系統識別號 U0026-2306201113324100
論文名稱(中文) 口腔癌細胞特定位點氮基醣鏈之分析
論文名稱(英文) Site-specific N-glycan Analysis of Oral Cancer Cell
校院名稱 成功大學
系所名稱(中) 醫學檢驗生物技術學系碩博士班
系所名稱(英) Department of Medical Laboratory Science and Biotechnology
學年度 99
學期 2
出版年 100
研究生(中文) 張逸敏
研究生(英文) Yi-Min Chong
學號 T36984051
學位類別 碩士
語文別 英文
論文頁數 90頁
口試委員 指導教授-張權發
中文關鍵字 氮基醣鏈  核心岩藻醣化  唾液酸醣化  口腔癌 
英文關鍵字 N-glycan  Core-fucosylation  Sialylation  Oral Cancer 
中文摘要 在真核細胞內超過半數的蛋白質會被醣化,而這些醣類結構的改變在癌症的病程發展中扮演了重要的角色。在實驗中,我們分析了三種不同狀態的細胞上的氮基醣鏈,包括正常人類初代口腔細胞 (HOK)、正常口腔齒齦細胞株 (SG) 和人類口腔癌細胞株(OC2)。利用化學標定的方式,我們偵測在這三株細胞內的兩群組酵素的活性:岩藻醣轉移酶 (fucosyltransferases, FUT)和唾液酸轉移酶 (sialyltransferases, ST)。接著我們進一步利用即時定量聚合酶連鎖反應來偵測各個岩藻醣轉移酶和唾液酸轉移酶的mRNA的表現量。相較於HOK和SG這兩個正常細胞株,OC2具有較高的FUT8表現量,其整體唾液酸轉移酶(ST)的表現量也是較高的。接著我們利用質譜的方式去分析細胞上方的氮基醣鏈,發現OC2上含有較豐富的核心岩藻醣化 (core-fucosylated) 以及唾液酸醣化 (sialylated) 的氮基醣鏈 (complex type),然而HOK和SG上是以高甘露醣鏈 (high mannose) 類型的氮基醣鏈為主。從上述實驗結果,我們推論蛋白質上的唾液酸醣化以及核心岩藻醣化對於口腔癌的病程發展可能具有一定的意義。進一步利用凝集素親和性層析法純化和質譜儀,我們純化並鑑定了OC2當中有核心岩藻醣化的蛋白質。其中,參與在密切參與在細胞間交互作用和細胞移行的蛋白質分子例如basigin、ALCAM、4F2和integrins可做為未來探討口腔癌生物標誌的參考。
英文摘要 More than half proteins in eukaryotes are glycosylated. Alteration of glycosylation in glycoproteins is known to involve in mediating key pathophysiological events during tumorigenesis. In this study, we aimed to establish a MS based strategy for glycomic mapping and sequencing for cell lines and investigated the N-glycosylation status of OC2 (oral cancer cells), SG cells (Smulow-Glikcman gingival cells) which were immortalized from normal human gingival and HOK (primary human oral keratinocytes). The semiquantitative mRNA results indicated that OC2 have higher FUT8 and overall sialyltransferases mRNA levels compared to HOK and SG cells. In addition, we analyzed the cell surface N-glycan profiles and monosaccharide composition of OC2, SG and HOK cells by MALDI-mass spectrometry and tandem mass spectrometry. We found that the carbohydrate patterns of OC2 were different from SG and HOK cells. The results also indicated that the sialylated and core-fucosylated N-glycans were highly expressed on the cell surface of OC2, whereas the major N-glycans on the SG cells and HOK were high mannose types. Combine these information, we suggested that the α1-6 core fucosylation and terminal sialylation were significant issues during tumorigenesis. Using AAL lectin-affinity chromatography combined with MS, we identified the core-fucosylated proteins that derived from OC2. The key adhesion molecules such as basigin, ALCAM, 4F2 and integrins could be considered as the candidates of potential oral cancer biomarkers in the future studies.
論文目次 摘要 I
Abstract II
Acknowledgement III
Abbreviations IV
Contents VI
List of Figures IX
List of Tables X
Chapter 1 Introduction 1
1-1 Glycosylation 1
1-2 Alteration of Glycosylation in Cancer 4
1-3 Oral Cancer in Taiwan 5
1-4 Introduction of Glycomics & Glycoproteomics 6
1-4.1 Definition of Glycomics & Glycoproteomics 6
1-4.2 Glycoproteomics & Glycomics strategies 6
Chapter 2 Study Objective and Specific Aims 9
2-1 Study Objective 9
2-2 Specific Aims 9
2-3 Study Flow Chart 10
Chapter 3 Experimental Procedures 11
3-1 Cell culture 11
3-2 RNA isolation and real-time quantitative PCR analysis 11
3-3 Metabolic labeling for fluorescent imaging of fucosylated and sialylated glycans 12
3-4 MALDI-MS analysis of permethylated N-glycans 12
3-4.1 Cell membrane preparation and membrane protein extraction 12
3-4.2 Trypsin digestion of proteins 13
3-4.3 Release and purification of N-glycans 13
3-4.4 Permethylation of N-glycans 14
3-4.5 Mass analysis and data evaluation 14
3-5 Lectin affinity chromatography and protein identification 14
3-5.1 AAL – Affinity chromatography 14
3-5.2 TCA protein precipitation 15
3-5.3 SDS-PAGE and gel staining 15
3-5.4 In-gel digestion 16
3-5.5 MS analysis and proteins identification 16
Chapter 4 Results 17
4-1 Metabolic labeling of fucosylated and sialylated glycoproteins in HOK, SG and OC2 cells. 17
4-2 Expression levels of fucosyltransferase genes in HOK, SG and OC2 cells. 18
4-3 Expression levels of sialyltransferase genes in HOK, SG and OC2 cells. 18
4-4 N-glycome analysis in HOK, SG and OC2 cells. 19
4-4.1 MS analysis of N-glycan pools 19
4-4.2 The MS/MS analysis of N-glycan pools 21
4-5 Enrichment and identification of core-fucosylated glycoproteins in OC2 cells. 23
Chapter 5 Discussions 24
5-1 Alteration of fucosylated and sialylated glycoconjugates in cancer 24
5-2 The cell models in this work 25
5-3 The transcript levels of fucosyltransferase and sialyltransferase family in HOK, SG and OC2 cells. 25
5-4 The biological roles of FUT8 in OC2 cells. 26
5-5 The N-glycome analysis in HOK, SG and OC2 cells. 27
5-6 Enrichment and identification of core-fucosylated glycoproteins in OC2 cells. 28
Conclusion 32
References 33
Figures and Figure legends 42
Table 58
Appendix -1 84
Appendix -2 85
Appendix -3 86
Appendix -4 87
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