non-small cell lung cancer. Cancer research. 2004;64(16):5564-9. 46. Bertram J, Palfner K, Hiddemann W, and Kneba M. Elevated expression of S100P, CAPL and MAGE 3 in doxorubicin-resistant cell lines: comparison of mRNA differential display reverse transcription-polymerase chain reaction and subtractive suppressive hybridization for the analysis of differential gene expression. Anti-cancer drugs. 1998;9(4):311-7. 47. Guerreiro Da Silva ID, Hu YF, Russo IH, Ao X, Salicioni AM, Yang X, and Russo J. S100P calcium-binding protein overexpression is associated with immortalization of human breast epithelial cells in vitro and early stages of breast cancer development in vivo. International journal of oncology. 2000;16(2):231-40. 48. Averboukh L, Liang P, Kantoff PW, and Pardee AB. Regulation of S100P expression by androgen. The Prostate. 1996;29(6):350-5. 49. Director's Challenge Consortium for the Molecular Classification of Lung A, Shedden K, Taylor JM, Enkemann SA, Tsao MS, Yeatman TJ, Gerald WL, Eschrich S, Jurisica I, Giordano TJ, et al. Gene expression-based survival prediction in lung adenocarcinoma: a multi-site, blinded validation study. Nature medicine. 2008;14(8):822-7. 50. Shyu RY, Huang SL, and Jiang SY. Retinoic acid increases expression of the calcium-binding protein S100P in human gastric cancer cells. Journal of biomedical science. 2003;10(3):313-9. 51. Logsdon CD, Simeone DM, Binkley C, Arumugam T, Greenson JK, Giordano TJ, Misek DE, Kuick R, and Hanash S. Molecular profiling of pancreatic adenocarcinoma and chronic pancreatitis identifies multiple genes differentially regulated in pancreatic cancer. Cancer research. 2003;63(10):2649-57. 52. Sato N, and Hitomi J. S100P expression in human esophageal epithelial cells: Human esophageal epithelial cells sequentially produce different S100 proteins in the process of differentiation. The Anatomical record. 2002;267(1):60-9. 53. Parkkila S, Pan PW, Ward A, Gibadulinova A, Oveckova I, Pastorekova S, Pastorek J, Martinez AR, Helin HO, and Isola J. The calcium-binding protein S100P in normal and malignant human tissues. BMC clinical pathology. 2008;8(2. 54. Whiteman HJ, Weeks ME, Dowen SE, Barry S, Timms JF, Lemoine NR, and Crnogorac-Jurcevic T. The role of S100P in the invasion of pancreatic cancer cells is mediated through cytoskeletal changes and regulation of cathepsin D. Cancer research. 2007;67(18):8633-42. 55. Koltzscher M, Neumann C, Konig S, and Gerke V. Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P. Molecular biology of the cell. 2003;14(6):2372-84. 56. Austermann J, Nazmi AR, Muller-Tidow C, and Gerke V. Characterization of the Ca2+ -regulated ezrin-S100P interaction and its role in tumor cell migration. The Journal of biological chemistry. 2008;283(43):29331-40. 57. Ko C, and Citrin D. Radiotherapy for the management of locally advanced squamous cell carcinoma of the head and neck. Oral diseases. 2009;15(2):121-32. 58. Small W, Jr., Mittal BB, Brand WN, Shetty RM, Rademaker AW, Beck GG, and Hoover SV. Role of radiation therapy in the management of carcinoma in situ of the larynx. The Laryngoscope. 1993;103(6):663-7. 59. Aleman BM, Bartelink H, and Gunderson LL. The current role of radiotherapy in colorectal cancer. European journal of cancer. 1995;31A(7-8):1333-9. 60. Cantero-Munoz P, Urien MA, and Ruano-Ravina A. Efficacy and safety of intraoperative radiotherapy in colorectal cancer: a systematic review. Cancer letters. 2011;306(2):121-33. 61. Pieters BR, de Back DZ, Koning CC, and Zwinderman AH. Comparison of three radiotherapy modalities on biochemical control and overall survival for the treatment of prostate cancer: a systematic review. Radiotherapy and oncology : journal of the European Society for Therapeutic Radiology and Oncology. 2009;93(2):168-73. 62. Thoms J, Goda JS, Zlotta AR, Fleshner NE, van der Kwast TH, Supiot S, Warde P, and Bristow RG. Neoadjuvant radiotherapy for locally advanced and high-risk prostate cancer. Nature reviews Clinical oncology. 2011;8(2):107-13. 63. Sadozye AH, and Reed N. A review of recent developments in image-guided radiation therapy in cervix cancer. Current oncology reports. 2012;14(6):519-26. 64. Powell ME. Modern radiotherapy and cervical cancer. International journal of gynecological cancer : official journal of the International Gynecological Cancer Society. 2010;20(11 Suppl 2):S49-51. 65. Barker HE, Paget JT, Khan AA, and Harrington KJ. The tumour microenvironment after radiotherapy: mechanisms of resistance and recurrence. Nature reviews Cancer. 2015;15(7):409-25. 66. Hein AL, Ouellette MM, and Yan Y. Radiation-induced signaling pathways that promote cancer cell survival (review). International journal of oncology. 2014;45(5):1813-9. 67. Skvortsova I, Debbage P, Kumar V, and Skvortsov S. Radiation resistance: Cancer stem cells (CSCs) and their enigmatic pro-survival signaling. Seminars in cancer biology. 2015;35(39-44. 68. Ogawa K, Yoshioka Y, Isohashi F, Seo Y, Yoshida K, and Yamazaki H. Radiotherapy targeting cancer stem cells: current views and future perspectives. Anticancer research. 2013;33(3):747-54. 69. Clarke MF, Dick JE, Dirks PB, Eaves CJ, Jamieson CH, Jones DL, Visvader J, Weissman IL, and Wahl GM. Cancer stem cells--perspectives on current status and future directions: AACR Workshop on cancer stem cells. Cancer research. 2006;66(19):9339-44. 70. Chen J, Li Y, Yu TS, McKay RM, Burns DK, Kernie SG, and Parada LF. A restricted cell population propagates glioblastoma growth after chemotherapy. Nature. 2012;488(7412):522-6. 71. Zeimet AG, Reimer D, Sopper S, Boesch M, Martowicz A, Roessler J, Wiedemair AM, Rumpold H, Untergasser G, Concin N, et al. Ovarian cancer stem cells. Neoplasma. 2012;59(6):747-55. 72. Lacerda L, Pusztai L, and Woodward WA. The role of tumor initiating cells in drug resistance of breast cancer: Implications for future therapeutic approaches. Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy. 2010;13(4-5):99-108. 73. Seshacharyulu P, Baine MJ, Souchek JJ, Menning M, Kaur S, Yan Y, Ouellette MM, Jain M, Lin C, and Batra SK. Biological determinants of radioresistance and their remediation in pancreatic cancer. Biochimica et biophysica acta. 2017;1868(1):69-92. 74. Naik PP, Das DN, Panda PK, Mukhopadhyay S, Sinha N, Praharaj PP, Agarwal R, and Bhutia SK. Implications of cancer stem cells in developing therapeutic resistance in oral cancer. Oral oncology. 2016;62(122-35. 75. Furukawa Y, and Kikuchi J. Epigenetic mechanisms of cell adhesion-mediated drug resistance in multiple myeloma. International journal of hematology. 2016;104(3):281-92. 76. Shukla S, and Meeran SM. Epigenetics of cancer stem cells: Pathways and therapeutics. Biochimica et biophysica acta. 2014;1840(12):3494-502. 77. Yang G, Quan Y, Wang W, Fu Q, Wu J, Mei T, Li J, Tang Y, Luo C, Ouyang Q, et al. Dynamic equilibrium between cancer stem cells and non-stem cancer cells in human SW620 and MCF-7 cancer cell populations. British journal of cancer. 2012;106(9):1512-9. 78. Jaatinen T, Hemmoranta H, Hautaniemi S, Niemi J, Nicorici D, Laine J, Yli-Harja O, and Partanen J. Global gene expression profile of human cord blood-derived CD133+ cells. Stem cells. 2006;24(3):631-41. 79. Wong DJ, Liu H, Ridky TW, Cassarino D, Segal E, and Chang HY. Module map of stem cell genes guides creation of epithelial cancer stem cells. Cell stem cell. 2008;2(4):333-44. 80. Yang XH, Tang F, Shin J, and Cunningham JM. A c-Myc-regulated stem cell-like signature in high-risk neuroblastoma: A systematic discovery (Target neuroblastoma ESC-like signature). Scientific reports. 2017;7(1):41. 81. Marquardt JU, Factor VM, and Thorgeirsson SS. Epigenetic regulation of cancer stem cells in liver cancer: current concepts and clinical implications. Journal of hepatology. 2010;53(3):568-77. 82. Krivtsov AV, and Armstrong SA. MLL translocations, histone modifications and leukaemia stem-cell development. Nature reviews Cancer. 2007;7(11):823-33. 83. Haladyna JN, Yamauchi T, Neff T, and Bernt KM. Epigenetic modifiers in normal and malignant hematopoiesis. Epigenomics. 2015;7(2):301-20. 84. Bertani S, Sauer S, Bolotin E, and Sauer F. The noncoding RNA Mistral activates Hoxa6 and Hoxa7 expression and stem cell differentiation by recruiting MLL1 to chromatin. Molecular cell. 2011;43(6):1040-6. 85. Mishra BP, Zaffuto KM, Artinger EL, Org T, Mikkola HK, Cheng C, Djabali M, and Ernst P. The histone methyltransferase activity of MLL1 is dispensable for hematopoiesis and leukemogenesis. Cell reports. 2014;7(4):1239-47. 86. Heddleston JM, Wu Q, Rivera M, Minhas S, Lathia JD, Sloan AE, Iliopoulos O, Hjelmeland AB, and Rich JN. Hypoxia-induced mixed-lineage leukemia 1 regulates glioma stem cell tumorigenic potential. Cell death and differentiation. 2012;19(3):428-39. 87. Zou JX, Duan Z, Wang J, Sokolov A, Xu J, Chen CZ, Li JJ, and Chen HW. Kinesin family deregulation coordinated by bromodomain protein ANCCA and histone methyltransferase MLL for breast cancer cell growth, survival, and tamoxifen resistance. Molecular cancer research : MCR. 2014;12(4):539-49. 88. Huo H, Magro PG, Pietsch EC, Patel BB, and Scotto KW. Histone methyltransferase MLL1 regulates MDR1 transcription and chemoresistance. Cancer research. 2010;70(21):8726-35. 89. Capell BC, Drake AM, Zhu J, Shah PP, Dou Z, Dorsey J, Simola DF, Donahue G, Sammons M, Rai TS, et al. MLL1 is essential for the senescence-associated secretory phenotype. Genes & development. 2016;30(3):321-36. 90. Fong CY, Gilan O, Lam EY, Rubin AF, Ftouni S, Tyler D, Stanley K, Sinha D, Yeh P, Morison J, et al. BET inhibitor resistance emerges from leukaemia stem cells. Nature. 2015;525(7570):538-42. 91. Malik R, Khan AP, Asangani IA, Cieslik M, Prensner JR, Wang X, Iyer MK, Jiang X, Borkin D, Escara-Wilke J, et al. Targeting the MLL complex in castration-resistant prostate cancer. Nature medicine. 2015;21(4):344-52. 92. Rathert P, Roth M, Neumann T, Muerdter F, Roe JS, Muhar M, Deswal S, Cerny-Reiterer S, Peter B, Jude J, et al. Transcriptional plasticity promotes primary and acquired resistance to BET inhibition. Nature. 2015;525(7570):543-7. 93. Lim DA, Huang YC, Swigut T, Mirick AL, Garcia-Verdugo JM, Wysocka J, Ernst P, and Alvarez-Buylla A. Chromatin remodelling factor Mll1 is essential for neurogenesis from postnatal neural stem cells. Nature. 2009;458(7237):529-33. 94. Nayak A, Viale-Bouroncle S, Morsczeck C, and Muller S. The SUMO-specific isopeptidase SENP3 regulates MLL1/MLL2 methyltransferase complexes and controls osteogenic differentiation. Molecular cell. 2014;55(1):47-58. 95. Mishra BP, Ansari KI, and Mandal SS. Dynamic association of MLL1, H3K4 trimethylation with chromatin and Hox gene expression during the cell cycle. The FEBS journal. 2009;276(6):1629-40. 96. Terranova R, Agherbi H, Boned A, Meresse S, and Djabali M. Histone and DNA methylation defects at Hox genes in mice expressing a SET domain-truncated form of Mll. Proceedings of the National Academy of Sciences of the United States of America. 2006;103(17):6629-34. 97. Milne TA, Briggs SD, Brock HW, Martin ME, Gibbs D, Allis CD, and Hess JL. MLL targets SET domain methyltransferase activity to Hox gene promoters. Molecular cell. 2002;10(5):1107-17. 98. Takahashi K, Tanabe K, Ohnuki M, Narita M, Ichisaka T, Tomoda K, and Yamanaka S. Induction of pluripotent stem cells from adult human fibroblasts by defined factors. Cell. 2007;131(5):861-72. 99. Marson A, Foreman R, Chevalier B, Bilodeau S, Kahn M, Young RA, and Jaenisch R. Wnt signaling promotes reprogramming of somatic cells to pluripotency. Cell stem cell. 2008;3(2):132-5. 100. Li J, Yu B, Deng P, Cheng Y, Yu Y, Kevork K, Ramadoss S, Ding X, Li X, and Wang CY. KDM3 epigenetically controls tumorigenic potentials of human colorectal cancer stem cells through Wnt/beta-catenin signalling. Nature communications. 2017;8(15146. 101. Qiang R, Cai N, Wang X, Wang L, Cui K, Wang X, and Li X. MLL1 promotes cervical carcinoma cell tumorigenesis and metastasis through interaction with beta-catenin. OncoTargets and therapy. 2016;9(6631-40. 102. Cetinkaya M, Ozgur E, Dalay N, and Gezer U. Global quantification of heterochromatin-associated histone methylations in cell lines with differential sensitivity to ionizing radiation. Acta biochimica Polonica. 2015;62(2):173-6. 103. Chopra M, and Bohlander SK. Disturbing the histone code in leukemia: translocations and mutations affecting histone methyl transferases. Cancer genetics. 2015;208(5):192-205. 104. Thiel AT, Blessington P, Zou T, Feather D, Wu X, Yan J, Zhang H, Liu Z, Ernst P, Koretzky GA, et al. MLL-AF9-induced leukemogenesis requires coexpression of the wild-type Mll allele. Cancer cell. 2010;17(2):148-59. 105. Wang WJ, Wu SP, Liu JB, Shi YS, Huang X, Zhang QB, and Yao KT. MYC regulation of CHK1 and CHK2 promotes radioresistance in a stem cell-like population of nasopharyngeal carcinoma cells. Cancer research. 2013;73(3):1219-31. 106. Ansari KI, Hussain I, Das HK, and Mandal SS. Overexpression of human histone methylase MLL1 upon exposure to a food contaminant mycotoxin, deoxynivalenol. The FEBS journal. 2009;276(12):3299-307. 107. Xu X, Fan Z, Liang C, Li L, Wang L, Liang Y, Wu J, Chang S, Yan Z, Lv Z, et al. A signature motif in LIM proteins mediates binding to checkpoint proteins and increases tumour radiosensitivity. Nature communications. 2017;8(14059. 108. Kurth I, Hein L, Mabert K, Peitzsch C, Koi L, Cojoc M, Kunz-Schughart L, Baumann M, and Dubrovska A. Cancer stem cell related markers of radioresistance in head and neck squamous cell carcinoma. Oncotarget. 2015;6(33):34494-509. 109. Huang EH, Hynes MJ, Zhang T, Ginestier C, Dontu G, Appelman H, Fields JZ, Wicha MS, and Boman BM. Aldehyde dehydrogenase 1 is a marker for normal and malignant human colonic stem cells (SC) and tracks SC overpopulation during colon tumorigenesis. Cancer research. 2009;69(8):3382-9. 110. Gilormini M, Wozny AS, Battiston-Montagne P, Ardail D, Alphonse G, and Rodriguez-Lafrasse C. Isolation and Characterization of a Head and Neck Squamous Cell Carcinoma Subpopulation Having Stem Cell Characteristics. Journal of visualized experiments : JoVE. 2016111). 111. Khorrami S, Zavaran Hosseini A, Mowla SJ, and Malekzadeh R. Verification of ALDH Activity as a Biomarker in Colon Cancer Stem Cells-Derived HT-29 Cell Line. Iranian journal of cancer prevention. 2015;8(5):e3446. 112. Marcato P, Dean CA, Liu RZ, Coyle KM, Bydoun M, Wallace M, Clements D, Turner C, Mathenge EG, Gujar SA, et al. Aldehyde dehydrogenase 1A3 influences breast cancer progression via differential retinoic acid signaling. Molecular oncology. 2015;9(1):17-31. 113. Kwon MJ, and Shin YK. Epigenetic regulation of cancer-associated genes in ovarian cancer. International journal of molecular sciences. 2011;12(2):983-1008. 114. Yan GN, Lv YF, and Guo QN. Advances in osteosarcoma stem cell research and opportunities for novel therapeutic targets. Cancer letters. 2016;370(2):268-74. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/20803 | - |
dc.description.abstract | 惡性度較高的癌細胞通常表現出較高的侵入能力以及生長力,而這些能力與促使口腔鱗狀上皮細胞癌轉移有所關聯,也似乎會去影響到癌細胞對於治療的反應。基因的轉錄、分子的表基因調控、以及細胞的訊息傳遞皆是促成口腔鱗狀上皮細胞癌生成的基礎,並且更會造成細胞顯型的改變。本論文在探討促使口腔癌進程的可能致癌基因以及研究表基因修飾調控所造成的口腔癌放射線抗性機轉。
在第二章中,我們著重在細胞凋零調控蛋白BCL10,其已經被發現與口腔癌惡性程度以及再復發有所關聯。抑制內生性BCL10 的表現量能夠顯著的降低細胞移動以及侵襲能力,並且阻礙細胞生長以及抑制腫瘤生成。在分子層面上,我們發現S100P 是BCL10 誘導細胞進程的重要下游調控因子。S100P 的mRNA 以及蛋白質表現皆在抑制BCL10 轉殖株中顯著降低,且轉染S100P 表現質體後可以明顯的恢復細胞移動、侵入、生長以及腫瘤生長的能力。我們也提供證據證實BCL10 調控S100 的表現量是經由轉錄因子STAT1 以及ATF4,在抑制BCL10表現量後會明顯降低S100P 啟動子活性,但是將其SAT1/ATF4 的結合位置截斷的啟動子則 不會受到影響。除此之外,BCL10 促進的口腔癌進程有P50/P65 訊息傳遞參與,在抑制BCL10轉植株中回復S100P 表現量可以明顯重建P65 的活性。 由於現今口腔癌的再復發一直是臨床上遇到的重大難題,其中一部分是因為口腔癌的惡性以及侵入能力,而另一方面則是放射線治療上無法成功的移除殘餘癌細胞。在第三章中,我們分析了組蛋白甲基化轉移酶的表現量在癌症幹細胞、脂肪幹細胞以及放射線處理之癌細胞中,發現了H3K4 組蛋白甲基化轉移酶在幹細胞特性以及放射線抗性上實為重要。除此之外,我們更進一步找出其中一個H3K4 組蛋白甲基化轉移酶MLL1 在癌症幹細胞以及具有放射線抗性的口腔癌細胞和大腸癌細胞皆有高度表現。抑制MLL1 的表現會明顯增加原本具有抗性之口腔癌及大腸癌細胞的放射線敏感度、降低癌細胞聚球以及腫瘤生成能力。更進一步的我們分析出具有放射線抗性的細胞以及口腔癌臨床檢體中c-MYC 下游基因皆有顯著上升的情形,並且發現MLL1 會經由直接結合到c-MYC 啟動子的區域,促進其表現量後使其下游 基因表現量增加進而造成細胞具有幹細胞特性以及放射線抗性。 總結來說,我們發現了一個經由BCL10 調控STAT1/ATF4/S100P/P65 訊息傳遞鏈促使口腔癌進成的新路徑,可作為口腔癌的預後因子以及有潛力發展為口腔癌治療的新策略。除此之外,我們還證實了組蛋白甲基化轉移酶MLL1 可以經由表基因修飾機轉調控幹細胞特性以及放射線抗性,提供了一個新的移除癌症幹細胞的治療目標。 | zh_TW |
dc.description.abstract | Advanced cancer cells show higher invasion and proliferation abilities, and such capacities have implications in progression of oral squamous cell carcinoma (OSCC) to metastasis, and will likely influence response to therapy. The transcriptional and epigenetic regulation of molecular and cell signaling that underlie OSCC and result in characteristic change in cell phenotype. We investigated the potential oncogene in cancer progression and elucidated the crucial epigenetic regulator in radioresistance of OSCC.
In chapter II, we focus on an apoptotic regulatory protein named BCL10, which related to advanced TNM stage and disease recurrence in OSCC. Knockdown of endogenous BCL10 significantly reduce cell migration and invasion abilities, retard cell proliferation and inhibit tumorigenicity in vivo. In molecular level, we identified S100P as a crucial downstream effeter of BCL10-mediated OSCC progression. S100P mRNA and protein expression levels significantly diminished in silenced BCL10 clones, and transfected S100P expression plasmids restored migration, invasion, proliferation abilities and tumorigenicity in shBCL10 transfectants. We provided evidence that BCL10 regulated S100P expression through STAT1 and ATF4, and knockdown of BCL10 decreased S100P promoter activity, but showed no effect in truncated STAT1/ATF4 S100P promoter. In addition, P50/P65 signaling pathway was involved in BCL10-enhanced OSCC progression. Restored S100P in silenced-BCL10 clones could markedly reverse P65 activation via outside-in signaling. Because relapsed of OSCC represents a major clinical challenge in part due to their aggressive and invasive behaviors, and the fact that the radiotherapy has not succeeded eliminate the residual cancer. In chapter III, we analyzed histone methyltranferases (HMT) expression profile of stem-like cancer cells, adipose-derived stem cells, and IR-treated cancer cells, and identified histone H3-lysine 4 (H3K4) as a crucial residue for epigenetic modification in stem cell phenotype and radio-resistance contribution. Moreover, we have determined that one of H3K4 HMT, mixed-lineage leukemia 1 (MLL1), which is highly expressed in stem-like cells and IR-resistant OSCC and colorectal cancer cells (CRC). Knockdown of MLL1 in IR-resistant OSCC and CRC cells significantly induced radiosensitivity, disrupted cancer spheroid formation, and decreased tumorigenicity in vivo. Furthermore, IR-resistant subpopulation in both cancer cell lines and OSCC patients were highly expressed c-MYC downstream target genes, and we founded that MLL1 directly bound to HOXC8 and c-MYC promoter region, and further induced downstream effecter expression that contribute stemness properties and IR resistance. In summary, we discover a novel axis of BCL10-regulated OSCC progression via STAT1/ATF4/S100P/P65 signaling, which could predict the prognosis of OSCC and will be beneficial for developing therapeutic strategy against advanced OSCC. In addition, we also demonstrate and characterize an epigenetic mechanism that underlines MLL1 in the regulation of stem cell feature and IR resistance, suggesting a potential therapeutic target for eradicating stem-like cancer cells. | en |
dc.description.provenance | Made available in DSpace on 2021-06-08T03:04:21Z (GMT). No. of bitstreams: 1 ntu-106-D01422004-1.pdf: 8465148 bytes, checksum: 2e7b4dfcc29161db28603bac780873d0 (MD5) Previous issue date: 2017 | en |
dc.description.tableofcontents | 目錄 (Index)
口試委員審定書.............................................. i 中文摘要.................................................. ii 英文摘要.................................................. iv 目錄 (Index) ............................................ vi 第一章 序論 (Introduction) ................................ 1 第一節 人類口腔鱗狀細胞癌 (Human oral squamous cell carcinoma) ............................................... 2 第二節 B 細胞淋巴癌10 號(B cell lymphoma/leukemia 10) ....... 4 第三節 組蛋白甲基化酶 (Histone methyltransferase) ........... 5 第四節本論文的研究動機與方向 (Motivation and purpose in this thesis)....................................................6 第二章 (B-Cell Lymphoma/Leukemia 10 Promotes Oral Cancer Progression through STAT1/ATF4/S100P Signaling Pathway) ................................................. 7 第一節 摘要 (Abstract) .................................... 8 第二節 前言 (Introduction)............................................ 9 第三節 材料與方法 (Materials and methods) ................. 11 第四節 實驗結果 (Results) ................................. 16 第五節 討論 (Discussion) ................................. 20 第六節 表格 (Tables) ..................................... 22 第六節 附圖及說明 (Figures and figure legends)............. 25 第三章(Methyltransferase MLL1 Increased Radioresistance and Stemness Properties in Cancer Cells through c-MYC) ...... 39 第一節 摘要 (Abstract) ................................... 40 第二節 前言 (Introduction) ............................... 41 第三節 材料與方法 (Materials and methods) ................. 43 第四節 實驗結果 (Results) ................................. 47 第五節 討論 (Discussion) ................................. 54 第六節 附圖及說明 (Figures and figure legends)............. 58 第四章 結論 (Conclusion) ................................. 86 參考文獻 (Reference)...................................... 89 附錄:已發表之論文(Publication list) ...................... 103 | |
dc.language.iso | en | |
dc.title | MLL1經由c-MYC增加癌細胞放射線抗性及幹細胞特性 | zh_TW |
dc.title | Methyltransferase MLL1 Increased Radioresistance and
Stemness Properties in Cancer Cells through c-MYC | en |
dc.type | Thesis | |
dc.date.schoolyear | 105-2 | |
dc.description.degree | 博士 | |
dc.contributor.coadvisor | 章浩宏 | |
dc.contributor.oralexamcommittee | 江俊斌,魏耀揮,林芸薇 | |
dc.subject.keyword | BCL10,癌症轉移,放射線抗性,表基因修飾,癌症幹細胞,口腔鱗狀上皮細胞癌, | zh_TW |
dc.subject.keyword | BCL10,Metastasis,Radioresistance,Epigenetic modification,Cancer stem cell,OSCC, | en |
dc.relation.page | 103 | |
dc.identifier.doi | 10.6342/NTU201701361 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2017-07-11 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 臨床牙醫學研究所 | zh_TW |
顯示於系所單位: | 臨床牙醫學研究所 |
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