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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 楊泮池 | |
| dc.contributor.author | Abushinova Yulia | en |
| dc.contributor.author | 席玉瑄 | zh_TW |
| dc.date.accessioned | 2021-06-15T04:00:24Z | - |
| dc.date.available | 2010-03-12 | |
| dc.date.copyright | 2010-03-12 | |
| dc.date.issued | 2010 | |
| dc.date.submitted | 2010-02-26 | |
| dc.identifier.citation | 7. References
1. Travis, W.D., L.B. Travis, and S.S. Devesa, Lung cancer. Cancer,1995. 75(1 Suppl): p. 191-202. 2. Vaporciyan, A.A., Cancer Medicine. 2000. pp.1227-1292. 3. Edition, M.M.P., Lung Carcinoma: Tumor of Lungs. 4. Minna, J.D., Shiller, J.H, Harrison's Principles of Internal Medicine 17 ed. 2008: McGraw-Hill. pp.551-562. 5. Chen, J.J., et al., Global analysis of gene expression in invasion by a lung cancer model. Cancer Res, 2001. 61(13): p. 5223-30. 6. Shih, J.Y., et al., Transcription repressor slug promotes carcinoma invasion and predicts outcome of patients with lung adenocarcinoma. Clin Cancer Res, 2005. 11(22): p. 8070-8. 7. Shih, J.Y., et al., Collapsin response mediator protein-1 and the invasion and metastasis of cancer cells. J Natl Cancer Inst, 2001. 93(18): p. 1392-400. 8. Sepulveda, J.L. and C. Wu, The parvins. Cell Mol Life Sci, 2006. 63(1): p. 25-35. 9. Fukuda, T., et al., PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival. Journal of Biological Chemistry, 2003. 278(51): p. 51324-51333. 10. Zhang, Y., et al., Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival. Journal of Biological Chemistry, 2004. 279(40): p. 41695-705. 11. Fukuda, T., et al., CH-ILKBP regulates cell survival by facilitating the membrane translocation of protein kinase B/Akt. J Cell Biol, 2003. 160(7): p. 1001-8. 12. Wu, C. and S. Dedhar, Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes. J Cell Biol, 2001. 155(4): p. 505-10. 13. Delcommenne, M., et al., Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc Natl Acad Sci U S A, 1998. 95(19): p. 11211-6. 14. Wu, C., et al., The PINCH-ILK-parvin complexes: assembly, functions and regulation. Biochim Biophys Acta, 2004. 1692(2): p. 55-62. 15. Chung, D.H., et al., ILK (beta1-integrin-linked protein kinase): a novel immunohistochemical marker for Ewing's sarcoma and primitive neuroectodermal tumour. Virchows Arch, 1998. 433(2): p. 113-7. 16. Wu, C., et al., Integrin-linked protein kinase regulates fibronectin matrix assembly, E-cadherin expression, and tumorigenicity. J Biol Chem, 1998. 273(1): p. 528-36. 17. Graff, J.R., et al., Integrin-linked kinase expression increases with prostate tumor grade. Clin Cancer Res, 2001. 7(7): p. 1987-91. 18. Ito, R., et all., Expression of integrin-linked kinase is closely correlated with invasion and metastasis of gastric carcinoma. Virchows Arch, 2003. 442(2): p.118-123. 19. Persad, S. and S. Dedhar, The role of integrin-linked kinase (ILK) in cancer progression. Cancer Metastasis Rev, 2003. 22(4): p. 375-84. 20 Geiger, B. and Bershadsky, A., Assembly and mechanosensory function of focal contacts. Curr Opin Cell Biol, 2001. 13(5): p.584-592 21. Papachristou, D.J., et al., Expression of integrin-linked kinase and its binding partners in chondrosarcoma: association with prognostic significance. Eur J Cancer, 2008. 44(16): p. 2518-25. 22. Li, L., et al., Correlation of growth capacity of human tumor cells in hard agarose with their in vivo proliferative capacity at specific metastatic sites. J Natl Cancer Inst, 1989. 81(18): p. 1406-12. 23. Takanami, I., Increased expression of integrin-linked kinase is associated with shorter survival in non-small cell lung cancer. BMC Cancer, 2005. 5: p. 1. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/44985 | - |
| dc.description.abstract | Background: PARVA - is a member of parvin family of actin–binding proteins, which is involved in linkage of integrins and association with intracellular proteins that regulate actin cytoskeleton dynamics and cell survival. Recent studies indicated that PARVA is critical for survival for cell survival in a variety of cells, including certain cancer cells, kidney podocytes and cardiac myocytes, and may be involved in malignant transformation of chondroblasts. Therefore we investigated the role of PARVA in lung cancer progression.
Methods: We established the PARVA overexpressed cells in human lung cancer cell line CL1-0 with lower invasive potential compared to CL1-5. Then we analyzed cell anchorage-independent growth, colony formation, proliferation, cell migration, invasion and in vivo metastasis of cell transfectants. Results: PARVA expression might be positively correlated with metastatic potential of lung cancer cells and overexpressed in the highly invasive cell line CL1-5. PARVA enhances migration and invasion potential of lung cancer cells in vitro and in vivo metastasis, but is not involved in the regulation of anchorage–independent growth, tumorigenecity and tumor growth. Conclusion: PARVA showed an oncogenic role in adenocarcinoma of NSCLC consistently with its previously reported role in chondrosarcomas. Our study indicated that the role of PARVA in lung cancer progression was characterized PARVA as metastasis promoting gene. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T04:00:24Z (GMT). No. of bitstreams: 1 ntu-99-R95448015-1.pdf: 1297624 bytes, checksum: dbb47a51a6548d4fca28138b47cd4df3 (MD5) Previous issue date: 2010 | en |
| dc.description.tableofcontents | 口試委員會審訂書……………………………………………………………………I
英文摘要…………………………………………………………………………..….II Table of content……………………………………………………………….....IV 1.Introduction...........................................................................................................1 1.1 Lung cancer.....................................................................................................................1 1.2 Metastasis and clinical limit..........................................................................................1 1.3 Genes and cancer progression.......................................................................................2 1.4 α-parvin (PARVA) - is a member of parvin family of actin–binding proteins……3 1.5 α-parvin, ILK and cancer..............................................................................................6 2.Results......................................................................................................................8 2.1 PARVA expression is higher in CL 1-5 than in CL 1-0…………………………...8 2.2 Transfection of PARVA cDNA and selection of stable clones…………………….9 2.3 PARVA enhances invasion and migration of lung cancer cells……………………9 2.4 PARVA is not involved in cell anchorage-independent growth, colony formation and proliferation………………………………………………………10 2.5 PARVA enhances lung cancer cell metastasis in vivo…………………………....11 3. Discussion………………………………………………………………………12 4. Materials and Methods…………………………………………………...14 4.1 Cell lines and culture conditions………………………………………………....14 4.2 Total RNA isolation…………………………………………………………..….14 4.3 Construction of expression vector and stable transfection………………………15 4.4 Western blot……………………………………………………………………...16 4.5 Quantitative real-time PCR………………………………………………………17 4.6 Migration and invasion assays…………………………………………………...17 4.7 Anchorage –independent growth assay………………………………………….18 4.8 Anchorage- depended growth……………………………………………............18 4.9 MTT cell proliferation…………………………………………………………...19 4.10 In vivo metastasis assay………………………………………………………...19 5.Figures………………………………………………………………...21 Figure 1. The expression of PARVA positively correlated with the invasion activity in lung cancer cells…………………………………………………21 Figure 2. Overexpression of PARVA in CL1-0………………..…………………......23 Figure 3. The effect of PARVA expression on in vitro invasion and migration of lung cancer cells……………………………………………..25 Figure 4.Overexpression of PARVA did not affect cells tumorigenecity in vitro, anchorage-dependent growth and proliferation…………………………….27 Figure 5. PARVA enhances cell metastasis in vivo…………………………………..29 6.Appendix………………………………………………………………………..32 6.1.Flow chart………………………………………………………………………..32 6.2.Structural features of PARVA protein…………………………………………..32 7.References………………………………………………………………………34 | |
| dc.language.iso | en | |
| dc.subject | NSCLC | zh_TW |
| dc.subject | PARVA | zh_TW |
| dc.subject | PARVA | en |
| dc.subject | invasion | en |
| dc.subject | metastasis | en |
| dc.subject | NSCLC | en |
| dc.subject | adenocarcinoma | en |
| dc.title | PARVA基因在非小細胞肺癌的致癌機制 | zh_TW |
| dc.title | Oncogenic Role of PARVA Gene in Non-Small Cell Lung Carcinoma | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 98-1 | |
| dc.description.degree | 碩士 | |
| dc.contributor.coadvisor | 俞松良,李芳仁 | |
| dc.contributor.oralexamcommittee | #VALUE! | |
| dc.subject.keyword | PARVA,NSCLC, | zh_TW |
| dc.subject.keyword | PARVA,NSCLC,metastasis,invasion,adenocarcinoma, | en |
| dc.relation.page | 35 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2010-02-26 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 分子醫學研究所 | zh_TW |
| 顯示於系所單位： | 分子醫學研究所 | |
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