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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 游偉絢 | |
| dc.contributor.author | Ning-Xing Tsai | en |
| dc.contributor.author | 蔡寧馨 | zh_TW |
| dc.date.accessioned | 2021-06-08T05:00:18Z | - |
| dc.date.copyright | 2010-09-09 | |
| dc.date.issued | 2010 | |
| dc.date.submitted | 2010-08-17 | |
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/23388 | - |
| dc.description.abstract | Matrix metalloptroteinase-7 (MMP-7; matrilysin) is a member of the MMPs family, which is involved in the extracellular matrix (ECM) component degradation and tissue remodeling. MMP-7 was reported as a secreted enzyme localized in the epical surface of normal glandular epithelial cells by Western blot and zymography analysis. Interestingly, a 31 kDa protein with protease activity found in nucleus was identified as pro-MMP-7. Furthermore, the protein sequence of MMP-7 was analyzed and a putative sumoylation site was defined by Dr. Wei-Hsuan Yu. (1998 Gordon Research Conferences poster)
To determine the sumoylation state of MMP-7, we used two anti-MMP7 antibodies to immunoprecipitate MMP-7, and then analyzed by Western blot with an anti-SUMO3 antibody. These results demonstrated that MMP-7 was modified by SUMO3. The prominent SUMO3 modified MMP-7 in the nucleus fraction implicated that SUMOylation post-translational modification for MMP-7 could be a nucleus trafficking signature for MMP-7. Also, by analyzing the total cell lysate with immunoprecipitation method, we found that MMP-7 were also ubiquitinated. The SUMO3 and ubiquitin tagged on MMP-7 could be responsible for MMP-7 intracellular trafficking route. The detail mechanism remains for further investigation. After the nuclear translocation of MMP-7 was verified, we further found that lamin B1 became fragmented when MMP-7 was overexpressed. Using an anti-lamin B1 antibody, the immunoprecipitation data showed that the active site mutated MMP-7 was pulled down and was detected by Western blotting. Furthermore, the intact structure of lamin B1 at nuclear lamina was changed when MMP-7 was overexpressed. My data suggested that lamin B1 could be a substrate of MMP-7 in the nucleus. As the MMP-7/SUMO3 overexpressed cells formed colonies in the soft agar assay, the SUMOylated MMP-7 might involved in cancer progression by chromatin remodeling. The detailed underlying mechanism will be addressed in the near future. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-08T05:00:18Z (GMT). No. of bitstreams: 1 ntu-99-R97442012-1.pdf: 2318917 bytes, checksum: 69b66150df3de7aa003d46886313a9d4 (MD5) Previous issue date: 2010 | en |
| dc.description.tableofcontents | 口試委員會審定書 i
謝誌 ii 摘要 I Abstract II Contents IV List of figures V Chapter 1. Introduction - 1 - Chapter 2. Materials and Methods - 13 - 2.1 Materials - 14 - 2.2 Methods - 20 - Chapter 3. Results - 27 - Chapter 4. Discussion - 38 - Chapter 5. Figures - 45 - Chapter 6. References - 60 - Appendix - 74 - | |
| dc.language.iso | en | |
| dc.subject | 細胞癌化 | zh_TW |
| dc.subject | 基質金屬蛋白酶 | zh_TW |
| dc.subject | 細胞核基質 | zh_TW |
| dc.subject | SUMO修飾 | zh_TW |
| dc.subject | 核纖層蛋白B1 | zh_TW |
| dc.subject | laminB1 | en |
| dc.subject | tumor progression | en |
| dc.subject | nuclear matrix | en |
| dc.subject | MMP-7 | en |
| dc.subject | SUMOylation | en |
| dc.title | SUMO蛋白轉譯後修飾之基質金屬蛋白酶-7在細胞核中參與核纖層蛋白蛋白質裂解之研究 | zh_TW |
| dc.title | The nucleus translocation of SUMOylated MMP-7 mediated proteolysis of nucleus matrix protein lamin B1 | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 98-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 湯志永,楊偉勛,陳佑宗,俞松良 | |
| dc.subject.keyword | 基質金屬蛋白酶,-7,細胞核基質,SUMO修飾,核纖層蛋白B1,細胞癌化, | zh_TW |
| dc.subject.keyword | MMP-7,SUMOylation,laminB1,nuclear matrix,tumor progression, | en |
| dc.relation.page | 77 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2010-08-17 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 生物化學暨分子生物學研究所 | zh_TW |
| 顯示於系所單位： | 生物化學暨分子生物學科研究所 | |
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