肝细胞癌患者血清糖蛋白质组及其糖链结构研究
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摘要
国际癌症研究机构的最新资料表明,肝细胞癌(Hepatocellular Carcinoma,HCC)是全球最常见的五种恶性肿瘤之一。从2009年起恶性肿瘤致死率已跃居我国主要疾病死亡率的首位,而其中HCC排在恶性肿瘤死亡率的第二位。HCC死亡率高的原因之一是当前肝癌的确诊通常是在晚期,因而错过了最佳的治疗时期,因此寻找一种能在发生早期快速灵敏的诊断HCC的方法就显得尤为必要。利用蛋白质组学和糖组学技术对HCC发生过程中糖蛋白及其糖基化修饰进行深入的研究,可以揭示糖蛋白在肝癌发生过程中作用和功能,探究HCC发生的分子机理,并促进临床诊断方法的发展。
第一部分：通过对Fe304磁性粒子的硅烷化修饰制备出了环氧化磁性微粒,并建立了一套利用环氧化磁性微粒制备凝集素-磁性微粒复合物(LMPCs)的方法。经表征,制备的环氧化磁性微粒是一种粒径相对均一,d(0.5)为3.50μm,饱和磁化强度为69.55emu/g,比表面积为96.29m2/g,且表面具有丰富环氧基团的超顺磁性材料。通过条件优化,在保持凝集素生物活性的前提下,确定1g磁性微粒最多可以固定186.31±5.16mg伴刀豆球蛋白凝集素(ConA)。
第二部分：利用制备的LMPCs建立了一种简单快速且高通量的凝集素-磁性微粒复合物分离N-连接糖蛋白的方法(N-glyco-LMPCs),并与质谱技术联用同时鉴定和解析糖蛋白及其糖链结构。通过CMPCs对模式蛋白中糖蛋白核糖核酸酶B(RNase B)的分离及结构鉴定,获得了分离的RNase B的蛋白酶切图谱,分析了其糖型的微不均一性。利用CMPCs分离健康志愿者和HCC患者血清中的糖蛋白,并利用质谱技术对分离的糖蛋白及其糖链结构进行鉴定和分析。最终从健康志愿者和HCC患者血清分别鉴定到93和85种糖蛋白,并且有21种糖蛋白只在健康志愿者血清中鉴定到,另外有13种糖蛋白只在HCC患者血清中鉴定到。同时从健康志愿者和HCC患者血清分离的糖蛋白上分别鉴定到28和30种糖链结构,并且有10种糖链结构只在健康志愿者血清中鉴定到,另外有12种糖链结构只在HCC患者血清中鉴定到。这种健康志愿者和HCC患者血清中糖蛋白和糖链结构差异被用凝集素印迹技术(lectin blotting),蛋白质印迹技术(western blott ing)和凝集素/糖抗体芯片技术(lectin/glyco-antibody microarrays)验证。结果显示健康志愿者和HCC患者血清中糖蛋白的差异不仅是蛋白质表达水平差异,且其糖基化修饰水平也存在明显差异。
第三部分：利用单凝集素-磁性微粒复合物(S-LMPCs)和多凝集素-磁性微粒复合物(M-LMPCs)的N-glyco-LMPCs法结合质谱技术分离和鉴定健康志愿者和HCC患者血清中的糖蛋白,并利用emPAI方法对两种血清中分离的糖蛋白进行定量分析。两种方法从健康志愿者和HCC患者血清中共鉴定到371种N-连接糖蛋白,且结果显示不同糖蛋白与四种凝集素(伴刀豆凝集素A,Con A;扁豆凝集素,LCA；橙黄网胞盘菌凝集素,AAL；麦胚凝集素,WGA)的结合具有特异性,初步显示了糖蛋白的糖链结构,揭示了HCC发生过程中一些糖链微结构的变化。通过非标记emPAI;定量分析,发现有315种(84.9%)糖蛋白的丰度在HCC发生过程中没有发生或者发生了很小的变化,另外有49种(13.2%)糖蛋白在HCC患者血清中高表达,有27种(7.3%)糖蛋白在HCC患者血清中低表达。其中高表达的糖蛋白中包括已经作为肝癌诊断标志物的α-甲胎蛋白以及补体蛋白C6(Component C6),免疫球蛋白轻链C(Ig mu chain C),β-2-糖蛋白(β-2-glycoprotein),G蛋白偶联受体(G-protein coupled receptor)等重要的HCC潜在标志物。第四部分：采用滤膜辅助的凝集素分离糖蛋白糖肽法(N-glyco-FASP)对健康志愿者和HCC患者血清中N-连接糖蛋白及其糖基化位点进行鉴定和分析。两种血清中共鉴定出137条N-连接糖肽,包含144个N-连接糖基化位点,分别来自74种糖蛋白,其中只出现在健康志愿者血清中的糖基化位点有54个,只出现在HCC癌患者血清中的糖基化位点有53个。经该方法富集后的糖肽占鉴定到的多肽的28%,相对于富集前提高了近60倍。结合N-glyco-LMPCs分离鉴定到的糖蛋白,从血清中共鉴定出451种糖蛋白,其中在健康志愿者血清中鉴定出305种,HCC患者血清中鉴定出298种,使血清中糖蛋白鉴定的覆盖率得到提高。经功能分析,发现这些糖蛋白主要分子功能是结合,催化以及酶调节活性；主要参与细胞过程,刺激应答,生物调节和代谢过程；并且主要分布在细胞中,细胞外区域,以及细胞器中。经过对只在HCC患者血清中鉴定出的蛋白质进行功能聚类分析后发现,这些蛋白主要是一类分泌性,并具有信号肽序列的糖蛋白。
第五部分：采用滤膜辅助分离全糖蛋白N-连接糖链法(N-glycan-FASP-T)和滤膜辅助的凝集素分离糖蛋白N-连接糖链法(N-glycan-FASP-L)对健康志愿者和HCC患者血清中全糖蛋白N-连接糖链和凝集素结合的糖蛋白N-连接糖链分别进行比较分析,并利用MALDI-TOF/TOF串联质谱解析糖链结构。其中两种血清经N-glycan-FASP-T法分析共鉴定出26种,且主要分布在小分子量范围；通过N-glycan-FASP-L法分析共鉴定出24种,其分布更均匀,糖链鉴定范围相对更广。其中用N-glycan-FASP-T法分析中有9种糖链同时在两种血清中鉴定到,N-glycan-FASP-L法分析中也有9种糖链同时在两种血清中鉴定到。经分析后发现无论是单独在HCC患者血清中鉴定到的(6/16)或者是初步定量分析后在HCC中相对高表达的糖链(4/5)均主要是岩藻糖化修饰的糖链。N-glycan-FASP-T法和N-glycan-FASP-L法两种分析策略对糖链的鉴定具有一定的偏好性,可以相互补充更好地分析与HCC发生相关的糖链结构。
The International Agency for Research on Cancer (IARC) indicated that Hepatocellular Carcinoma (HCC) was one of the top five prevalent primary malignant tumors. It showed that malignant carcinoma has been the most common cause of disease death and the HCC has been the second most common cause of cancer death in China. The diagnosis of HCC is usually achieved at a late stage, which results in the high mortality. A rapid and sensitive diagnosis method of the HCC would be particularly necessary. The study of the glycoproteomics can reveal the functions of the glycoproteins and explore the molecular mechanism of the HCC, and also devebpe a method for clinical diagnosis.
For the first part:The epoxy-activated magnetic particles were synthesized by modification of the Fe3O4fluids using silaning agent.The method to preparation the lectin-magnetic particle conjugates was established using the home-made epoxy-activated magnetic particle. The epoxy-activated magnetic particles were characterized as uniform superparamagnetism material with3.50μm diameter,69.55emu/g saturation magnetic moments, and96.29m2/g specific surface area. For the biological activated lectin-magnetic particle conjugates preparation (LMPCs), the binding buffer, binding time, binding capacity, and surface coverage were optimized. It was estimated that the each gram of the magnetic particles could be saturated with186.31±5.16mg Concanavalin A (Con A).
For the second part:A simple, rapid and high-throughput method was established for the N-linked glycoprotein isolation using lectin-magnetic particle conjugates (N-glyco-LMPCs). Meantime, combined with the mass spec tro me try could implement the identification and characterization the glycoprteins and glycans in one flow. At first, the strategy was involved in the isolation and identification the glycoprotein RNase B from model protein. The peptide spectra of the RNase B were identified by the MALDI-MS. The microheterogeneity of the glycan on the RNase B was characterized as five glycoform. Additional, the Con A-magnetic particle conjugate-based method was utilized to selectively isolate the glycoproteins and their glycomes from the healthy donor and HCC case sera. Followed the isolated glycoproteins and their JV-linked glycans were identified by LC-ESI-MS/MS and MALDI-TOF/TOF-MS, respectively.93glycoproteins from the healthy donors and85glycoproteins from the HCC cases were identified. There were34different glycoproteins shown between the healthy donors (21/34) and the HCC cases (13/34).28glycans from the healthy donors and30glycans from the HCC cases were detected and there were22different glycans shown between the healthy donors (10/22) and HCC cases (12/22). Moreover, the lectin blotting, western blotting and lectin/glyco-antibody microarrays were applied to definitely elucidate the change of the expressions of selective protein and their glycosylatio n, the results indicated that the differences of the identified glycoproteins between the healthy donors and HCC cases were caused by the change of both protein expression and their glycosylation levels.
For the third part:The glycoproteins of the normal donors and HCC cases sera were isolated by the single-and multi-lectin-magnetic particle conjugates and identified by the high-accuracy ESI-Q-TOF-MS, respectively. The exponentially modified protein abundance index (emPAI) method was applied in the absolute quantification of the glycoproteia371N-linked glycoproteins were identified from the two serum pools. From the results, it showed that the binding specificity of the identified glycoproteins to the four lectins (Con A, Lens Culinaris Agglutinin (LCA), Aleuria Aurantia Lectin (AAL), Wheat Germ Agglutinin (WGA)) and the glycan structures of the identified glycoproteins were tentative estimated. With the stringent criteria emPAI quantification, it indicated that315(84.9%) glycoproteins were no significant difference in the two serum pools. However,49(13.2%) glycoproteins were measured up-regulation and27(7.3%) were down-regulation in the HCC cases. The up-regulation proteins included the verified HCC biomarkers AFP and the potential biomarker Component C6, Ig mu chain C, β-2-glycoprotein, G-protein coupled receptor, and so on.
For the fourth part:We applied the filter aided sample preparation-based N-linked glycopeptides enrichment (N-glyco-FASP) from the healthy donors and HCC cases sera.144N-glycosylation sites were mapped on74proteins in the two serum pools using high-accuracy mass spectrometry. With lectin enrichment, glycopeptides were28%of total peptides, indicating an enrichment factor of nearly60-fold. Combined the N-glyco-LMPCs and the N-glyco-FASP,451proteins were identified in the two serum pools, which305and298proteins were identified from the normal donors and HCC cases sera, respectively. After the analysis of the functional of the proteins by the Blast2Go, It indicated that the mainly molecular function of the protein was binding, catalytic activity, enzyme regulator activity. The proteins mainly located at the cell, the extracellular region, as well as organelle. The biological processes mediated by the proteins were cellular processes, response to stimulus, biological regulation and metabolic process. After the functional cluster analysis of the proteins only identified in the HCC, it showed that the proteins were secreted glycoproteins with signal peptide.
For the fifth part:We developed a filter aided sample preparation-based total glycoprotein N-linked glycans enrichment (N-glycan-FASP-T) and lectin binding glycoprotein N-linked glycans enrichment (N-glycan-FASP-L) from the normal donors and HCC cases sera, respectively. The enriched N-linked glycans were characterized by the MALDI-TOF/TOF-MS to obtain the glycan spectra and structures.26glycans were annotated from the total glycoproteins using N-glycan-FASP-T in the two serum pools, which were centralized in the small molecular weight Additional,24glycans were annotated from the lectin binding glycoproteins using N-glycan-FASP-L in the two serum pools, which distributed more homogeneous and wider. The glycans between the two serum pools were mostly same using the two methods, which9glycans were identified both in the healthy donors and HCC cases sera using N-glycan-FASP-T, and also9glycans for the N-glycan-FASP-L. It showed that the characterized glycans only in the HCC were fucosylated oligosaccharide whatever by qualification (6/16) or by quantification (4/5). The two strategies for the glycan isolation and characterization displayed preference and could be mutual complementation in the study of the glycomics in HCC.
第一部分：通过对Fe304磁性粒子的硅烷化修饰制备出了环氧化磁性微粒,并建立了一套利用环氧化磁性微粒制备凝集素-磁性微粒复合物(LMPCs)的方法。经表征,制备的环氧化磁性微粒是一种粒径相对均一,d(0.5)为3.50μm,饱和磁化强度为69.55emu/g,比表面积为96.29m2/g,且表面具有丰富环氧基团的超顺磁性材料。通过条件优化,在保持凝集素生物活性的前提下,确定1g磁性微粒最多可以固定186.31±5.16mg伴刀豆球蛋白凝集素(ConA)。
第二部分：利用制备的LMPCs建立了一种简单快速且高通量的凝集素-磁性微粒复合物分离N-连接糖蛋白的方法(N-glyco-LMPCs),并与质谱技术联用同时鉴定和解析糖蛋白及其糖链结构。通过CMPCs对模式蛋白中糖蛋白核糖核酸酶B(RNase B)的分离及结构鉴定,获得了分离的RNase B的蛋白酶切图谱,分析了其糖型的微不均一性。利用CMPCs分离健康志愿者和HCC患者血清中的糖蛋白,并利用质谱技术对分离的糖蛋白及其糖链结构进行鉴定和分析。最终从健康志愿者和HCC患者血清分别鉴定到93和85种糖蛋白,并且有21种糖蛋白只在健康志愿者血清中鉴定到,另外有13种糖蛋白只在HCC患者血清中鉴定到。同时从健康志愿者和HCC患者血清分离的糖蛋白上分别鉴定到28和30种糖链结构,并且有10种糖链结构只在健康志愿者血清中鉴定到,另外有12种糖链结构只在HCC患者血清中鉴定到。这种健康志愿者和HCC患者血清中糖蛋白和糖链结构差异被用凝集素印迹技术(lectin blotting),蛋白质印迹技术(western blott ing)和凝集素/糖抗体芯片技术(lectin/glyco-antibody microarrays)验证。结果显示健康志愿者和HCC患者血清中糖蛋白的差异不仅是蛋白质表达水平差异,且其糖基化修饰水平也存在明显差异。
第三部分：利用单凝集素-磁性微粒复合物(S-LMPCs)和多凝集素-磁性微粒复合物(M-LMPCs)的N-glyco-LMPCs法结合质谱技术分离和鉴定健康志愿者和HCC患者血清中的糖蛋白,并利用emPAI方法对两种血清中分离的糖蛋白进行定量分析。两种方法从健康志愿者和HCC患者血清中共鉴定到371种N-连接糖蛋白,且结果显示不同糖蛋白与四种凝集素(伴刀豆凝集素A,Con A;扁豆凝集素,LCA；橙黄网胞盘菌凝集素,AAL；麦胚凝集素,WGA)的结合具有特异性,初步显示了糖蛋白的糖链结构,揭示了HCC发生过程中一些糖链微结构的变化。通过非标记emPAI;定量分析,发现有315种(84.9%)糖蛋白的丰度在HCC发生过程中没有发生或者发生了很小的变化,另外有49种(13.2%)糖蛋白在HCC患者血清中高表达,有27种(7.3%)糖蛋白在HCC患者血清中低表达。其中高表达的糖蛋白中包括已经作为肝癌诊断标志物的α-甲胎蛋白以及补体蛋白C6(Component C6),免疫球蛋白轻链C(Ig mu chain C),β-2-糖蛋白(β-2-glycoprotein),G蛋白偶联受体(G-protein coupled receptor)等重要的HCC潜在标志物。第四部分：采用滤膜辅助的凝集素分离糖蛋白糖肽法(N-glyco-FASP)对健康志愿者和HCC患者血清中N-连接糖蛋白及其糖基化位点进行鉴定和分析。两种血清中共鉴定出137条N-连接糖肽,包含144个N-连接糖基化位点,分别来自74种糖蛋白,其中只出现在健康志愿者血清中的糖基化位点有54个,只出现在HCC癌患者血清中的糖基化位点有53个。经该方法富集后的糖肽占鉴定到的多肽的28%,相对于富集前提高了近60倍。结合N-glyco-LMPCs分离鉴定到的糖蛋白,从血清中共鉴定出451种糖蛋白,其中在健康志愿者血清中鉴定出305种,HCC患者血清中鉴定出298种,使血清中糖蛋白鉴定的覆盖率得到提高。经功能分析,发现这些糖蛋白主要分子功能是结合,催化以及酶调节活性；主要参与细胞过程,刺激应答,生物调节和代谢过程；并且主要分布在细胞中,细胞外区域,以及细胞器中。经过对只在HCC患者血清中鉴定出的蛋白质进行功能聚类分析后发现,这些蛋白主要是一类分泌性,并具有信号肽序列的糖蛋白。
第五部分：采用滤膜辅助分离全糖蛋白N-连接糖链法(N-glycan-FASP-T)和滤膜辅助的凝集素分离糖蛋白N-连接糖链法(N-glycan-FASP-L)对健康志愿者和HCC患者血清中全糖蛋白N-连接糖链和凝集素结合的糖蛋白N-连接糖链分别进行比较分析,并利用MALDI-TOF/TOF串联质谱解析糖链结构。其中两种血清经N-glycan-FASP-T法分析共鉴定出26种,且主要分布在小分子量范围；通过N-glycan-FASP-L法分析共鉴定出24种,其分布更均匀,糖链鉴定范围相对更广。其中用N-glycan-FASP-T法分析中有9种糖链同时在两种血清中鉴定到,N-glycan-FASP-L法分析中也有9种糖链同时在两种血清中鉴定到。经分析后发现无论是单独在HCC患者血清中鉴定到的(6/16)或者是初步定量分析后在HCC中相对高表达的糖链(4/5)均主要是岩藻糖化修饰的糖链。N-glycan-FASP-T法和N-glycan-FASP-L法两种分析策略对糖链的鉴定具有一定的偏好性,可以相互补充更好地分析与HCC发生相关的糖链结构。
The International Agency for Research on Cancer (IARC) indicated that Hepatocellular Carcinoma (HCC) was one of the top five prevalent primary malignant tumors. It showed that malignant carcinoma has been the most common cause of disease death and the HCC has been the second most common cause of cancer death in China. The diagnosis of HCC is usually achieved at a late stage, which results in the high mortality. A rapid and sensitive diagnosis method of the HCC would be particularly necessary. The study of the glycoproteomics can reveal the functions of the glycoproteins and explore the molecular mechanism of the HCC, and also devebpe a method for clinical diagnosis.
For the first part:The epoxy-activated magnetic particles were synthesized by modification of the Fe3O4fluids using silaning agent.The method to preparation the lectin-magnetic particle conjugates was established using the home-made epoxy-activated magnetic particle. The epoxy-activated magnetic particles were characterized as uniform superparamagnetism material with3.50μm diameter,69.55emu/g saturation magnetic moments, and96.29m2/g specific surface area. For the biological activated lectin-magnetic particle conjugates preparation (LMPCs), the binding buffer, binding time, binding capacity, and surface coverage were optimized. It was estimated that the each gram of the magnetic particles could be saturated with186.31±5.16mg Concanavalin A (Con A).
For the second part:A simple, rapid and high-throughput method was established for the N-linked glycoprotein isolation using lectin-magnetic particle conjugates (N-glyco-LMPCs). Meantime, combined with the mass spec tro me try could implement the identification and characterization the glycoprteins and glycans in one flow. At first, the strategy was involved in the isolation and identification the glycoprotein RNase B from model protein. The peptide spectra of the RNase B were identified by the MALDI-MS. The microheterogeneity of the glycan on the RNase B was characterized as five glycoform. Additional, the Con A-magnetic particle conjugate-based method was utilized to selectively isolate the glycoproteins and their glycomes from the healthy donor and HCC case sera. Followed the isolated glycoproteins and their JV-linked glycans were identified by LC-ESI-MS/MS and MALDI-TOF/TOF-MS, respectively.93glycoproteins from the healthy donors and85glycoproteins from the HCC cases were identified. There were34different glycoproteins shown between the healthy donors (21/34) and the HCC cases (13/34).28glycans from the healthy donors and30glycans from the HCC cases were detected and there were22different glycans shown between the healthy donors (10/22) and HCC cases (12/22). Moreover, the lectin blotting, western blotting and lectin/glyco-antibody microarrays were applied to definitely elucidate the change of the expressions of selective protein and their glycosylatio n, the results indicated that the differences of the identified glycoproteins between the healthy donors and HCC cases were caused by the change of both protein expression and their glycosylation levels.
For the third part:The glycoproteins of the normal donors and HCC cases sera were isolated by the single-and multi-lectin-magnetic particle conjugates and identified by the high-accuracy ESI-Q-TOF-MS, respectively. The exponentially modified protein abundance index (emPAI) method was applied in the absolute quantification of the glycoproteia371N-linked glycoproteins were identified from the two serum pools. From the results, it showed that the binding specificity of the identified glycoproteins to the four lectins (Con A, Lens Culinaris Agglutinin (LCA), Aleuria Aurantia Lectin (AAL), Wheat Germ Agglutinin (WGA)) and the glycan structures of the identified glycoproteins were tentative estimated. With the stringent criteria emPAI quantification, it indicated that315(84.9%) glycoproteins were no significant difference in the two serum pools. However,49(13.2%) glycoproteins were measured up-regulation and27(7.3%) were down-regulation in the HCC cases. The up-regulation proteins included the verified HCC biomarkers AFP and the potential biomarker Component C6, Ig mu chain C, β-2-glycoprotein, G-protein coupled receptor, and so on.
For the fourth part:We applied the filter aided sample preparation-based N-linked glycopeptides enrichment (N-glyco-FASP) from the healthy donors and HCC cases sera.144N-glycosylation sites were mapped on74proteins in the two serum pools using high-accuracy mass spectrometry. With lectin enrichment, glycopeptides were28%of total peptides, indicating an enrichment factor of nearly60-fold. Combined the N-glyco-LMPCs and the N-glyco-FASP,451proteins were identified in the two serum pools, which305and298proteins were identified from the normal donors and HCC cases sera, respectively. After the analysis of the functional of the proteins by the Blast2Go, It indicated that the mainly molecular function of the protein was binding, catalytic activity, enzyme regulator activity. The proteins mainly located at the cell, the extracellular region, as well as organelle. The biological processes mediated by the proteins were cellular processes, response to stimulus, biological regulation and metabolic process. After the functional cluster analysis of the proteins only identified in the HCC, it showed that the proteins were secreted glycoproteins with signal peptide.
For the fifth part:We developed a filter aided sample preparation-based total glycoprotein N-linked glycans enrichment (N-glycan-FASP-T) and lectin binding glycoprotein N-linked glycans enrichment (N-glycan-FASP-L) from the normal donors and HCC cases sera, respectively. The enriched N-linked glycans were characterized by the MALDI-TOF/TOF-MS to obtain the glycan spectra and structures.26glycans were annotated from the total glycoproteins using N-glycan-FASP-T in the two serum pools, which were centralized in the small molecular weight Additional,24glycans were annotated from the lectin binding glycoproteins using N-glycan-FASP-L in the two serum pools, which distributed more homogeneous and wider. The glycans between the two serum pools were mostly same using the two methods, which9glycans were identified both in the healthy donors and HCC cases sera using N-glycan-FASP-T, and also9glycans for the N-glycan-FASP-L. It showed that the characterized glycans only in the HCC were fucosylated oligosaccharide whatever by qualification (6/16) or by quantification (4/5). The two strategies for the glycan isolation and characterization displayed preference and could be mutual complementation in the study of the glycomics in HCC.
引文
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