請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/74165
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 阮雪芬 | |
dc.contributor.author | Chia-Chi Wang | en |
dc.contributor.author | 王嘉琪 | zh_TW |
dc.date.accessioned | 2021-06-17T08:22:34Z | - |
dc.date.available | 2024-08-20 | |
dc.date.copyright | 2019-08-20 | |
dc.date.issued | 2019 | |
dc.date.submitted | 2019-08-13 | |
dc.identifier.citation | 1. Wang, L. H., Li, Y., Yang, S. N., Wang, F. Y., Hou, Y., Cui, W., Chen, K., Cao, Q., Wang, S., Zhang, T. Y., Wang, Z. Z., Xiao, W., Yang, J. Y., and Wu, C. F. (2014) Gambogic acid synergistically potentiates cisplatin-induced apoptosis in non-small-cell lung cancer through suppressing NF-kappaB and MAPK/HO-1 signalling. Br J Cancer 110, 341-352.
2. Ali, A., Goffin, J. R., Arnold, A., and Ellis, P. M. (2013) Survival of patients with non-small-cell lung cancer after a diagnosis of brain metastases. Curr Oncol 20, e300-e306. 3. Omenn, G. S., Goodman, G. E., Thornquist, M. D., Balmes, J., Cullen, M. R., Glass, A., Keogh, J. P., Meyskens, F. L., Jr., Valanis, B., Williams, J. H., Jr., Barnhart, S., Cherniack, M. G., Brodkin, C. A., and Hammar, S. (1996) Risk Factors for Lung Cancer and for Intervention Effects in CARET, the Beta-Carotene and Retinol Efficacy Trial. J Natl Cancer Inst 88, 1550-1559. 4. Wender, R., Fontham, E. T. H., Barrera Jr, E., Colditz, G. A., Church, T. R., Ettinger, D. S., Etzioni, R., Flowers, C. R., Scott Gazelle, G., Kelsey, D. K., LaMonte, S. J., Michaelson, J. S., Oeffinger, K. C., Shih, Y.-C. T., Sullivan, D. C., Travis, W., Walter, L., Wolf, A. M. D., Brawley, O. W., and Smith, R. A. (2013) American Cancer Society lung cancer screening guidelines. CA Cancer J Clin 63, 106-117. 5. Posther, K. E., and Harpole, D. H. (2006) The Surgical Management of Lung Cancer. Cancer Invest 24, 56-67. 6. Ullah, I., Subbarao, R. B., and Rho, G. J. (2015) Human mesenchymal stem cells - current trends and future prospective. Biosci Rep 35. 7. Wei, X., Yang, X., Han, Z. P., Qu, F. F., Shao, L., and Shi, Y. F. (2013) Mesenchymal stem cells: a new trend for cell therapy. Acta Pharmacol Sin 34, 747-754. 8. Pittenger, M. F. (1999) Multilineage Potential of Adult Human Mesenchymal Stem Cells. Science 284, 143-147. 9. Mahla, R. S. (2016) Stem Cells Applications in Regenerative Medicine and Disease Therapeutics. Int J Cell Biol 2016, 6940283. 10. Ankrum, J. A., Ong, J. F., and Karp, J. M. (2014) Mesenchymal stem cells: immune evasive, not immune privileged. Nat Biotechnol 32, 252-260. 11. Gregory, C. A., Prockop, D. J., and Spees, J. L. (2005) Non-hematopoietic bone marrow stem cells: Molecular control of expansion and differentiation. Exp Cell Res 306, 330-335. 12. Wagner, W., Wein, F., Seckinger, A., Frankhauser, M., Wirkner, U., Krause, U., Blake, J., Schwager, C., Eckstein, V., Ansorge, W., and Ho, A. D. (2005) Comparative characteristics of mesenchymal stem cells from human bone marrow, adipose tissue, and umbilical cord blood. Exp Hematol 33, 1402-1416. 13. Tsai, M. S., Lee, J. L., Chang, Y. J., and Hwang, S. M. (2004) Isolation of human multipotent mesenchymal stem cells from second-trimester amniotic fluid using a novel two-stage culture protocol. Hum Reprod 19, 1450-1456. 14. Seifrtová, M., Havelek, R., Ćmielová, J., Jiroutová, A., Soukup, T., Brůčková, L., Mokrý, J., English, D., and Řezáčová, M. (2012) The response of human ectomesenchymal dental pulp stem cells to cisplatin treatment. Int Endod J 45, 401-412. 15. Jiao, F., Wang, J., Dong, Z. L., Wu, M. J., Zhao, T. B., Li, D. D., and Wang, X. (2012) Human mesenchymal stem cells derived from limb bud can differentiate into all three embryonic germ layers lineages. Cell Reprogram 14, 324-333. 16. Kita, K., Gauglitz, G. G., Phan, T. T., Herndon, D. N., and Jeschke, M. G. (2010) Isolation and Characterization of Mesenchymal Stem Cells From the Sub-Amniotic Human Umbilical Cord Lining Membrane. Stem Cells Dev 19, 491-502. 17. Schüring, A. N., Schulte, N., Kelsch, R., Röpke, A., Kiesel, L., and Götte, M. (2011) Characterization of endometrial mesenchymal stem-like cells obtained by endometrial biopsy during routine diagnostics. Fertil Steril 95, 423-426. 18. Pendleton, C., Li, Q., Chesler, D. A., Yuan, K., Guerrero-Cazares, H., and Quinones-Hinojosa, A. (2013) Mesenchymal Stem Cells Derived from Adipose Tissue vs Bone Marrow: In Vitro Comparison of Their Tropism towards Gliomas. PLoS One 8, e58198. 19. Thirumala, S., Goebel, W. S., and Woods, E. J. (2009) Clinical grade adult stem cell banking. Organogenesis 5, 143-154. 20. Sibov, T. T., Severino, P., Marti, L. C., Pavon, L. F., Oliveira, D. M., Tobo, P. R., Campos, A. H., Paes, A. T., Amaro, E., Jr., L, F. G., and Moreira-Filho, C. A. (2012) Mesenchymal stem cells from umbilical cord blood: parameters for isolation, characterization and adipogenic differentiation. Cytotechnology 64, 511-521. 21. Bieback, K., Kern, S., Klüter, H., and Eichler, H. (2004) Critical Parameters for the Isolation of Mesenchymal Stem Cells from Umbilical Cord Blood. Stem Cells 22, 625-634. 22. Erices, A., Conget, P., and Minguell, J. J. (2000) Mesenchymal progenitor cells in human umbilical cord blood. Br J Haematol 109, 235-242. 23. Gang, E. J., Hong, S. H., Jeong, J. A., Hwang, S. H., Kim, S. W., Yang, I. I. H., Ahn, C., Han, H., and Kim, H. (2004) In vitro mesengenic potential of human umbilical cord blood-derived mesenchymal stem cells. Biochem Biophys Res Commun 321, 102-108. 24. Lee, M. W., Choi, J., Yang, M. S., Moon, Y. J., Park, J. S., Kim, H. C., and Kim, Y. J. (2004) Mesenchymal stem cells from cryopreserved human umbilical cord blood. Biochem Biophys Res Commun 320, 273-278. 25. Chamberlain, G., Fox, J., Ashton, B., and Middleton, J. (2007) Concise Review: Mesenchymal Stem Cells: Their Phenotype, Differentiation Capacity, Immunological Features, and Potential for Homing. Stem Cells 25, 2739-2749. 26. Ridge, S. M., Sullivan, F. J., and Glynn, S. A. (2017) Mesenchymal stem cells: key players in cancer progression. Mol Cancer 16, 31. 27. Karnoub, A. E., Dash, A. B., Vo, A. P., Sullivan, A., Brooks, M. W., Bell, G. W., Richardson, A. L., Polyak, K., Tubo, R., and Weinberg, R. A. (2007) Mesenchymal stem cells within tumour stroma promote breast cancer metastasis. Nature 449, 557. 28. Nabha, S. M., dos Santos, E. B., Yamamoto, H. A., Belizi, A., Dong, Z., Meng, H., Saliganan, A., Sabbota, A., Bonfil, R. D., and Cher, M. L. (2008) Bone marrow stromal cells enhance prostate cancer cell invasion through type I collagen in an MMP-12 dependent manner. Int J Cancer 122, 2482-2490. 29. Prantl, L., Muehlberg, F., Navone, N. M., Song, Y.-H., Vykoukal, J., Logothetis, C. J., and Alt, E. U. (2010) Adipose tissue-derived stem cells promote prostate tumor growth. Prostate 70, 1709-1715. 30. Kucerova, L., Matuskova, M., Hlubinova, K., Altanerova, V., and Altaner, C. (2010) Tumor cell behaviour modulation by mesenchymal stromal cells. Mol Cancer 9, 129. 31. Bussard, K. M., Mutkus, L., Stumpf, K., Gomez-Manzano, C., and Marini, F. C. (2016) Tumor-associated stromal cells as key contributors to the tumor microenvironment. Breast Cancer Res 18, 84. 32. Yuan, Y., Jiang, Y. C., Sun, C. K., and Chen, Q. M. (2016) Role of the tumor microenvironment in tumor progression and the clinical applications. Oncol Rep 35, 2499-2515. 33. Whiteside, T. L. (2008) The tumor microenvironment and its role in promoting tumor growth. Oncogene 27, 5904-5912. 34. Spaeth, E. L., Dembinski, J. L., Sasser, A. K., Watson, K., Klopp, A., Hall, B., Andreeff, M., and Marini, F. (2009) Mesenchymal stem cell transition to tumor-associated fibroblasts contributes to fibrovascular network expansion and tumor progression. PLoS One 4, e4992. 35. Wang, M., Zhao, J., Zhang, L., Wei, F., Lian, Y., Wu, Y., Gong, Z., Zhang, S., Zhou, J., and Cao, K. (2017) Role of tumor microenvironment in tumorigenesis. J Cancer 8, 761. 36. Leonardi, G. C., Candido, S., Cervello, M., Nicolosi, D., Raiti, F., Travali, S., Spandidos, D. A., and Libra, M. (2012) The tumor microenvironment in hepatocellular carcinoma (review). Int J Oncol 40, 1733-1747. 37. Yu, Y., Xiao, C. H., Tan, L. D., Wang, Q. S., Li, X. Q., and Feng, Y. M. (2013) Cancer-associated fibroblasts induce epithelial–mesenchymal transition of breast cancer cells through paracrine TGF-β signalling. Br J Cancer 110, 724. 38. Mishra, P. J., Mishra, P. J., Humeniuk, R., Medina, D. J., Alexe, G., Mesirov, J. P., Ganesan, S., Glod, J. W., and Banerjee, D. (2008) Carcinoma-Associated Fibroblast–Like Differentiation of Human Mesenchymal Stem Cells. Cancer Res 68, 4331-4339. 39. Jotzu, C., Alt, E., Welte, G., Li, J., Hennessy, B. T., Devarajan, E., Krishnappa, S., Pinilla, S., Droll, L., and Song, Y.-H. (2010) Adipose Tissue-Derived Stem Cells Differentiate into Carcinoma-Associated Fibroblast-Like Cells under the Influence of Tumor-Derived Factors. Anal Cell Pathol 33. 40. Krawiec, J. T., Liao, H.-T., Kwan, L., D'Amore, A., Weinbaum, J. S., Rubin, J. P., Wagner, W. R., and Vorp, D. A. (2017) Evaluation of the stromal vascular fraction of adipose tissue as the basis for a stem cell-based tissue-engineered vascular graft. J Vasc Surg 66, 883-890.e881. 41. Zhu, Q., Zhang, X., Zhang, L., Li, W., Wu, H., Yuan, X., Mao, F., Wang, M., Zhu, W., Qian, H., and Xu, W. (2014) The IL-6–STAT3 axis mediates a reciprocal crosstalk between cancer-derived mesenchymal stem cells and neutrophils to synergistically prompt gastric cancer progression. Cell Death Dis 5, e1295. 42. Nwabo Kamdje, A. H., Kamga, P. T., Simo, R. T., Vecchio, L., Seke Etet, P. F., Muller, J. M., Bassi, G., Lukong, E., Goel, R. K., Amvene, J. M., and Krampera, M. (2017) Mesenchymal stromal cells' role in tumor microenvironment: involvement of signaling pathways. Cancer Biol Med 14, 129-141. 43. Sun, Z., Wang, S., and Zhao, R. C. (2014) The roles of mesenchymal stem cells in tumor inflammatory microenvironment. J Hematol Oncol 7, 14-14. 44. Trivanovic, D., Krstic, J., Djordjevic, I. O., Mojsilovic, S., Santibanez, J. F., Bugarski, D., and Jaukovic, A. (2016) The Roles of Mesenchymal Stromal/Stem Cells in Tumor Microenvironment Associated with Inflammation. Mediators Inflamm 2016, 7314016. 45. Zhang, W., and Liu, H. T. J. C. r. (2002) MAPK signal pathways in the regulation of cell proliferation in mammalian cells. Cell Res 12, 9. 46. Morrison, D. K. (2012) MAP kinase pathways. Cold Spring Harb Perspect Biol 4. 47. Wang, J., Pan, C., Wang, Y., Ye, L., Wu, J., Chen, L., Zou, T., and Lu, G. (2015) Genome-wide identification of MAPK, MAPKK, and MAPKKK gene families and transcriptional profiling analysis during development and stress response in cucumber. BMC Genomics 16, 386. 48. Roux, P. P., and Blenis, J. (2004) ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol Mol Biol Rev 68, 320-344. 49. Kohno, M., and Pouyssegur, J. (2006) Targeting the ERK signaling pathway in cancer therapy. Ann Med 38, 200-211. 50. McKay, M. M., and Morrison, D. K. (2007) Integrating signals from RTKs to ERK/MAPK. Oncogene 26, 3113-3121. 51. Chang, F., Steelman, L. S., Lee, J. T., Shelton, J. G., Navolanic, P. M., Blalock, W. L., Franklin, R. A., and McCubrey, J. A. (2003) Signal transduction mediated by the Ras/Raf/MEK/ERK pathway from cytokine receptors to transcription factors: potential targeting for therapeutic intervention. Leukemia 17, 1263-1293. 52. Basset-Séguin, N., Escot, C., Molès, J. P., Blanchard, J. M., Kerai, C., and Guilhou, J. J. (1991) C-fos and c-jun Proto-Oncogene Expression Is Decreased in Psoriasis: an In Situ Quantitative Analysis. J Invest Dermatol 97, 672-678. 53. Milde-Langosch, K. (2005) The Fos family of transcription factors and their role in tumourigenesis. Eur J Cancer 41, 2449-2461. 54. Chiu, R., Boyle, W. J., Meek, J., Smeal, T., Hunter, T., and Karin, M. (1988) The c-fos protein interacts with c-Jun/AP-1 to stimulate transcription of AP-1 responsive genes. Cell 54, 541-552. 55. Angel, P., and Karin, M. (1991) The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation. Biochim Biophys Acta 1072, 129-157. 56. Ameyar, M., Wisniewska, M., and Weitzman, J. B. (2003) A role for AP-1 in apoptosis: the case for and against. Biochimie 85, 747-752. 57. Tulchinsky, E. (2000) Fos family members: regulation, structure and role in oncogenic transformation Histol Histopathol 15, 921-928. 58. Fialka, I. (1996) The estrogen-dependent c-JunER protein causes a reversible loss of mammary epithelial cell polarity involving a destabilization of adherens junctions. J Cell Biol 132, 1115-1132. 59. Yoshida, M., Muneyuki, E., and Hisabori, T. (2001) ATP synthase — a marvellous rotary engine of the cell. Nat Rev Mol Cell Biol 2, 669. 60. Jonckheere, A. I., Smeitink, J. A., and Rodenburg, R. J. (2012) Mitochondrial ATP synthase: architecture, function and pathology. J Inherit Metab Dis 35, 211-225. 61. Guo, H., Bueler, S. A., and Rubinstein, J. L. (2017) Atomic model for the dimeric FO region of mitochondrial ATP synthase. Science 358, 936-940. 62. Velours, J., Paumard, P., Soubannier, V., Spannagel, C., Vaillier, J., Arselin, G., and Graves, P.-V. (2000) Organisation of the yeast ATP synthase F0:a study based on cysteine mutants, thiol modification and cross-linking reagents. Biochim Biophys Acta 1458, 443-456. 63. Ma, Z., Cao, M., Liu, Y., He, Y., Wang, Y., Yang, C., Wang, W., Du, Y., Zhou, M., and Gao, F. (2010) Mitochondrial F1Fo-ATP synthase translocates to cell surface in hepatocytes and has high activity in tumor-like acidic and hypoxic environment. Acta Biochim Biophys Sin 42, 530-537. 64. Chang, H. Y., Huang, H. C., Huang, T. C., Yang, P. C., Wang, Y. C., and Juan, H. F. (2012) Ectopic ATP synthase blockade suppresses lung adenocarcinoma growth by activating the unfolded protein response. Cancer Res 72, 4696-4706. 65. Chi, S. L., Wahl, M. L., Mowery, Y. M., Shan, S., Mukhopadhyay, S., Hilderbrand, S. C., Kenan, D. J., Lipes, B. D., Johnson, C. E., Marusich, M. F., Capaldi, R. A., Dewhirst, M. W., and Pizzo, S. V. (2007) Angiostatin-like activity of a monoclonal antibody to the catalytic subunit of F1F0 ATP synthase. Cancer Res 67, 4716-4724. 66. Zhang, X., Gao, F., Yu, L. L., Peng, Y., Liu, H. H., Liu, J. Y., Yin, M., and Ni, J. (2008) Dual functions of a monoclonal antibody against cell surface F1F0 ATP synthase on both HUVEC and tumor cells. Acta Pharmacol Sin 29, 942-950. 67. Burnstock, G. (1972) Purinergic Nerves. Pharmacol Rev 24, 509-581. 68. Ralevic, V., and Burnstock, G. (1998) Receptors for Purines and Pyrimidines. Pharmacol Rev 50, 413-492. 69. Burnstock, G., and Kennedy, C. (1985) Is there a basis for distinguishing two types of P2-purinoceptor? Gen Pharmacol 16, 433-440. 70. Webb, T. E., Simon, J., Krishek, B. J., Bateson, A. N., Smart, T. G., King, B. F., Burnstock, G., and Barnard, E. A. (1993) Cloning and functional expression of a brain G-protein-coupled ATP receptor. FEBS J 324, 219-225. 71. Geoffrey, B. (2004) Introduction: P2 Receptors. Curr Top Med Chem 4, 793-803. 72. Burnstock, G., and Knight, G. E. (2004) Cellular Distribution and Functions of P2 Receptor Subtypes in Different Systems. Int Rev Cytol 240, 31-304. 73. Burnstock, G. (2006) Purinergic signalling. Br J Pharmacol 147 Suppl 1, S172-181. 74. Burnstock, G., and Di Virgilio, F. (2013) Purinergic signalling and cancer. Purinergic Signal 9, 491-540. 75. Vizi, E. S., and Burnstock, G. (1988) Origin of ATP release in the rat vas deferens: Concomitant measurement of [3H]noradrenaline and [14C]ATP. Eur J Pharmacol 158, 69-77. 76. Sperlagh, B., and Vizi, E. S. (1991) Effect of Presynaptic P2 Receptor Stimulation on Transmitter Release. J Neurochem 56, 1466-1470. 77. Vizi, E. S., Liang, S. D., Sperlágh, B., Kittel, Á., and Jurányi, Z. (1997) Studies on the release and extracellular metabolism of endogenous ATP in rat superior cervical ganglion: support for neurotransmitter role of ATP. Neuroscience 79, 893-903. 78. Vizi, E. S., Sperlágh, B., and Baranyi, M. (1992) Evidence that ATP, released from the postsynaptic site by noradrenaline, is involved in mechanical responses of guinea-pig vas deferens: Cascade transmission. Neuroscience 50, 455-465. 79. Burnstock, G. (2006) Purinergic Signalling—An Overview. In: Goode, D. J. C. a. J., ed. Purinergic Signalling in Neuron–Glia Interactions. 80. Di Virgilio, F., Sarti, A. C., Falzoni, S., De Marchi, E., and Adinolfi, E. (2018) Extracellular ATP and P2 purinergic signalling in the tumour microenvironment. Nat Rev Cancer 18, 601-618. 81. Di Virgilio, F. (2012) Purines, purinergic receptors, and cancer. Cancer Res 72, 5441-5447. 82. Kepp, O., Loos, F., Liu, P., and Kroemer, G. (2017) Extracellular nucleosides and nucleotides as immunomodulators. Immuno Rev 280, 83-92. 83. Di Virgilio, F., and Adinolfi, E. (2016) Extracellular purines, purinergic receptors and tumor growth. Oncogene 36, 293. 84. Idzko, M., Ferrari, D., and Eltzschig, H. K. (2014) Nucleotide signalling during inflammation. Nature 509, 310. 85. Di Virgilio, F., Dal Ben, D., Sarti, A. C., Giuliani, A. L., and Falzoni, S. (2017) The P2X7 Receptor in Infection and Inflammation. Immunity 47, 15-31. 86. North, R. A. (2002) Molecular Physiology of P2X Receptors. Physiol Rev 82, 1013-1067. 87. Pellegatti, P., Raffaghello, L., Bianchi, G., Piccardi, F., Pistoia, V., and Di Virgilio, F. (2008) Increased Level of Extracellular ATP at Tumor Sites: In Vivo Imaging with Plasma Membrane Luciferase. PLoS One 3, e2599. 88. Baricordi, O. R., Melchiorri, L., Adinolfi, E., Falzoni, S., Chiozzi, P., Buell, G., and Di Virgilio, F. (1999) Increased Proliferation Rate of Lymphoid Cells Transfected with the P2X7 ATP Receptor. J Biol Chem 274, 33206-33208. 89. Adinolfi, E., Callegari, M. G., Ferrari, D., Bolognesi, C., Minelli, M., Wieckowski, M. R., Pinton, P., Rizzuto, R., and Di Virgilio, F. (2005) Basal activation of the P2X7 ATP receptor elevates mitochondrial calcium and potential, increases cellular ATP levels, and promotes serum-independent growth. Mol Biol Cell 16, 3260-3272. 90. Vázquez-Cuevas, F. G., Martínez-Ramírez, A. S., Robles-Martínez, L., Garay, E., García-Carrancá, A., Pérez-Montiel, D., Castañeda-García, C., and Arellano, R. O. (2014) Paracrine Stimulation of P2X7 Receptor by ATP Activates a Proliferative Pathway in Ovarian Carcinoma Cells. J Cell Biochem 115, 1955-1966. 91. Chen, S., Ma, Q., Krafft, P. R., Chen, Y., Tang, J., Zhang, J., and Zhang, J. H. (2013) P2X7 receptor antagonism inhibits p38 mitogen-activated protein kinase activation and ameliorates neuronal apoptosis after subarachnoid hemorrhage in rats. Crit Care Med 41, e466-e474. 92. Young, C. N. J., and Górecki, D. C. (2018) P2RX7 Purinoceptor as a Therapeutic Target-The Second Coming? Front Chem 6, 248-248. 93. Nuka, E., Ohnishi, K., Terao, J., and Kawai, Y. (2018) ATP/P2X7 receptor signaling as a potential anti-inflammatory target of natural polyphenols. PLoS One 13, e0204229-e0204229. 94. Di Virgilio, F., Falzoni, S., Giuliani, A. L., and Adinolfi, E. (2016) P2 receptors in cancer progression and metastatic spreading. Curr Opin Pharmacol 29, 17-25. 95. Gu, B. J., and Wiley, J. S. (2006) Rapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor. Blood 107, 4946-4953. 96. Adinolfi, E., Cirillo, M., Woltersdorf, R., Falzoni, S., Chiozzi, P., Pellegatti, P., Callegari, M. G., Sandonà, D., Markwardt, F., Schmalzing, G., and Virgilio, F. D. (2010) Trophic activity of a naturally occurring truncated isoform of the P2X7 receptor. FASEB J 24, 3393-3404. 97. Jelassi, B., Chantôme, A., Alcaraz-Pérez, F., Baroja-Mazo, A., Cayuela, M. L., Pelegrin, P., Surprenant, A., and Roger, S. (2011) P2X7 receptor activation enhances SK3 channels- and cystein cathepsin-dependent cancer cells invasiveness. Oncogene 30, 2108. 98. Xia, J., Yu, X., Tang, L., Li, G., and He, T. (2015) P2X7 receptor stimulates breast cancer cell invasion and migration via the AKT pathway. Oncol Rep 34, 103-110. 99. Moller, D. E., Xia, C. H., Tang, W., Zhu, A. X., and Jakubowski, M. (1994) Human rsk isoforms: cloning and characterization of tissue-specific expression. Am J Physiol 266, C351-C359. 100. Roux, P. P., Richards, S. A., and Blenis, J. (2003) Phosphorylation of p90 Ribosomal S6 Kinase (RSK) Regulates Extracellular Signal-Regulated Kinase Docking and RSK Activity. Mol Cell Biol 23, 4796-4804. 101. Zhou, Y., Yamada, N., Tanaka, T., Hori, T., Yokoyama, S., Hayakawa, Y., Yano, S., Fukuoka, J., Koizumi, K., Saiki, I., and Sakurai, H. (2015) Crucial roles of RSK in cell motility by catalysing serine phosphorylation of EphA2. Nat Commun 6, 7679. 102. Sun, Y., Liu, W. Z., Liu, T., Feng, X., Yang, N., and Zhou, H. F. (2015) Signaling pathway of MAPK/ERK in cell proliferation, differentiation, migration, senescence and apoptosis. J Recept Signal Transduct Res 35, 600-604. 103. Kake, S., Usui, T., Ohama, T., Yamawaki, H., and Sato, K. (2017) Death-associated protein kinase 3 controls the tumor progression of A549 cells through ERK MAPK/c-Myc signaling. Oncol Rep 37, 1100-1106. 104. Zhou, Q., Gui, S., Zhou, Q., and Wang, Y. (2014) Melatonin inhibits the migration of human lung adenocarcinoma A549 cell lines involving JNK/MAPK pathway. PLoS One 9, e101132. 105. Okazaki, K., and Sagata, N. (1995) The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J 14, 5048-5059. 106. Deng, T., and Karin, M. (1994) c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK. Nature 371, 171-175. 107. Gupta, S., Campbell, D., Derijard, B., and Davis, R. J. (1995) Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science 267, 389. 108. Bianchi, G., Vuerich, M., Pellegatti, P., Marimpietri, D., Emionite, L., Marigo, I., Bronte, V., Di Virgilio, F., Pistoia, V., and Raffaghello, L. (2014) ATP/P2X7 axis modulates myeloid-derived suppressor cell functions in neuroblastoma microenvironment. Cell Death Dis 5, e1135. 109. Maffey, A., Storini, C., Diceglie, C., Martelli, C., Sironi, L., Calzarossa, C., Tonna, N., Lovchik, R., Delamarche, E., Ottobrini, L., and Bianco, F. (2017) Mesenchymal stem cells from tumor microenvironment favour breast cancer stem cell proliferation, cancerogenic and metastatic potential, via ionotropic purinergic signalling. Sci Rep 7, 13162. 110. Cao, Y. J. C., and Bioscience (2017) Tumorigenesis as a process of gradual loss of original cell identity and gain of properties of neural precursor/progenitor cells. Cell Biosci 7, 61. 111. Hanahan, D., and Weinberg, R. A. (2011) Hallmarks of cancer: the next generation. Cell 144, 646-674. 112. Hanahan, D., and Weinberg, R. A. (2000) The hallmarks of cancer. Cell 100, 57-70. 113. Giraldo, N. A., Sanchez-Salas, R., Peske, J. D., Vano, Y., Becht, E., Petitprez, F., Validire, P., Ingels, A., Cathelineau, X., Fridman, W. H., and Sautès-Fridman, C. (2019) The clinical role of the TME in solid cancer. Br J Cancer 120, 45-53. 114. Hanahan, D., and Coussens, L. M. (2012) Accessories to the crime: functions of cells recruited to the tumor microenvironment. Cancer Cell 21, 309-322. 115. Cirri, P., and Chiarugi, P. (2011) Cancer associated fibroblasts: the dark side of the coin. Am J Cancer Res 1, 482-497. 116. Seke Etet, P. F., Vecchio, L., and Nwabo Kamdje, A. H. (2012) Signaling pathways in chronic myeloid leukemia and leukemic stem cell maintenance: key role of stromal microenvironment. Cell Signal 24, 1883-1888. 117. Seke Etet, P. F., Vecchio, L., Bogne Kamga, P., Nchiwan Nukenine, E., Krampera, M., and Nwabo Kamdje, A. H. (2013) Normal hematopoiesis and hematologic malignancies: role of canonical Wnt signaling pathway and stromal microenvironment. Biochim Biophys Acta 1835, 1-10. 118. Vecchio, L., Seke Etet, P. F., Kipanyula, M. J., Krampera, M., and Nwabo Kamdje, A. H. (2013) Importance of epigenetic changes in cancer etiology, pathogenesis, clinical profiling, and treatment: what can be learned from hematologic malignancies? Biochim Biophys Acta 1836, 90-104. 119. Clark, D. E., Errington, T. M., Smith, J. A., Frierson, H. F., Weber, M. J., and Lannigan, D. A. (2005) The Serine/Threonine Protein Kinase, p90 Ribosomal S6 Kinase, Is an Important Regulator of Prostate Cancer Cell Proliferation. Cancer Res 65, 3108-3116. 120. Whitworth, H., Bhadel, S., Ivey, M., Conaway, M., Spencer, A., Hernan, R., Holemon, H., and Gioeli, D. (2012) Identification of Kinases Regulating Prostate Cancer Cell Growth Using an RNAi Phenotypic Screen. PLoS One 7, e38950. 121. Steiner, H., Godoy-Tundidor, S., Rogatsch, H., Berger, A. P., Fuchs, D., Comuzzi, B., Bartsch, G., Hobisch, A., and Culig, Z. (2003) Accelerated in Vivo Growth of Prostate Tumors that Up-Regulate Interleukin-6 Is Associated with Reduced Retinoblastoma Protein Expression and Activation of the Mitogen-Activated Protein Kinase Pathway. Am J Pathol 162, 655-663. 122. Gilley, R., March, H. N., and Cook, S. J. (2009) ERK1/2, but not ERK5, is necessary and sufficient for phosphorylation and activation of c-Fos. Cell Signal 21, 969-977. 123. Monje, P., Hernandez-Losa, J., Lyons, R. J., Castellone, M. D., and Gutkind, J. S. (2005) Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1. J Biol Chem 280, 35081-35084. 124. Chalmers, C. J., Gilley, R., March, H. N., Balmanno, K., and Cook, S. J. (2007) The duration of ERK1/2 activity determines the activation of c-Fos and Fra-1 and the composition and quantitative transcriptional output of AP-1. Cell Signal 19, 695-704. 125. Wang, Y., and Prywes, R. (2000) Activation of the c-fos enhancer by the Erk MAP kinase pathway through two sequence elements: the c-fos AP-1 and p62TCF sites. Oncogene 19, 1379-1385. 126. Chang, H. Y., Huang, T. C., Chen, N. N., Huang, H. C., and Juan, H. F. (2014) Combination therapy targeting ectopic ATP synthase and 26S proteasome induces ER stress in breast cancer cells. Cell Death Dis 5, e1540-e1540. 127. Ma, Z., Cao, M., Liu, Y., He, Y., Wang, Y., Yang, C., Wang, W., Du, Y., Zhou, M., and Gao, F. (2010) Mitochondrial F1Fo-ATP synthase translocates to cell surface in hepatocytes and has high activity in tumor-like acidic and hypoxic environment. Acta Biochim Biophys Sin 42, 530-537. 128. Li, W., Li, Y., Li, G., Zhou, Z., Chang, X., Xia, Y., Dong, X., Liu, Z., Ren, B., Liu, W., and Li, Y. (2017) Ectopic expression of the ATP synthase beta subunit on the membrane of PC-3M cells supports its potential role in prostate cancer metastasis. Int J Oncol 50, 1312-1320. 129. Adinolfi, E., Raffaghello, L., Giuliani, A. L., Cavazzini, L., Capece, M., Chiozzi, P., Bianchi, G., Kroemer, G., Pistoia, V., and Di Virgilio, F. (2012) Expression of P2X7 Receptor Increases In Vivo Tumor Growth. Cancer Res 72, 2957-2969. 130. Gilbert, S. M., Oliphant, C. J., Hassan, S., Peille, A. L., Bronsert, P., Falzoni, S., Di Virgilio, F., McNulty, S., and Lara, R. (2019) ATP in the tumour microenvironment drives expression of nfP2X7, a key mediator of cancer cell survival. Oncogene 38, 194-208. 131. Amoroso, F., Falzoni, S., Adinolfi, E., Ferrari, D., and Di Virgilio, F. (2012) The P2X7 receptor is a key modulator of aerobic glycolysis. Cell Death Dis 3, e370. 132. Vaupel, P., and Multhoff, G. (2017) Accomplices of the Hypoxic Tumor Microenvironment Compromising Antitumor Immunity: Adenosine, Lactate, Acidosis, Vascular Endothelial Growth Factor, Potassium Ions, and Phosphatidylserine. Front Immunol 8, 1887-1887. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/74165 | - |
dc.description.abstract | 腫瘤微環境由腫瘤細胞與異質性的基質細胞組合而成,包括間充質幹細胞與其衍生的成纖維細胞。然而這些基質細胞能夠透過旁分泌趨化因子及生長因子來調節腫瘤的生成,血管新生以及促進癌症轉移及侵襲。在本研究中我們試圖探討間充質幹細胞在肺癌腫瘤微環境中所扮演的角色。首先我們以培養間充質幹細胞三天的條件培養基對於肺癌細胞進行處理,結果發現間充質幹細胞的條件培養基會增強肺癌細胞的生長能力及遷移情形。進一步我們想了解其中的調控機制,我們以磷酸化蛋白質體學的方式剖析其參與調控的訊號途徑,我們總共鑑定到有差異表現的磷酸化蛋白700個,其中含有1926個磷酸化位點,此外我們進行激酶的預測分析,發現間充質幹細胞透過激活肺癌細胞中絲裂原活化蛋白激酶信號途徑 (MAPK pathway) 促使轉錄因子c-Fos在磷酸化位點絲氨酸374處 (serine 374) 的活化。進一步我們透過使用MAPK抑制劑來抑制c-Fos S374的磷酸化,結果發現原本肺癌細胞增強的生長及遷移能力因此而受到抑制。另一方面我們也構築了去磷酸化的c-Fos質體DNA,將其於細胞中過度表現。在與野生型的c-Fos相比之下,去磷酸化的c-Fos導致細胞增殖與集落形成的能力下降,而細胞的遷移情形也受到抑制。整合上述實驗結果,我們的研究表明,間充質幹細胞所衍生的腫瘤微環境會介導肺癌細胞MAPK信號途徑的活化,進一步將c-Fos S374磷酸化,並且促進肺癌細胞的生長及轉移。
另一方面,根據最近的文獻報導顯示腫瘤微環境中存在著大量的三磷酸腺苷(ATP),其能透過嘌呤能信號傳導途徑活化癌細胞膜上的P2X7受體。然而在我們的研究中觀察到間充質幹細胞的細胞表面存在著大量的異位ATP合成酶,此外腫瘤微環境中的ATP會激活肺癌細胞的MAPK信號途徑,進一步導致c-Fos S374的磷酸化。綜合來說,我們的研究證明,間充質幹細胞表面的異位ATP合成酶會釋放大量的ATP進入肺癌的腫瘤微環境,並且透過MAPK信號途徑的活化進一步將c-Fos S374磷酸化,最後促進肺癌細胞的生長以及轉移能力。 | zh_TW |
dc.description.abstract | Tumor microenvironment contains tumor cells and a mixture of heterogeneous stromal cells, including mesenchymal stem cells (MSCs) and MSC-derived fibroblast. These stromal cells are able to regulate tumor growth, angiogenesis, metastasis and invasion by paracrine secretion of cytokines, chemokine and growth factors. Here, we attempt to dissect the roles of MSCs in the tumor microenvironment of lung cancer. At first, we found that the MSCs conditioned medium (MSC-CM) enhanced lung cancer cell proliferation and migration. However, the signaling pathways mediated by MSC-secreting factors are still unclear. To further elucidate MSC regulatory pathways, we performed quantitative phosphoproteomics for MSC-CM treated lung cancer cells, and a total of 1926 phosphorylation sites on 700 phosphoproteins were identified. Moreover, integrative analysis of phosphoproteins and predicted kinases suggested that phosphorylation of c-Fos at serine 374 was induced by MSC-CM through activating mitogen-activated protein kinases (MAPK) signaling pathway in lung cancer cells. Consistently, our results showed that MSC-induced cell proliferation and migration were abrogated by inhibiting c-Fos phosphorylation using ERK1/2 inhibitor. In addition, the dephosphorylated form of c-Fos at serine 374 led to decreased cell proliferation, cell motility and colony forming ability compared to wild-type form of c-Fos in MSC-CM treated lung cancer cells. Collectively, our study demonstrated that MSCs might trigger the MAPK pathway followed by the phosphorylation of c-Fos at serine 374 to promote cancer proliferation and migration.
Recent studies have reported that extracellular ATPs accumulate in the tumor microenvironment and stimulate the P2X7 receptor on the cancer cell membrane through purinergic signaling. In our data, we observed that ectopic ATP synthase was overexpressed on the cell surface of MSCs. In addition, extracellular ATPs in the lung cancer microenvironment trigger the MAPK pathway to phosphorylate c-Fos on serine 374. In conclusion, our study suggested that ectopic ATP synthase on the surface of MSCs released extracellular ATPs into the lung cancer microenvironment and promoted cancer progression through c-Fos S374 phosphorylation in the MAPK signaling pathway. | en |
dc.description.provenance | Made available in DSpace on 2021-06-17T08:22:34Z (GMT). No. of bitstreams: 1 ntu-108-R06b43014-1.pdf: 5932485 bytes, checksum: 01407056ddebbfa857499f2ecf8ce413 (MD5) Previous issue date: 2019 | en |
dc.description.tableofcontents | 口試委員會審定書 i
謝辭 ii 中文摘要 iii Abstract v Contents vii List of Figures xii List of Tables xiv Chapter 1. Introduction 1 1.1 Non-small-cell lung cancer (NSCLC) 1 1.2 Mesenchymal stem cells (MSCs) 1 1.3 Tumor microenvironment 2 1.4 MAPK pathway 3 1.5 Proto-oncogene c-Fos 4 1.6 Ecotopic ATP synthase 5 1.7 Purinergic signaling 6 1.8 Previous studies 7 1.8.1 Quantitative phosphoproteomic profiling of lung cancer cells treated with MSC-CM 7 1.8.2 Motif enrichment analysis indicated that the MAPK pathway might be involved in the MSC-induced lung cancer cells 8 1.9 Motivation 9 Chapter 2. Materials and Methods 10 2.1 Cell culture 10 2.2 Conditioned medium collection 11 2.3 Cell proliferation analysis 11 2.3.1 Cell counting 11 2.3.2 MTS assay 11 2.4 Cell migration assay 12 2.5 Colony forming assay 12 2.6 Western blotting 13 2.7 ERK1/2 inhibitor (SCH772984) treatment of LM cells 14 2.8 RNA extraction 15 2.9 Reverse transcription 16 2.10 Construction of c-Fos 16 2.10.1 PCR amplification 16 2.10.2 Restriction enzyme digestion 17 2.10.3 Gel extraction 18 2.10.4 Ligation 18 2.10.5 Transformation 19 2.10.6 Colony PCR 19 2.10.7 Plasmid DNA purification 20 2.11 Overexpression of c-Fos in LM cells 21 2.12 Fluorescence immunocytochemistry (ICC) 22 2.13 Flow cytometry 23 2.14 ATP bioluminescence assay 23 2.15 ATP treatment of lung cancer cells 24 2.16 P2X7 receptor antagonist (A 438079) treatment of lung cancer cells 24 2.17 Statistical analysis 25 Chapter 3. Results 26 3.1 MSC-CM promote proliferation and migration in lung cancer cells 26 3.2 MSC-CM triggers MAPK pathway for phosphorylation of c-Fos at Serine 374 27 3.3 MSC-CM mediates cancer development by regulating MAPK/pho-c-Fos signaling axis 28 3.4 Phosphorylation of c-Fos plays an essential role in MSC-regulated function 29 3.5 Ectopic ATP synthase on the cell surface of MSCs might release ATP into the lung cancer tumor microenvironment 30 3.6 Extracellular ATPs trigger MAPK pathway to phosphorylate c-Fos of serine 374 in lung cancer cells 31 3.7 P2X7 receptor blockade inhibits MSC-induced c-Fos S374 phosphorylation in MAPK signaling pathway of lung cancer cells 32 3.8 P2X7 receptor blockade down-regulates MSC-induced cell proliferation and migration of lung cancer cells 33 Chapter 4. Discussion 34 Chapter 5. Conclusion 37 References 39 Figures 59 Tables 83 Appendix 84 | |
dc.language.iso | en | |
dc.title | 間充質幹細胞衍生之腫瘤微環境介導MAPK信號途徑中c-Fos S374的磷酸化並促進肺癌進程 | zh_TW |
dc.title | Mesenchymal Stem Cells-derived Microenvironment Promotes Lung Cancer Cell Progression via c-Fos S374 Phosphorylation in MAPK Signaling Pathway | en |
dc.type | Thesis | |
dc.date.schoolyear | 107-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 黃宣誠,王憶卿,李佳霖,李岳倫 | |
dc.subject.keyword | 腫瘤微環境,間充質幹細胞,磷酸化蛋白質體學,絲裂原活化蛋白激?信號途徑,轉錄因子c-Fos,異位ATP合成?,P2X7受體,嘌呤能信號傳導途徑, | zh_TW |
dc.subject.keyword | tumor microenvironment,mesenchymal stem cells (MSCs),phosphoproteomics,mitogen-activated protein kinases (MAPK) signaling pathway,c-Fos,ectopic ATP synthase,P2X7 receptor,purinergic signaling, | en |
dc.relation.page | 87 | |
dc.identifier.doi | 10.6342/NTU201903131 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2019-08-14 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 分子與細胞生物學研究所 | zh_TW |
顯示於系所單位: | 分子與細胞生物學研究所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-108-1.pdf 目前未授權公開取用 | 5.79 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。