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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
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dc.contributor.advisor | 阮雪芬(Hsueh-Fen Juan) | |
dc.contributor.author | Hui-Ting Tsai | en |
dc.contributor.author | 蔡惠婷 | zh_TW |
dc.date.accessioned | 2021-06-16T17:15:50Z | - |
dc.date.available | 2017-08-27 | |
dc.date.copyright | 2012-08-27 | |
dc.date.issued | 2012 | |
dc.date.submitted | 2012-08-19 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/63659 | - |
dc.description.abstract | ATP synthase is essential for almost all organisms because ATP is the common “energy currency” of cells. It is a multimeric protein complex including beta subunit (ATP5B) that catalyzes the synthesis of ATP from ADP and phosphate. Although ATP synthase was initially thought to be located exclusively in the mitochondrial inner membrane, its presence has now been described on the outside of the plasma membrane of both normal cells (e.g. endothelial cells, hepatocytes and adipocytes) and tumor cells. We are interested to understand whether ATP5B interacts with different proteins and performs different functions. Here, we perform a human proteome microarray to reveal the novel interacting proteins with ATP5B and identified 16 proteins which interact strongly with ATP5B. The identified ATP5B interacting proteins are functionally enriched in mitogen activated protein kinase 12 (MAPK12) dependent pathways. Our previous results showed that ATP5B was overexpressed on the plasma membrane with the potential as a cell proliferation regulator in both breast and lung cancers. Hence we further combined ATP synthase inhibitor, citrovirodin, and MAPK12 inhibitor, and found this combination leads to addictive inhibition on lung cancer cell proliferation. Taken together, these findings suggest that these interacting proteins of ATP5B as a cell proliferation signal linking to MAPK12 in response to a variety of extracellular stimuli. | en |
dc.description.provenance | Made available in DSpace on 2021-06-16T17:15:50Z (GMT). No. of bitstreams: 1 ntu-101-R99b43005-1.pdf: 3722277 bytes, checksum: eb04797dab0cbd549113023352b502a5 (MD5) Previous issue date: 2012 | en |
dc.description.tableofcontents | 誌謝 i
中文摘要 iii Abstract iv Contents vi List of Figures x List of Tables xi Chapter 1 Introduction 1 1.1 ATP synthase 1 1.2 ATP synthase β-subunit 2 1.3 Ectopic ATP synthase 3 1.4 Human proteome microarray 5 1.5 Motivation 7 1.6 Experimental design 8 Chapter 2 Materials and Methods 9 2.1 Cloning of ATP5B open reading frame 9 2.1.1 Cell culture 10 2.1.2 Total RNA extraction 10 2.1.3 Measurement of DNA concentration 11 2.2 Construction of pET-22b (+)-ATP5B, pET-43.1a (+)-ATP5B, pGEX-4T-1-ATP5B, and pMAL-c2X-ATP5B 11 2.2.1 Bacterial strains and bacterial culture 12 2.2.2 Transformation 12 2.2.3 Mini plasmid purification 13 2.3 Overexpression of ATP5B 13 2.3.1 Low temperature induction 14 2.3.2 Coomassie Brilliant Blue stained SDS-PAGE 14 2.3.3 Western blot 15 2.4 Purification of ATP5B 15 2.4.1 His-tagged protein purification 16 2.4.2 MBP-tagged protein purification 17 2.4.3 Bradford protein assay 17 2.4.4 Mass spectrometry 18 2.5 Hybridization of ATP5B with human proteome microarray 19 2.6 MataCore–pathway enrichment analysis 19 2.7 IPA–protein-protein interaction network analysis 20 2.8 RTCA system–cell growth assay 20 Chapter 3 Results 22 3.1 ATP5B construction and expression 22 3.2 Strategy I – control of the E. coli cellular milieu 23 3.3 Strategy II – engineered fusion protein 24 3.4 Strategy III –inclusion bodies re-solubilization and refolding 25 3.5 Hybridization of ATP5B with human proteome microarray 26 3.6 ATP5B interacting proteins are functionally enriched in MAPK12 dependent pathway 27 3.7 Top one protein-protein interaction network of ATP5B interacting proteins is highly connected 28 3.8 Combining citreoviridin and PD169316 leads to addictive inhibition on A549 proliferation 29 Chapter 4 Discussion 31 Chapter 5 Conclusion 36 Chapter 6 Future Works 37 References 38 Figures 45 Tables 58 Appendix A 62 Appendix B 63 Appendix C 64 Appendix D 68 Appendix E 69 | |
dc.language.iso | en | |
dc.title | 利用人類蛋白質體晶片探討ATP合成酶之交互作用蛋白 | zh_TW |
dc.title | Revealing Novel Interacting Proteins of ATP Synthase by Human Proteome Microarray | en |
dc.type | Thesis | |
dc.date.schoolyear | 100-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 黃宣誠(Hsuan-Cheng Huang),陳健生(Chien-Sheng Chen),徐駿森(Chun-Hua Hsu),王憶卿(Yi-Ching Wang) | |
dc.subject.keyword | 三磷酸腺苷,合成酶,β 次單位,交互作用蛋白,人類蛋白質體晶片,有絲分裂原活化蛋白質激酶,12, | zh_TW |
dc.subject.keyword | ATP synthase,ATP5B,interacting proteins,human proteome microarray,MAPK12, | en |
dc.relation.page | 69 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2012-08-19 | |
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 |
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