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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 陳義雄 | |
| dc.contributor.author | Chia-Jen Tseng | en |
| dc.contributor.author | 曾嘉珍 | zh_TW |
| dc.date.accessioned | 2021-06-17T00:11:07Z | - |
| dc.date.available | 2015-07-26 | |
| dc.date.copyright | 2012-07-26 | |
| dc.date.issued | 2012 | |
| dc.date.submitted | 2012-07-13 | |
| dc.identifier.citation | Alland, L., Muhle, R., Hou, H., Jr., Potes, J., Chin, L., Schreiber-Agus, N., and
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/65754 | - |
| dc.description.abstract | CTCF 是一個分佈廣且高度保守的轉錄因子，其分子量約82 kDa。先
前證實獲能的小白鼠精子之CTCF 會在酪胺酸基磷酸化。本研究探討這一 個巨大蛋白分子的酪胺酸磷酸化位置，並評估該化學修飾對標的核酸親和 力的影響。我們發現頂體反應不會導致存於頂體內CTCF 的釋放。運用基 因重組技術，融合GST 於CTCF 三個區域（domain），包括鋅指部位 （Zinc-finger domain，ZD/ residues 266-573），ZD 的N-端區域（ND/ residues 1-265）和ZD 的C-端區域（CD/ residues 574-736）。GST-ND 可被獲能精 子的酪胺酸激酶活性磷酸化，但GST-ZD 和GST-CD 卻不會。進一步將ND 的Y25, Y138, Y197, Y214, or Y226 突變成苯丙胺酸（Phenylalanine）而製備了突變 蛋白。相對原始蛋白（wild-type GST-ND），Y25F、Y138F 和Y214F 具有 相同的激酶基質活化，但Y197F 和Y226F 的基質活性則顯著降低，提示 Y197F 和Y226F 是兩個主要的磷酸化位置。進一步發現EGFR 的抑制劑 AG1478 可降低激酶對GST-ND 的磷酸化。配合可被磷酸化酪胺酸鄰近胺 基酸順序預測Y197 可被EGFR 磷酸化。運用核酸電泳動移動分析法 （electrophoretic mobility shift assay）量測CTCF 對β-APP、FpV 和c-Myc 啟 動子的親和力。相對於尚未獲能精子的CTCF，獲能精子的CTCF 對三個 啟動子的親和力較弱，但對甲基化的啟動子則親和力較強。 | zh_TW |
| dc.description.abstract | The CCCTC-binding nuclear factor (CTCF) is a widely expressed and highly
conserved 82-KDa protein. Using mice as experimental animals, work of our previous study identified the tyrosine-phosphorylated form of CTCF in the capacitated sperm. This work was conducted to determine the tyrosine-phosphorylated sites in the CTCF molecule and to assess the impact of such a phosphorylation modification on the affinity of this nuclear factor to its target DNAs. We found that acrosomal exocytosis did not result in the release of CTCF residing in spermatozoal acrosome region. We made recombinant polypeptides of GST in frame with the N-terminal (ND/residues 1-265), zinc-finger domain (ZD/residues 266-573) and C-terminal domain (CD/residues 574-736) in CTCF. Neither GST-ZD nor GST-CD but GST-ND could be phosphorylated by the tyrosine kinase activity in the capacitated sperm. Further, Y25, Y138, Y197, Y214, or Y226 in ND of GST-ND was mutated to phenylalanine. Mutants Y25F, Y138F, and Y214F showed virtually the same substrate activity as the wild type GST-ND for the capacitation-related tyrosine phosphorylation, whereas the mutants Y197F and Y226F showed weaker substrate activity, manifesting Y197 and Y226 as the two major phosphorylation sites in which the modification of Y197 could be suppressed by an EGFR inhibitor AG1478. The electrophoretic mobility shift assay was applied to measure the affinity of spermatozoal CTCF to its DNA target sequences found in the promotors of amyloid β-protein precursor (β-APP), FpV and c-Myc. Relative to CTCF in the incapacitated sperm, the tyrosine-phosphorylated protein in the BSA-treated sperm gave weaker affinity to each target DNA, whereas it showed stronger affinity to the methylated forms of these target DNAs. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-17T00:11:07Z (GMT). No. of bitstreams: 1 ntu-101-D91242007-1.pdf: 1630382 bytes, checksum: 25c2395cae36ecdd000e8bc4a09cdd13 (MD5) Previous issue date: 2012 | en |
| dc.description.tableofcontents | 縮寫表…………………………………………………………………………… 4
中文摘要………………………………………………………………………… 5 英文摘要………………………………………………………………………… 6 論文內容 第一章 概論 1.1. 哺乳類有性生殖…………………………………………………………....7 1.2. 精子的分化過程…………………………………………………….…...…7 1.3. 成熟精子在副睪進行的修飾………………………………………………9 1.4. 哺乳類雄性附屬性腺…………………………………………...….……....9 1.5. 精子的結構與獲能效應……………………………………………………9 1.6. 精子獲能效應的生理變化…………………………………….…...………12 1.7. 頂體反應（Acrosome reaction） ……………………………....…………12 1.8. 體外獲能效應的進行（In vitro capacitation）……………...……….……13 1.9. 精子獲能作用相關之蛋白質酪胺酸磷酸化研究…………...…………….16 1.10. CCCTC-結合轉錄因子（CCCTC-binding nuclear factor, CTCF）...….…17 1.11. 研究背景與本論文研究重點………………………………....……………20 第二章 實驗材料與方法 2.1. 動物實驗方法 2.1.1. 實驗動物……………………….…………………………….………21 2.1.2. 精子的製備……………………….………………………….………21 2.1.3. 試管獲能化效應（ In vitro capacitation ）………………..………22 2.1.4. 計算細胞的數量………………………….…………………….……23 2.1.5. 間接免疫螢光染色法………………………….……………….……24 2.1.6. 精子蛋白質酪胺酸磷酸化的偵測………………………….….……24 2.1.7. 精子頂體之觀察…………………………. …………………………25 2.1.8. 精子頂體反應的誘發………………………….………………….…25 2.1.9. 精子獲能效應在實驗上的觀察，定義及分析……………..………26 2.2. 分子生物學實驗方法 2.2.1. 聚合酶鏈鎖反應………………………….…………………….……27 2.2.2. 小量質體萃取………………………….……………………….……29 2.2.3. 重組質體製備………………………….……………………….……29 2.2.4. 質體轉型………………………….…………………………….……31 2.2.5. CTCF N 端的定點突變( Site-directed mutagenesis ) ………………31 2.3. 蛋白質實驗方法 2.3.1. GST 融和重組蛋白純化………………………….……………....…34 2.3.2. 還原性硫酸十二酯鈉聚丙烯醯胺凝膠電泳………………..........…35 2.3.3. 蛋白質染色分析- Coomassie Blue 染色…………………........……36 2.3.4. 西方墨點法（Western blotting）…………………………….…...…37 2.3.5. 蛋白質定量………………………….………….………...…....….…39 2.3.6. 免疫沉澱（Immunoprecipitation）……………………...…....….…40 2.3.7. In vitro kinase assay……………….………….…………….…..……40 2.3.8. In vitro kinase assay couple solid phase assay……….......…………..42 2.3.9. GST pull down………………………….……………..…….….……43 2.3.10.電泳膠體遲緩試驗………………………….….…..……….….……44 2.3.11.統計方法………………………….………….…….....…....…..….…46 第三章 結果 3.1. 精子頂體反應伴隨的CTCF 蛋白質酪胺酸磷酸化修飾.....…....…..….….47 3.2. 探討獲能效應引發CTCF 酪胺酸磷酸化修飾位置.....….............…..….…49 3.3. 探討獲能效應精子中會引發CTCF 酪胺酸磷酸化的激酶.....…....…..….52 3.4. 探討精子獲能效應之CTCF 對標的啟動子的親和力.....…....……..…….53 第四章 討論……………………….………….…….....……….......…..….…54 圖目錄……………….……………………..…….…….....……….......…..….…57 圖 1：Confirmation of CTCF in sperm at different stages.......…..….…………. 58 圖 2：Subcellular localization of CTCF in sperm at different stages…………... 60 圖 3：Electrophoretic analyses of the three bacterial expressed CTCF domains 62 圖 4：CTCF N terminal is the major capacitation-related tyrosine phosphorylation domain in vitro………………………………………… 64 圖 5：Identification of major capacitation-related tyrosine phosphorylation domain of CTCF by solid-phase assay …………………………………...66 圖 6：Expression profiles of the GST-ND mutants…………………………….. 68 圖 7：The capacitation –related tyrosine phosphorylation of GST-ND and its mutants pulled down from the reaction mixture by the GST beads.….….70 圖 8：Y197and Y226 are the dominant tyrosine phosphorylation sites of CTCF …....72 圖 9：Solid-phase assay for the capacitation-related phosphorylation of CTCF..74 圖10：Prediction of tyrosine kinase phosphorylation sites in ND of CTCF…....76 圖11：Impacts of several tyrosine kinase inhibitors on the phosphorylation of ND …………………………………………………………………………..78 圖12：Amino acid alignment for the CTCF ND from different species....80 圖 13：Binding ability of spermatozoal CTCF to its target DNA sequences….....82 參考文獻………………………………………………………………………..84 | |
| dc.language.iso | zh-TW | |
| dc.title | 以小白鼠為模式探討哺乳類精子轉錄因子CTCF：獲能效應引發CTCF酪胺酸基磷酸化會強化對甲基化標的核酸的親和力 | zh_TW |
| dc.title | Study on the spermatozoal CCCTC-binding nuclear factor （CTCF） using mice as a model ：The capacitation-related tyrosine phosphorylation of CTCF strengthens its affinity to the methylated target DNAs | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 100-2 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 潘榮隆,李明亭,蔡懷楨,梁博煌,李勝祥 | |
| dc.subject.keyword | 精子,頂體,CTCF,獲能效應,酪胺酸磷酸化, | zh_TW |
| dc.subject.keyword | sperm,acrosome,CTCF,capacitation,tyrosine phosphorylation, | en |
| dc.relation.page | 96 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2012-07-13 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科學研究所 | zh_TW |
| 顯示於系所單位： | 生化科學研究所 | |
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