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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 翁啟惠(Chi-Huey Wong),陳敏慧(Min-Huey Chen) | |
dc.contributor.author | Jung-Tsu Chen | en |
dc.contributor.author | 陳容慈 | zh_TW |
dc.date.accessioned | 2021-06-15T13:35:41Z | - |
dc.date.available | 2025-12-31 | |
dc.date.copyright | 2016-02-24 | |
dc.date.issued | 2015 | |
dc.date.submitted | 2016-01-28 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/51478 | - |
dc.description.abstract | 口腔癌居全球癌症發病率的第十一名,而在台灣,口腔癌的發生率佔十大癌症的第五名。即使發生率已經下降,但口腔癌的預後仍然不佳,整體存活率在過去二十年只改善了百分之五。口腔癌的五年存活率大約是50%,而當復發時,能治癒的機會是微乎其微。口腔癌治療的困境與缺乏有效的早期診斷方式和暴露於環境致癌因子的機會增加有關。因此,研究口腔癌的機制是非常重要的。近年來已經證實醣化現象與癌症有關,本實驗先利用醣探針標定細胞中的醣蛋白,比較口腔癌細胞株及正常口腔上皮細胞的差異,得到B7-H3在口腔癌細胞株中會有過量表現。B7-H3是一種位於細胞膜上的醣蛋白,一開始在免疫細胞中發現,與T細胞的生長及細胞激素INF-gamma的產生有關。許多癌症組織也會表現B7-H3蛋白,且與癌化程度、癌症轉移及低存活率有關。根據這些證據,探討B7-H3在口腔癌中所扮演的角色。
從大量口腔麟狀細胞癌的組織檢體中,發現B7-H3的表現有顯著的增加,且與較大的腫瘤(p=0.0001)及臨床分期(p=0.004)相關。並且B7-H3標記分數高於55%者,口腔麟狀細胞癌病人有較差的全存活率。細胞及動物實驗證明,減弱醣蛋白B7-H3會抑制口腔癌細胞的生長及種植在小鼠口腔及背部之腫瘤大小,反之亦然。進一步以質譜儀分析口腔癌細胞B7-H3的醣化現象及醣分子結構,比起正常細胞,癌細胞之B7-H3有顯著的fucosylation,醣分子結構的支鏈較多,且表現正常細胞所沒有的terminal alpha-galactose,而癌細胞B7-H3的這些特殊醣分子結構會與凝集素如DC-SIGN及Langerin結合,說明B7-H3與免疫反應的關係。研究結果顯示,醣蛋白B7-H3在口腔癌細胞中的過度表現及異常的醣化修飾會與腫瘤的生長和免疫反應有關。 | zh_TW |
dc.description.abstract | Oral cancer is the eleventh most-common cancer worldwide and the fifth most prevalent cancer in Taiwan. Although the incidence has decreased over the last decade, outcomes of oral cancer remain difficult with only 5% improvement in overall survival in the last 20 years. The five-year survival rate of oral cancer is about 50% and complete recovery is almost not possible as recurrence is occurred. It is partly due to the lack of effective early diagnosis and increasing environmental exposure to cancer-causing agents. It has been proved that aberrant glycosylation is involved in cellular transformation. To identify new markers for oral cancer, we employed a glycosylation probe to investigate the function of sialylated glycoproteins differentially expressed on oral cancer cells and B7-H3 was found to be significant. B7-H3 is a membrane protein originally identified from immune cells. It is a costimulatory molecule related with the proliferation and IFN-gamma production in T cells. B7-H3 is also found in a variety of cancers and correlated with tumor progression. The purpose of this study is to explore the role of B7-H3 involved in oral cancer.
B7-H3 was found to be overexpressed in oral squamous cell carcinoma (OSCC) specimens and correlated with larger tumor size (p=0.0001), advanced clinical stage (p=0.004) and low survival rate in OSCC patients (B7-H3 labeling score >= 55%). In addition, knockdown of B7-H3 suppressed tumor cell proliferation, and restoration of B7-H3 expression enhanced tumor growth. We also observed differences in the glycoforms of B7-H3 between cancer and normal cells; higher fucosylation, higher branching and terminal alpha-galacosylation of N-linked glycans were observed in the cancer cells but not in the normal cells. Moreover, B7-H3 derived from Ca9-22 oral cancer cells had better interaction with the lectin receptors DC-SIGN and Langerin than B7-H3 derived from normal cells. Overall, this study demonstrates that B7-H3 overexpression with characteristic aberrant glycosylation correlates with tumor growth and immune response. | en |
dc.description.provenance | Made available in DSpace on 2021-06-15T13:35:41Z (GMT). No. of bitstreams: 1 ntu-104-D99456001-1.pdf: 9987899 bytes, checksum: 01c651078cea8035feb43892be2460cf (MD5) Previous issue date: 2015 | en |
dc.description.tableofcontents | Table of Contents I
Table of Contents/Figures IV Table of Contents/Tables VI 中文摘要 VII Abstract VIII CHAPTER I INTRODUCTION 1 1.1 Oral Cancer 1 1.1.1 Anatomy 1 1.1.2 Histopathology 2 1.1.3 Risk factors 3 1.1.4 Stage 6 1.1.5 Symptoms and signs 6 1.1.6 Diagnosis 7 1.1.7 Treatment 8 1.1.8 Recurrence and Metastasis 11 1.2 Glycosylation 12 1.2.1 Definition 12 1.2.2 Classification of protein glycosylation 12 1.2.3 Lectins 13 1.2.4 Tumor-associated glycans 14 1.2.5 The specific glycan tagging systems 15 1.3 B7-H3 17 1.3.1 Structure and distribution 17 1.3.2 Function of B7-H3 19 1.3.3 Current reviews of B7-H3 involved in various cancers 20 1.4 Purpose 22 CHAPTER II MATERIALS AND METHODS 30 2.1 Materials 30 2.2 Methods 37 2.2.1 Cell cultures 37 2.2.2 Establishment of stable cell lines 39 2.2.3 RNA preparation and quantitative-PCR 40 2.2.4 Western blot, lectin blotting/staining 40 2.2.5 Glycosidase treatment 41 2.2.6 Immunohistochemistry 42 2.2.7 Cell proliferation assay 44 2.2.8 Wound healing and migration assay 44 2.2.9 Subcutaneous and orthotopic xenograft models 45 2.2.10 Preparation of Alkyne tagged glycoproteome 46 2.2.11 On-membrane click reaction 47 2.2.12 Identification of glycoproteomes 47 2.2.13 Plasmid construction and purification of FLAG-tagged sB7-H3 and B7-H3 49 2.2.14 In-solution tryptic and chymotryptic digestion, N-glycosite determination, assigning glycopeptides and exoglycosidases treatment 50 2.2.15 Nano-LC-MS/MS 52 2.2.16 Enzyme-linked immunoassay 52 2.2.17 Flow cytometric analysis 54 2.2.18 Statistical analysis 54 CHAPTER III RESULTS 57 3.1 Labeling sialylated glycoproteins in cell lysate 57 3.2 Identification of sialylated glycoproteins in SG and Ca9-22 cells 58 3.3 Expression of B7-H3 in OSCC cell lines and normal oral epithelial cells 58 3.4 Correlation of B7-H3 expression and clinicopathological parameters in OSCC patients 59 3.5 Involvement of B7-H3 in cell proliferation, migration and tumor formation 61 3.6 Glycoform analysis of B7-H3 in Ca9-22 and SG 62 3.7 Identification of terminal alpha-galactose in B7-H3 N-glycans 65 3.8 Involvement of different glycoforms of soluble form B7-H3 in cell function 66 3.9 Innate immune receptors interact with B7-H3 through carbohydrate interaction 67 3.10 Evaluation of the presence of B7-H3 counter-receptors on immune cells 68 3.11 Summary 69 CHAPTER IV DISCUSSIONS 70 4.1 The role of B7-H3 in tumorigenesis 70 4.2 The difference of B7-H3 glycan structures found in cancer versus normal cells 72 4.3 The importance of identifying site-specific glycoforms of B7-H3 74 4.4 The interaction between B7-H3 and innate immune receptors 77 PERSPECTIVE 79 CHAPTER V FIGURES 82 CHAPTER VI TABLES 113 REFERENCES 121 APPENDIX 136 | |
dc.language.iso | en | |
dc.title | B7-H3在口腔癌的表現、醣化修飾及免疫反應 | zh_TW |
dc.title | Glycoprotein B7-H3 Overexpression and Aberrant Glycosylation in Oral Cancer and Immune Response | en |
dc.type | Thesis | |
dc.date.schoolyear | 104-1 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 江俊斌(Chun-Pin Chiang),劉扶東(Fu-Tong Liu),鄧述諄(Shu-Chun Teng),吳漢忠(Han-Chung Wu),蕭宏昇(Michael Hsiao) | |
dc.subject.keyword | CD276抗原,細胞生長,醣定序,末端alpha連結半乳糖, | zh_TW |
dc.subject.keyword | CD276,cell proliferation,glycan sequencing,terminal alpha-galactose, | en |
dc.relation.page | 136 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2016-01-28 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 轉譯醫學博士學位學程 | zh_TW |
顯示於系所單位: | 轉譯醫學博士學位學程 |
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