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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 陳水田(Shui-Tein Chen) | |
| dc.contributor.author | Zhi-Rong Wu | en |
| dc.contributor.author | 吳致榕 | zh_TW |
| dc.date.accessioned | 2021-06-16T17:20:00Z | - |
| dc.date.available | 2012-08-19 | |
| dc.date.copyright | 2012-08-19 | |
| dc.date.issued | 2012 | |
| dc.date.submitted | 2012-08-17 | |
| dc.identifier.citation | References
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/63820 | - |
| dc.description.abstract | 蛋白質醣修飾的改變在癌症進程中扮演重要的角色，包括細胞增生，細胞侵犯，細胞轉移…等。我們利用超量表現第四型岩藻醣轉酶(fucosyltransferase IV, FucT4)的肺癌細胞株(A549-FucT4)及其對照組細胞株(A549-Mock)作為實驗的模式細胞，以探討第四型岩藻醣轉酶對於細胞的影響。根據先前研究結果指出，第四型岩藻醣轉酶大量表現使得A549-FucT4細胞株在轉移盤移行實驗(transwell migration assay)、細胞貼附實驗(adhesion assay)、明膠酶譜實驗(zymography)和免疫缺陷型小鼠(SCID mice)體中增殖實驗中皆發現較A549-Mock細胞株表現更惡性。本研究中利用兩種不同方式的嗜醣蛋白親和純化法(lectin affinity enrichment)分離出許多具有岩藻醣修飾之醣蛋白，經由液相層析串連電灑游離飛行式質譜儀(LC/ESI-TOF-MS)鑑定醣蛋白身分。根據比對A549-FucT4及A549-Mock細胞株中的醣蛋白，找出14個具有差異的岩藻醣修飾之蛋白。經過綜合生物分子分析軟體(IPA)運算之後發現這14個醣蛋白分別參與細胞增生，細胞貼附，細胞移動，細胞凋亡癌症相關功能。另外在實驗中我們發現A549-FucT4細胞株的生長速度比A549-Mock細胞株快。因此藉由醣蛋白質體學的實驗結果選出參與細胞增生的醣蛋白HGFR及CD109。結果指出，在不同濃度HGF刺激下或經過不同時間後，A549-FucT4細胞株的HGFR磷酸化程度均小於A549-Mock細胞株。但利用TGF-beta 1 處理細胞後，下游訊息smad3蛋白的磷酸化並無顯著差異。實驗結果讓我們瞭解到第四型岩藻醣轉酶大量表現會對癌症進程中的特定蛋白造成功能上的影響。 | zh_TW |
| dc.description.abstract | Protein glycosylation alterations play an important role in cancer progression, including cell proliferation, cell invasion, and cell metastasis. We use A549-FucT4 cells, which over-expressed fucosyltransferase IV, and A549-Mock cell as a control cell line, as a research model to study the influence of fucosylation in cell biology. Our previous data showed that A549-FucT4 is more malignant than A549-Mock based on the transwell migration assay, adhesion assay, zymography assay, and proliferation of cancer cell lines in SCID mice. We also found that the proliferation rate of A549-FucT4 cells are more rapid than A549-Mock cells. In our study, we used two methods of lectin affinity glycoprotein enrichment to enrich fucosylated proteins, and identified their identities through the LC/ESI-TOF-MS. In comparison to the glycoproteins identified in A549-Mock cells, there were 14 distinctive glycoproteins identified solely in A549-FucT4. Using Ingenuity Pathway Analysis software, we found that these 14 glycoproteins are involved in cell migration, cell proliferation, cell movement, and cell apoptosis. We chose HGFR and CD109 for further study based on our glycoproteomic data. The result indicated that A549-FucT4 cells have less HGFR phosphorylation levels in comparison with A549-Mock cells after treatment with HGF in different doses and different incubation times. But there was no obvious difference in smad3 phosphorylation after TGF-beta 1 treatment between the two cell. We think fucosyltransferase IV overexpression may affect particular proteins which take parts in cancer progression. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-16T17:20:00Z (GMT). No. of bitstreams: 1 ntu-101-R99b46031-1.pdf: 1032615 bytes, checksum: 766ba97791c5dd68396cc38cea152ceb (MD5) Previous issue date: 2012 | en |
| dc.description.tableofcontents | TABLE OF CONTENTS
中文摘要 i Abstract ii List of abbreviations iii CHAPTER 1. INTRODUCTION 1 1.1. Lung cancer 1 1.2. Glycosylation 2 1.3. Fucosylation 3 1.4. Glycosylation and cancer 5 1.5. Fucosyltransferase and cancer 6 1.6. Glycoproteomics 7 1.7. The hepatocyte growth factor receptor 8 1.8. CD109 9 1.9. Purpose of the study 10 CHAPTER 2. MATERIALS AND METHODS 12 2.1. Cell lines and cell culture 12 2.2. Total cell protein lysate 12 2.3. Bradford assay 13 2.4. BrdU ELISA assay 13 2.5. Lectin blot 14 2.6. Western blot 15 2.7. AAL affinity chromatography 16 2.8. Streptavidin-particles & biotinylated-AAL glycoproteins enrichment 16 2.9. In-solution digestion 17 2.10. Liquid-chromatography electrospray ionization-tandem mass spectrometry (LC/ESI-MS/MS) 18 CHAPTER 3. RESULTS 19 3.1. Confirm the level of alpha-(1, 3/1, 4) linked fucosylation in A549-FucT4 and A549-Mock 19 3.2. Confirming the fucosylated terminal glycan structure difference between A549-FucT4 and A549-Mock 21 3.3. The use of two glycoprotein enrichments for further proteins identification by LC/ESI-MS/MS 23 3.3.1. AAL affinity chromatography enrichment 23 3.3.2. Streptavidin-particles & biotinylated-AAL enrichment 23 3.4. LC-ESI-MS/MS analysis to identify proteins extracted from the glycoproteins enrichment phase 25 3.4.1. Mascot protein analysis identified by AAL affinity chromatography enrichment 25 3.4.2. Mascot analysis proteins identified by streptavidin-particles & biotinylated-AAL enrichment 26 3.5. Comparison of the two glycoproteins-enrichment methods 28 3.6. A distinctive group of 14 glycoproteins identified in A549-FucT4 cells 29 3.7. IPA analysis of 14 glycoproteins in A549-FucT4 30 3.8. Using glycoproteomic data to elucidate the glycoproteins involved in cell proliferation 31 3.8.1. A549-FucT4 and A549-Mock cells proliferate differently 31 3.8.2. Cell proliferation-related glycoproteins 32 3.9. Role of fucosylation on hepatocyte growth factor receptor (MET) activation 33 3.9.1. Fucosylation of HGFR in A549-FucT4 and A549-Mock cells 33 3.9.2. Phosphorylation of Met tyrosine kinase in HGF treatment 34 3.10. Role of fucosylation on CD109 for TGF-beta signaling pathway activation 36 3.10.1. Fucosylation of CD109 in A549-FucT4 and A549-Mock cells 36 3.10.2. Phosphorylation of Smad in the TGF-beta pathway 37 CHAPTER 4. DISCUSSION 38 4.1. Different glycoproteomic approaches have advantages and disadvantages 38 4.2. Fourteen distinctive glycoproteins in A549-FucT4 cells 40 4.3. Difficulties and challenges in glycoproteomics 42 References 44 | |
| dc.language.iso | en | |
| dc.subject | 肺癌 | zh_TW |
| dc.subject | 醣蛋白 | zh_TW |
| dc.subject | 嗜醣蛋白親合純化 | zh_TW |
| dc.subject | 第四型岩藻醣轉酶 | zh_TW |
| dc.subject | 醣蛋白質體學 | zh_TW |
| dc.subject | Lung cancer | en |
| dc.subject | Glycoproteins | en |
| dc.subject | Lectin affinity enrichment | en |
| dc.subject | Fucosyltransferase IV | en |
| dc.subject | Glycoproteomic | en |
| dc.title | 第四型岩藻醣轉酶超量表現對肺癌細胞株醣蛋白的影響 | zh_TW |
| dc.title | Glycoproteomics of fucosyltransferase IV-overexpressed A549 cell | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 100-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 阮雪芬(Hsueh-Fen Juan),黃宣誠(Hsuan-Cheng Huang),吳盈達(Ying-Ta Wu) | |
| dc.subject.keyword | 肺癌,醣蛋白,嗜醣蛋白親合純化,第四型岩藻醣轉酶,醣蛋白質體學, | zh_TW |
| dc.subject.keyword | Lung cancer,Glycoproteins,Lectin affinity enrichment,Fucosyltransferase IV,Glycoproteomic, | en |
| dc.relation.page | 55 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2012-08-17 | |
| 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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