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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 賴亮全 | |
dc.contributor.author | Wei-Yung Huang | en |
dc.contributor.author | 黃為雍 | zh_TW |
dc.date.accessioned | 2021-06-16T06:39:28Z | - |
dc.date.available | 2019-10-09 | |
dc.date.copyright | 2014-10-09 | |
dc.date.issued | 2014 | |
dc.date.submitted | 2014-07-30 | |
dc.identifier.citation | References
1. Cancer Genome Atlas N (2012) Comprehensive molecular portraits of human breast tumours. Nature 490: 61-70. 2. Perou CM, Sorlie T, Eisen MB, van de Rijn M, Jeffrey SS, et al. (2000) Molecular portraits of human breast tumours. Nature 406: 747-752. 3. Masson N, Ratcliffe PJ (2014) Hypoxia signaling pathways in cancer metabolism: the importance of co-selecting interconnected physiological pathways. Cancer Metab 2: 3. 4. Gulledge CJ, Dewhirst MW (1996) Tumor oxygenation: a matter of supply and demand. Anticancer Res 16: 741-749. 5. Curran CS, Keely PJ (2013) Breast tumor and stromal cell responses to TGF-beta and hypoxia in matrix deposition. Matrix Biol 32: 95-105. 6. Harris AL (2002) Hypoxia--a key regulatory factor in tumour growth. Nat Rev Cancer 2: 38-47. 7. Hockel M, Schlenger K, Aral B, Mitze M, Schaffer U, et al. (1996) Association between tumor hypoxia and malignant progression in advanced cancer of the uterine cervix. Cancer Res 56: 4509-4515. 8. Bristow RG, Hill RP (2008) Hypoxia and metabolism. Hypoxia, DNA repair and genetic instability. Nat Rev Cancer 8: 180-192. 9. Knowles HJ, Harris AL (2001) Hypoxia and oxidative stress in breast cancer. Hypoxia and tumourigenesis. Breast Cancer Res 3: 318-322. 10. Hong SS, Lee H, Kim KW (2004) HIF-1alpha: a valid therapeutic target for tumor therapy. Cancer Res Treat 36: 343-353. 11. Toustrup K, Sorensen BS, Nordsmark M, Busk M, Wiuf C, et al. (2011) Development of a hypoxia gene expression classifier with predictive impact for hypoxic modification of radiotherapy in head and neck cancer. Cancer Res 71: 5923-5931. 12. Schmidt JV, Bradfield CA (1996) Ah receptor signaling pathways. Annu Rev Cell Dev Biol 12: 55-89. 13. Denison MS, Pandini A, Nagy SR, Baldwin EP, Bonati L (2002) Ligand binding and activation of the Ah receptor. Chem Biol Interact 141: 3-24. 14. Callero MA, Loaiza-Perez AI (2011) The role of aryl hydrocarbon receptor and crosstalk with estrogen receptor in response of breast cancer cells to the novel antitumor agents benzothiazoles and aminoflavone. Int J Breast Cancer 2011: 923250. 15. Wilhelmsson A, Cuthill S, Denis M, Wikstrom AC, Gustafsson JA, et al. (1990) The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein. Embo j 9: 69-76. 16. Meyer BK, Pray-Grant MG, Vanden Heuvel JP, Perdew GH (1998) Hepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity. Mol Cell Biol 18: 978-988. 17. Johnson JL, Toft DO (1994) A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. J Biol Chem 269: 24989-24993. 18. Kazlauskas A, Poellinger L, Pongratz I (1999) Evidence that the co-chaperone p23 regulates ligand responsiveness of the dioxin (Aryl hydrocarbon) receptor. J Biol Chem 274: 13519-13524. 19. Hankinson O (1995) The aryl hydrocarbon receptor complex. Annu Rev Pharmacol Toxicol 35: 307-340. 20. Probst MR, Reisz-Porszasz S, Agbunag RV, Ong MS, Hankinson O (1993) Role of the aryl hydrocarbon receptor nuclear translocator protein in aryl hydrocarbon (dioxin) receptor action. Mol Pharmacol 44: 511-518. 21. Bacsi SG, Reisz-Porszasz S, Hankinson O (1995) Orientation of the heterodimeric aryl hydrocarbon (dioxin) receptor complex on its asymmetric DNA recognition sequence. Mol Pharmacol 47: 432-438. 22. Port JL, Yamaguchi K, Du B, De Lorenzo M, Chang M, et al. (2004) Tobacco smoke induces CYP1B1 in the aerodigestive tract. Carcinogenesis 25: 2275-2281. 23. Kawajiri K, Fujii-Kuriyama Y (2007) Cytochrome P450 gene regulation and physiological functions mediated by the aryl hydrocarbon receptor. Arch Biochem Biophys 464: 207-212. 24. Wenger RH, Gassmann M (1997) Oxygen(es) and the hypoxia-inducible factor-1. Biol Chem 378: 609-616. 25. Wang GL, Semenza GL (1993) Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia. J Biol Chem 268: 21513-21518. 26. Greijer AE, van der Wall E (2004) The role of hypoxia inducible factor 1 (HIF-1) in hypoxia induced apoptosis. J Clin Pathol 57: 1009-1014. 27. Chan WK, Yao G, Gu YZ, Bradfield CA (1999) Cross-talk between the aryl hydrocarbon receptor and hypoxia inducible factor signaling pathways. Demonstration of competition and compensation. J Biol Chem 274: 12115-12123. 28. Terzuoli E, Puppo M, Rapisarda A, Uranchimeg B, Cao L, et al. (2010) Aminoflavone, a ligand of the aryl hydrocarbon receptor, inhibits HIF-1alpha expression in an AhR-independent fashion. Cancer Res 70: 6837-6848. 29. Zhang N, Walker MK (2007) Crosstalk between the aryl hydrocarbon receptor and hypoxia on the constitutive expression of cytochrome P4501A1 mRNA. Cardiovasc Toxicol 7: 282-290. 30. Vorrink SU, Severson PL, Kulak MV, Futscher BW, Domann FE (2014) Hypoxia perturbs aryl hydrocarbon receptor signaling and CYP1A1 expression induced by PCB 126 in human skin and liver-derived cell lines. Toxicol Appl Pharmacol 274: 408-416. 31. Yu RM, Ng PK, Tan T, Chu DL, Wu RS, et al. (2008) Enhancement of hypoxia-induced gene expression in fish liver by the aryl hydrocarbon receptor (AhR) ligand, benzo[a]pyrene (BaP). Aquat Toxicol 90: 235-242. 32. Zhu C, Xie Q, Zhao B (2014) The Role of AhR in Autoimmune Regulation and Its Potential as a Therapeutic Target against CD4 T Cell Mediated Inflammatory Disorder. Int J Mol Sci 15: 10116-10135. 33. Koliopanos A, Kleeff J, Xiao Y, Safe S, Zimmermann A, et al. (2002) Increased arylhydrocarbon receptor expression offers a potential therapeutic target for pancreatic cancer. Oncogene 21: 6059-6070. 34. Goode GD, Ballard BR, Manning HC, Freeman ML, Kang Y, et al. (2013) Knockdown of aberrantly upregulated aryl hydrocarbon receptor reduces tumor growth and metastasis of MDA-MB-231 human breast cancer cell line. Int J Cancer 133: 2769-2780. 35. DiNatale BC, Smith K, John K, Krishnegowda G, Amin SG, et al. (2012) Ah receptor antagonism represses head and neck tumor cell aggressive phenotype. Mol Cancer Res 10: 1369-1379. 36. Bae DH, Jansson PJ, Huang ML, Kovacevic Z, Kalinowski D, et al. (2013) The role of NDRG1 in the pathology and potential treatment of human cancers. J Clin Pathol 66: 911-917. 37. Fang BA, Kovacevic Z, Park KC, Kalinowski DS, Jansson PJ, et al. (2014) Molecular functions of the iron-regulated metastasis suppressor, NDRG1, and its potential as a molecular target for cancer therapy. Biochim Biophys Acta 1845: 1-19. 38. Salnikow K, An WG, Melillo G, Blagosklonny MV, Costa M (1999) Nickel-induced transformation shifts the balance between HIF-1 and p53 transcription factors. Carcinogenesis 20: 1819-1823. 39. Kurdistani SK, Arizti P, Reimer CL, Sugrue MM, Aaronson SA, et al. (1998) Inhibition of tumor cell growth by RTP/rit42 and its responsiveness to p53 and DNA damage. Cancer Res 58: 4439-4444. 40. Angst E, Dawson DW, Stroka D, Gloor B, Park J, et al. (2011) N-myc downstream regulated gene-1 expression correlates with reduced pancreatic cancer growth and increased apoptosis in vitro and in vivo. Surgery 149: 614-624. 41. Lu WJ, Chua MS, So SK (2014) Suppressing N-Myc downstream regulated gene 1 reactivates senescence signaling and inhibits tumor growth in hepatocellular carcinoma. Carcinogenesis 35: 915-922. 42. Wang Q, Li LH, Gao GD, Wang G, Qu L, et al. (2013) HIF-1alpha up-regulates NDRG1 expression through binding to NDRG1 promoter, leading to proliferation of lung cancer A549 cells. Mol Biol Rep 40: 3723-3729. 43. Salnikow K, Kluz T, Costa M, Piquemal D, Demidenko ZN, et al. (2002) The regulation of hypoxic genes by calcium involves c-Jun/AP-1, which cooperates with hypoxia-inducible factor 1 in response to hypoxia. Mol Cell Biol 22: 1734-1741. 44. Zhang P, Tchou-Wong KM, Costa M (2007) Egr-1 mediates hypoxia-inducible transcription of the NDRG1 gene through an overlapping Egr-1/Sp1 binding site in the promoter. Cancer Res 67: 9125-9133. 45. Ellen TP, Ke Q, Zhang P, Costa M (2008) NDRG1, a growth and cancer related gene: regulation of gene expression and function in normal and disease states. Carcinogenesis 29: 2-8. 46. Toffoli S, Delaive E, Dieu M, Feron O, Raes M, et al. (2009) NDRG1 and CRK-I/II are regulators of endothelial cell migration under Intermittent Hypoxia. Angiogenesis 12: 339-354. 47. Kovacevic Z, Richardson DR (2006) The metastasis suppressor, Ndrg-1: a new ally in the fight against cancer. Carcinogenesis 27: 2355-2366. 48. Cheng J, Xie HY, Xu X, Wu J, Wei X, et al. (2011) NDRG1 as a biomarker for metastasis, recurrence and of poor prognosis in hepatocellular carcinoma. Cancer Lett 310: 35-45. 49. Lai LC, Su YY, Chen KC, Tsai MH, Sher YP, et al. (2011) Down-regulation of NDRG1 promotes migration of cancer cells during reoxygenation. PLoS One 6: e24375. 50. Bunn HF, Poyton RO (1996) Oxygen sensing and molecular adaptation to hypoxia. Physiol Rev 76: 839-885. 51. Donderski R, Szczepanek J, Domagalski K, Tretyn A, Korenkiewicz J, et al. (2013) Analysis of relative expression level of VEGF ( vascular endothelial growth factor ), HIF-1alpha ( hypoxia inducible factor 1alpha ) and CTGF ( connective tissue growth factor ) genes in chronic glomerulonephritis (CGN) patients. Kidney Blood Press Res 38: 83-91. 52. Karaczyn A, Ivanov S, Reynolds M, Zhitkovich A, Kasprzak KS, et al. (2006) Ascorbate depletion mediates up-regulation of hypoxia-associated proteins by cell density and nickel. J Cell Biochem 97: 1025-1035. 53. Salnikow K, Blagosklonny MV, Ryan H, Johnson R, Costa M (2000) Carcinogenic nickel induces genes involved with hypoxic stress. Cancer Res 60: 38-41. 54. Poksay KS, Banwait S, Crippen D, Mao X, Bredesen DE, et al. (2012) The small chaperone protein p23 and its cleaved product p19 in cellular stress. J Mol Neurosci 46: 303-314. 55. Marlowe JL, Puga A (2005) Aryl hydrocarbon receptor, cell cycle regulation, toxicity, and tumorigenesis. J Cell Biochem 96: 1174-1184. 56. Marlowe JL, Fan Y, Chang X, Peng L, Knudsen ES, et al. (2008) The aryl hydrocarbon receptor binds to E2F1 and inhibits E2F1-induced apoptosis. Mol Biol Cell 19: 3263-3271. 57. Brooks J, Eltom SE (2011) Malignant transformation of mammary epithelial cells by ectopic overexpression of the aryl hydrocarbon receptor. Curr Cancer Drug Targets 11: 654-669. 58. Abdelrahim M, Smith R, 3rd, Safe S (2003) Aryl hydrocarbon receptor gene silencing with small inhibitory RNA differentially modulates Ah-responsiveness in MCF-7 and HepG2 cancer cells. Mol Pharmacol 63: 1373-1381. 59. Denison MS, Nagy SR (2003) Activation of the aryl hydrocarbon receptor by structurally diverse exogenous and endogenous chemicals. Annu Rev Pharmacol Toxicol 43: 309-334. 60. Liehr JG (2000) Is estradiol a genotoxic mutagenic carcinogen? Endocr Rev 21: 40-54. 61. Askautrud HA, Gjernes E, Gunnes G, Sletten M, Ross DT, et al. (2014) Global gene expression analysis reveals a link between NDRG1 and vesicle transport. PLoS One 9: e87268. 62. Arias-Romero LE, Chernoff J (2013) Targeting Cdc42 in cancer. Expert Opin Ther Targets 17: 1263-1273. 63. He Z, Chen H, Li G, Zhu H, Gao Y, et al. (2014) Diosgenin inhibits the migration of human breast cancer MDA-MB-231 cells by suppressing Vav2 activity. Phytomedicine 21: 871-876. 64. Ma J, Xue Y, Liu W, Yue C, Bi F, et al. (2013) Role of activated rac1/cdc42 in mediating endothelial cell proliferation and tumor angiogenesis in breast cancer. PLoS One 8: e66275. 65. Prasad CP, Chaurasiya SK, Axelsson L, Andersson T (2013) WNT-5A triggers Cdc42 activation leading to an ERK1/2 dependent decrease in MMP9 activity and invasive migration of breast cancer cells. Mol Oncol 7: 870-883. 66. Su JL, Lin MT, Hong CC, Chang CC, Shiah SG, et al. (2005) Resveratrol induces FasL-related apoptosis through Cdc42 activation of ASK1/JNK-dependent signaling pathway in human leukemia HL-60 cells. Carcinogenesis 26: 1-10. 67. Choi YK, Seo HS, Choi HS, Choi HS, Kim SR, et al. (2012) Induction of Fas-mediated extrinsic apoptosis, p21WAF1-related G2/M cell cycle arrest and ROS generation by costunolide in estrogen receptor-negative breast cancer cells, MDA-MB-231. Mol Cell Biochem 363: 119-128. 68. Liang Z, Guo YT, Yi YJ, Wang RC, Hu QL, et al. (2014) Ganoderma lucidum polysaccharides target a fas/caspase dependent pathway to induce apoptosis in human colon cancer cells. Asian Pac J Cancer Prev 15: 3981-3986. 69. Lavrik IN (2014) Systems biology of death receptor networks: live and let die. Cell Death Dis 5: e1259. 70. Liu W, Xing F, Iiizumi-Gairani M, Okuda H, Watabe M, et al. (2012) N-myc downstream regulated gene 1 modulates Wnt-beta-catenin signalling and pleiotropically suppresses metastasis. EMBO Mol Med 4: 93-108. 71. Jung EU, Yoon JH, Lee YJ, Lee JH, Kim BH, et al. (2010) Hypoxia and retinoic acid-inducible NDRG1 expression is responsible for doxorubicin and retinoic acid resistance in hepatocellular carcinoma cells. Cancer Lett 298: 9-15. 72. Box AH, Demetrick DJ (2004) Cell cycle kinase inhibitor expression and hypoxia-induced cell cycle arrest in human cancer cell lines. Carcinogenesis 25: 2325-2335. 73. Goda N, Ryan HE, Khadivi B, McNulty W, Rickert RC, et al. (2003) Hypoxia-inducible factor 1alpha is essential for cell cycle arrest during hypoxia. Mol Cell Biol 23: 359-369. 74. McLeskey SW, Tobias CA, Vezza PR, Filie AC, Kern FG, et al. (1998) Tumor growth of FGF or VEGF transfected MCF-7 breast carcinoma cells correlates with density of specific microvessels independent of the transfected angiogenic factor. Am J Pathol 153: 1993-2006. 75. Sanna K, Rofstad EK (1994) Hypoxia-induced resistance to doxorubicin and methotrexate in human melanoma cell lines in vitro. Int J Cancer 58: 258-262. 76. Maruyama Y, Ono M, Kawahara A, Yokoyama T, Basaki Y, et al. (2006) Tumor growth suppression in pancreatic cancer by a putative metastasis suppressor gene Cap43/NDRG1/Drg-1 through modulation of angiogenesis. Cancer Res 66: 6233-6242. 77. Kim KJ, Li B, Winer J, Armanini M, Gillett N, et al. (1993) Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumour growth in vivo. Nature 362: 841-844. 78. Bandyopadhyay S, Pai SK, Hirota S, Hosobe S, Takano Y, et al. (2004) Role of the putative tumor metastasis suppressor gene Drg-1 in breast cancer progression. Oncogene 23: 5675-5681. 79. Han LL, Hou L, Zhou MJ, Ma ZL, Lin DL, et al. (2013) Aberrant NDRG1 methylation associated with its decreased expression and clinicopathological significance in breast cancer. J Biomed Sci 20: 52. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/57257 | - |
dc.description.abstract | 過去研究發現N-myc downstream-regulated gene 1 (NDRG1)會影響到許多癌症的發展,也在腫瘤適應氧濃度變化上扮演重要的角色。先前我們實驗室發現乳癌細胞株MCF-7中、NDRG1在缺氧刺激下會大量表現,同時芳香烴受體(aryl hydrocarbon receptor, AHR)的結合位點存在於NDRG1的啟動子上。然而,我們仍然不清楚缺氧調控NDRG1表現的機制以及NDRG1對乳癌細胞的影響,因此本篇的研究目的是探討芳香烴受體能否在調控NDRG1表現上、扮演轉錄因子的角色,並且了解在氧濃度變化下、NDRG1對癌細胞功能的影響。在缺氧濃度下,免疫螢光染色和染色質免疫沈澱法顯示芳香烴受體轉移至核內並結合到NDRG1啟動子(-412 ~ -388鹼基對)上。同時,過度表現芳香烴受體會藉由增進NDRG1表現來促進細胞的增生與遷移,然而利用小片段干擾核糖核酸機制抑制NDRG1表現後,細胞會減低成長與遷移。另一方面,在正常氧濃度下、過度表現NDRG1會抑制細胞的生長與遷移。過度表現NDRG1也會抑制腫瘤細胞在裸鼠體內的生長。此外,NDRG1在乳癌細胞株與腫瘤組織中亦有明顯下降的情形。總而言之,本研究顯示一個新的轉錄調控,即在缺氧刺激下、芳香烴受體會促進NDRG1表現量上升;並且顯示NDRG1在乳癌細胞的成長與遷移能力上、扮演動態調控的角色。 | zh_TW |
dc.description.abstract | N-myc downstream-regulated gene 1 (NDRG1) has been reported to regulate tumor progression in various cancers. In addition, it plays a critical role in tumor adaptation to fluctuation of oxygen concentrations. Previously, we showed that NDRG1 was strongly up-regulated under hypoxia in a breast cancer cell line MCF-7, and predicted to contain binding sites for aryl hydrocarbon receptor (AHR) at its promoter. However, the regulatory mechanism of NDRG1 expression under hypoxia and its cellular function remained elusive. Therefore, the aims of this study were to elucidate whether AHR could modulate NDRG1 expression, and to investigate the functional roles of NDRG1 upon changes in oxygen concentrations. In hypoxia, immunofluorescence staining and chromatin immunoprecipitation assays showed that AHR translocated to nuclei and bound to NDRG1 promoter (-412 ~ -388 bp). Also, over-expression of AHR facilitated cell proliferation and migration via up-regulation of NDRG1, whereas shRNA knockdown of NDRG1 reduced cell growth and motility. On the other hand, over-expression of NDRG1 under normoxia suppressed cell proliferation and migration ability. Tumor growth on the nude mice was also inhibited in cells over-expressed with NDRG1. Clinically, NDRG1 was down-regulated in breast cancer cell lines and tumor tissues. In summary, these results showed a novel mechanism of NDRG1 regulated by AHR upon hypoxic stress, and highlighted the dynamic role of NDRG1 in regulating cell growth and migration capacity during oxygen fluctuation in breast cancer. | en |
dc.description.provenance | Made available in DSpace on 2021-06-16T06:39:28Z (GMT). No. of bitstreams: 1 ntu-103-R01441013-1.pdf: 2221516 bytes, checksum: 069734857306fec6c7b39930169eff08 (MD5) Previous issue date: 2014 | en |
dc.description.tableofcontents | 目錄
中文摘要 I Abstract II Chapter 1 Introduction 1 1.1 Breast cancer and hypoxia 1 1.2 Cross-talk between the aryl hydrocarbon receptor and hypoxia pathways 2 1.3 Relationship between NDRG1 and hypoxia 3 1.4 The aim of study 4 Chapter 2 Materials and Methods 6 2.1 Cell culture and treatments 6 2.2 Plasmid construction 7 2.3 Transfection and stable transfected cells 8 2.4 RNA extraction and real-time RT-PCR 8 2.5 Western blot analysis 9 2.6 Immunofluorescence 10 2.7 Chromatin immunoprecipitation (ChIP) 10 2.8 Lentiviral production and infection 12 2.9 Cell counting kit-8 (CCK-8) assay 12 2.10 Cell cycle analysis 13 2.11 BrdU incorporation assay 13 2.12 Wound healing assay 14 2.13 Transwell migration assay 14 2.14 Tumor xenografts in nude mice 15 2.15 Immunohistochemistry 15 2.16 Microarray data analysis 16 Chapter 3 Results 17 3.1 AHR enhanced NDRG1 transcription under hypoxia through direct binding to its promoter site (-412 ~ -388 bp) 17 3.2 shRNA knockdown of NDRG1 suppressed cell proliferation and migration in hypoxic MCF-7 cells 20 3.3 shRNA knockdown of NDRG1 induced cell cycle arrest at G1 phase in hypoxia 23 3.4 Ectopic expression of AHR increased cell proliferation and migration through inducing NDRG1 expression in hypoxic MCF-7 cells 24 3.5 Ectopic expression of NDRG1 inhibited cell growth through enhancing apoptosis in normoxic MCF-7 cells 26 3.6 Ectopic expression of NDRG1 repressed cell motility in normoxic MCF-7 cells 28 3.7 Over-expression of NDRG1 attenuated tumor development in vivo 29 3.8 NDRG1 expression levels in breast cancer cell lines and tumor tissues 30 3.9 The differential expression levels of NDRG1 during oxygen fluctuation 32 Chapter 4 Discussion 33 4.1 The regulation of NDRG1 under hypoxia 33 4.2 AHR played a ligand-independent transcription factor to regulate NDRG1 under hypoxia 35 4.3 AHR and carcinogenesis 36 4.4 NDRG1 had different function in normoxia and hypoxia 37 4.5 NDRG1 served as a tumor suppressor in vivo 40 References 42 Supplementary Data 55 List of Figures Fig. 1 AHR translocated to nuclei and bound to NDRG1 promoter in CoCl2 and hypoxia treatment. 19 Fig. 2 shRNA knockdown of NDRG1 inhibited cell growth and cell migration under hypoxia. 22 Fig. 3 shRNA knockdown of NDRG1 induced cell cycle arrest under hypoxia. 24 Fig. 4 Over-expression of AHR increased cell growth and cell migration under hypoxia through targeting NDRG1. 26 Fig. 5 Over-expression of NDRG1 attenuated cell growth through induction of apoptosis. 28 Fig. 6 Over-expression of NDRG1 inhibited cell migration. 29 Fig. 7 Over-expression of NDRG1 suppressed the growth of subcutaneous xenograft tumors derived from MCF-7 cells in nude mice. 30 Fig. 8 NDRG1 was down-regulated in breast cancer cell lines and breast tumors. 31 Fig. 9 Relative expression levels of NDRG1 in different oxygen concentrations. 32 Fig. S1 Over-expression of NDRG1 reduced cell growth and migration in SKBR3 cells. 55 Fig. S2 Over-expression of NDRG1 decreased CD31 levels of subcutaneous xenograft tumors derived from MCF-7 cells in nude mice. 56 | |
dc.language.iso | en | |
dc.title | 探討乳癌細胞株MCF-7在常氧與缺氧下NDRG1對細胞功能的影響與受到的新轉錄調控 | zh_TW |
dc.title | Identification of the Cellular Function and a Novel Transcriptional Regulation of NDRG1 Under Normoxia and Hypoxia in MCF-7 Breast Cancer Cells | en |
dc.type | Thesis | |
dc.date.schoolyear | 102-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 莊曜宇,蔡孟勳,佘玉萍,阮雪芬 | |
dc.subject.keyword | 芳香烴受體,NDRG1,常氧,缺氧,乳癌, | zh_TW |
dc.subject.keyword | aryl hydrocarbon receptor,NDRG1,normoxia,hypoxia,breast cancer, | en |
dc.relation.page | 56 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2014-07-30 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 生理學研究所 | zh_TW |
顯示於系所單位: | 生理學科所 |
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