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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/62786完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 周綠蘋 | |
| dc.contributor.author | Cheng-Chou Yu | en |
| dc.contributor.author | 游成州 | zh_TW |
| dc.date.accessioned | 2021-06-16T16:10:23Z | - |
| dc.date.available | 2018-09-24 | |
| dc.date.copyright | 2013-09-24 | |
| dc.date.issued | 2013 | |
| dc.date.submitted | 2013-02-22 | |
| dc.identifier.citation | 1. Coussens LM, Werb Z (2002) Inflammation and cancer. Nature 420: 860-867.
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/62786 | - |
| dc.description.abstract | 過去的研究結果已顯示valosin-containing protein (VCP) 和感染幽門螺旋桿菌所引起的胃癌有關。然而VCP與胃癌發展之間的關係尚未完全研究清楚，因此本論文的研究目的，是希望利用消去(subtractive )蛋白體學技術，先讓AGS 胃腺癌細胞中大量表達VCP蛋白質，接著利用免疫沉澱(immunoprecipitation)方法，得到細胞中與VCP交互作用的分子，然後進一步探討VCP其調控及胃癌發展的機制。首先，我們將免疫沉澱下來的VCP蛋白質複合體(complex)產物，經過一維電泳的展開，接著再利用液相層析偶合串聯式質譜儀(LC-MS/MS)進行分析，結果得到288個和VCP交互作用的蛋白，然後再藉由Ingenuity Pathway Analysis (IPA)軟體分析之後，得到18個和VCP交互作用的蛋白，主要都參與Akt訊息傳遞網路的的調控，於是我們利用免疫沉澱的方式，證明VCP和Akt之間的交互作用，除此之外，我們也觀察到當AGS細胞感染幽門螺旋桿菌時，會活化Akt激酶，進而促使VCP的磷酸化，同時我們也進一步分析發現， VCP的磷酸化會促使蛋白的泛素化和聚集體(aggresome)的形成，然後使一些細胞凋亡的蛋白的降解(degradation)，進而促進細胞生存，藉由這些結果，我們瞭解到VCP的磷酸化在幽門螺旋桿菌感染胃上皮細胞機制中扮演重要的角色，同時讓我們將近一步釐清VCP的磷酸化在細胞中所參予的功能，也提供一個關於幽門螺旋桿菌感染胃上皮細胞新的致病機制。 | zh_TW |
| dc.description.abstract | Previous studies have demonstrated that valosin-containing protein (VCP) is associated with H. pylori-induced gastric carcinogenesis. By identifying the interactome of VCP overexpressed in AGS cells using a subtractive proteomics approach, we aimed to characterize the cellular responses mediated by VCP and its functional roles in H. pylori-associated gastric cancer. VCP immunoprecipitations followed by proteomic analysis identified 288 putative interacting proteins, 18 VCP-binding proteins belonged to the PI3K/Akt signaling pathway. H. pylori infection increased the interaction between Akt and VCP, Akt-dependent phosphorylation of VCP, levels of ubiquitinated proteins, and aggresome formation in AGS cells. Furthermore, phosphorylated VCP co-localized with the aggresome, bound ubiquitinated proteins, and increased the degradation of cellular regulators to protect H. pylori-infected AGS cells from apoptosis. Our study demonstrates that VCP phosphorylation following H. pylori infection promotes both gastric epithelial cell survival, mediated by the PI3K/Akt pathway, and the degradation of cellular regulators. These findings provide novel insights into the mechanisms of H. pylori infection induced gastric carcinogenesis. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-16T16:10:23Z (GMT). No. of bitstreams: 1 ntu-102-D93442005-1.pdf: 3736889 bytes, checksum: a849aa4303726fb7e5705ceb41d7d766 (MD5) Previous issue date: 2013 | en |
| dc.description.tableofcontents | 口試委員會審定書 i
誌謝 ii 中文摘要 iii Abstract iv Abbreviations v Table of Contents viii Chapter I – Overview and Rationale 1 1.1 Overview of gastric cancer 2 1.2 The relationship between Helicobacter pylori and gastric cancer 5 1.3 Role of Helicobacter pylori in gastric cancer 6 1.4 Valosin-containing protein (VCP) as a gastric cancer crucial biomarker 8 1.5 Structure and biological functions of VCP 10 1.6 VCP is highly modulated by phosphorylation 14 1.7 VCP and cancer 16 1.8 VCP inhibitors for anti-cancer therapy 17 Specific aim 19 Chapter II - VCP phosphorylation-dependent interaction partners prevent apoptosis in Helicobacter pylori-infected gastric epithelial cells 21 2.1 Introduction 22 2.2 Materials and Methods 25 2.3 Results 40 2.4 Discussion 50 Chapter III – Conclusion and perspectives 58 Conclusion and perspectives 59 List of Figures 62 Figure 1. Expression level of VCP in H. pylori infected gastric cancer tissue. 62 Figure 2. H. pylori infection induced high expression of VCP in mouse gastric tissues. 64 Figure 3. The VCP interactome. 65 Figure 4. Bioinformatic ontology of interacting proteins of VCP co-immunoprecipitates. 66 Figure 5. Ingenuity Pathway Analysis (IPA) prediction and analysis of signal transduction networks for the 288 proteins in the VCP interactome in AGS cells. 68 Figure 6. Increased interaction between VCP and Akt in AGS cells caused by H. pylori infection. 69 Figure 7. Scansite software prediction VCP phosphorylation sites 70 Figure 8. Analysis of VCP phosphorylation sites in H. pylori-infected AGS cells. 71 Figure 9. Akt and VCP involved in against apoptosis of AGS cells infected with H. pylori. 72 Figure 10. Akt activity is involved in VCP phosphorylation-induced protection against apoptosis of AGS cells infected with H. pylori. 73 Figure 11. Tri-mut VCP induced apoptosis of AGS cells infected with H. pylori. 74 Figure 12. Akt activity is involved in VCP phosphorylation-induced proliferation and cell division of AGS cells infected with H. pylori. 75 Figure 13. H. pylori induces aggresome formation and around the nucleus through VCP phosphorylation during infection of AGS cells. 76 Figure 14. H. pylori induces aggresome formation and polyubiquitinated proteins through VCP phosphorylation during infection of AGS cells. 77 Figure 15. Aggresome formation and polyubiquitinated proteins were reduced in Tri-mut VCP-Flag-transfected AGS cells infected with H. pylori. 78 Figure 16. Co-regulation analysis of cell survival in H. pylori-infected AGS cells. 79 Figure 17. Immunoprecipitation and immunoblotting analysis of VCP interaction partners in H. pylori-infected AGS cells. 80 Figure 18. NF-κB activation caused by H. pylori infection involves phosphorylation of VCP. 81 Figure 19. Cellular regulator degradation caused by H. pylori infection involves phosphorylation of VCP. 82 Figure 20. H. pylori stimulated polyubiquitination of Cellular regulator. 83 Figure 21. H. pylori induced cellular regulators colocalized with ubiquitinated proteins during infection of AGS cells. 84 Figure 22. Protein degradation was inhibited in AGS ells overexpressing Tri-mut VCP-Flag 85 Figure 23. Schematic model of the hypothetical mechanism for VCP anti-apoptotic pathways in gastric epithelial cells infected with H. pylori. 86 List of Tables 87 Table 1. Primer sequences for VCP and site-specific VCP mutant constructs 87 Table 2. List of 288 VCP interaction proteins immunoprecipitated with anti-Flag M2 affinity gel from H. pylori infected AGS cells. 88 Table 3. List of biological functions of VCP-interacting proteins from Gene Ontology. 95 Table 4. Top 10 list of canonical pathways activated by VCP-interacting proteins from Ingenuity Pathway Analysis. 96 Table 5. Top high-level functions identified by Ingenuity global function analysis of VCP-interacting proteins in H. pylori-infected AGS cells. 97 Reference 98 List of instrument 109 | |
| dc.language.iso | zh-TW | |
| dc.subject | 細胞凋亡 | zh_TW |
| dc.subject | 訊息傳導 | zh_TW |
| dc.subject | 纈酪胺酸蛋白質 | zh_TW |
| dc.subject | 交互作用體 | zh_TW |
| dc.subject | 免疫沉澱 | zh_TW |
| dc.subject | 幽門螺旋桿菌 | zh_TW |
| dc.subject | 聚集體 | zh_TW |
| dc.subject | PI3K/Akt pathway | en |
| dc.subject | apoptosis | en |
| dc.subject | Helicobacter pylori | en |
| dc.subject | valosin-containing protein | en |
| dc.subject | aggresome | en |
| dc.title | 利用蛋白體學方法鑑定胃上皮細胞中磷酸化缬絡胺酸蛋白質的交互作用分子及其防止幽門螺旋桿菌誘發細胞凋亡之特性 | zh_TW |
| dc.title | Proteomics approach to identify and characterize VCP phosphorylation-dependent interaction partners for prevention Helicobacter pylori-induced apoptosis of gastric epithelial cells | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 101-1 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 蔡孟勳,林中梧,楊智欽,黃麗華 | |
| dc.subject.keyword | 聚集體,細胞凋亡,幽門螺旋桿菌,纈酪胺酸蛋白質,免疫沉澱,交互作用體,訊息傳導, | zh_TW |
| dc.subject.keyword | aggresome,apoptosis,Helicobacter pylori,PI3K/Akt pathway,valosin-containing protein, | en |
| dc.relation.page | 109 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2013-02-22 | |
| 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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