6A8α-甘露糖苷酶表达对Jurkat细胞粘附性的影响
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摘要
蛋白质糖基化在细胞的功能行为中起重要的作用。本实验室以往克隆到了1个新的人α-甘露糖苷酶cDNA(6A8)，并观察到了6A8α-甘露糖苷酶表达抑制影响包括Jurkat细胞在内的多种细胞的生物学行为。在预实验中观察到6A8α-甘露糖苷酶表达抑制的Jurkat细胞(AS)在培养中聚集成大的团块，这提示AS细胞间的粘附性增强。为研究其机制，首先用含有粘附分子和其它免疫分子基因在内的440个基因的DNA芯片对AS和M细胞(转导空载体的对照细胞)间的基因表达差异作了分析，见AS细胞有19个基因的表达上调，有20个基因的表达下调。表达上调的基因中包括CD11a(整合素α-L)、CD54(ICAM-1)、CD82、CD24、CD11c(整合素α-X)、整合素α-7、CD103(整合素α-E)、TNFSF9、IL-1R和IL-2Rγ等与细胞间粘附相关的基因。RT-PCR和免疫荧光染色支持芯片的结果。这些基因中以CD54和CD11a最为重要。本论文工作中对它们作了重点研究。与对照细胞(野生型细胞W与M细胞)相比，AS细胞与包被有CD54分子的培养板的粘附增强。封闭性CD11a单抗能阻断细胞与包被有CD54分子的培养板的粘附及细胞间的粘附。这证明了CD54和CD11a表达增强参与AS细胞间粘附增强。AS细胞LFA-1分子的亲和力也增高。另外，AS细胞间的粘附增强也与细胞骨架排列改变相关。异种细胞间的粘附在免疫应答等的生命活动中也起重要的作用。在对AS细胞与对照细胞和Raji细胞间粘附的比较中，观察到前者和Raji细胞间的粘附增强。在超抗原SEB存在下，Jurkat细胞与Raji细胞间可形成免疫突触，并有信号传导发生。6A8α-甘露糖苷酶的功能是修剪N-糖链中的甘露糖，Con A结合实验能检测细胞糖蛋白N-糖链中的甘露糖被α-甘露糖苷酶修剪的程度。与对照细胞相比，Con A与AS细胞的结合明显增强。关于6A8α-甘露糖苷酶表达抑制所致的蛋白质糖基化改变影响Jurkat细胞粘附性的确切机制须作深入研究。
Glycosylation of protein plays important roles in the function of cells. In thislaboratory, a cDNA (6A8) encoding a new humanα-mannosidase has been isolated. It hasbeen previously found that biological activities are affected by the inhibition of 6A8α-mannosidase expression in the cells studied including Jurkat cell. In this study, cell massformation in the Jurkat cells with inhibition of 6A8α-mannosidase expression (AS cell)was observed. It suggested an enhancement of adhesion among the AS cells. In order tofind clues for studying the mechanisms, mRNA differential display analysis was performedbetween AS cell and a control M cell (the Jurkat cell-tranduced with a mock) on a DNAchip containing 440 genes including those encoding a number of adhesion and immunemolecules. Nineteen genes were found to be up-regulated and 20 genes be down-regulated.The genes which were up-regulated included CD11a, CD54, CD82, CD24, CD11c, intgrinα-7, CD103, TNFSF9, IL-1R and IL-2Rγ. They were related to cell-cell adhesion. The datafrom DNA chip study were confirmed by the RT-PCR and the immunofluorescencestaining analysis. Among the genes mentioned, CD54 and CD11a are the most important.Thus, this study concentrated on the role played by them in the adhesion enhancementamong AS cells. In comparing to the controls, the wild-type cell (W) and the M cell, AScell showed an enhancement of adhesion to the plate coated with CD54 molecules. Inaddition, the blocking CD11a antibody could block the adhesion and the adhesion amongthe Jurkat cells. These data demonstrated the role played by the enhancement of CD54 andCD11a expression in the adhesion enhancement among AS cells. In addition, an increase ofaffinity in CD11a molecule was also observed in AS cell. Moreover, cytoskeleton in AScell was found to be rearranged. Since cell-cell adhesion is also related to cytoskeleton, itcould be suggested that the rearrangement would play roles in the enhancement of AS celladhesion. Adhesion between heterogeneous cells also plays important roles in life activities, such as immune response etc. Adhesion between AS cell and Raji cell was observed to beenhanced in comparison to that between the control and Raji cell. At the presence of thesuperantigen SEB, immune synapse was formed between Jurkat cell and Raji cell.
The function ofα-mannosidase is to trim the mannoses in the N-glycan ofglycoproteins. The high mannose structure in the N-glycan is the receptor of ConA. Thus,ConA binding assay could be used to detect the extent of mannose trimming byα-mannosidase in the N-glycan of glycoproteins. In my study, an enhancement of ConAbinding to the AS cells was observed. Of course, the mechanisms of the effect of thealternation of glycosylation resulted from the inhibition of 6A8α-mannosidase expressionon the adhesiveness of Jurkat cells remains to be discovered in the future.
Glycosylation of protein plays important roles in the function of cells. In thislaboratory, a cDNA (6A8) encoding a new humanα-mannosidase has been isolated. It hasbeen previously found that biological activities are affected by the inhibition of 6A8α-mannosidase expression in the cells studied including Jurkat cell. In this study, cell massformation in the Jurkat cells with inhibition of 6A8α-mannosidase expression (AS cell)was observed. It suggested an enhancement of adhesion among the AS cells. In order tofind clues for studying the mechanisms, mRNA differential display analysis was performedbetween AS cell and a control M cell (the Jurkat cell-tranduced with a mock) on a DNAchip containing 440 genes including those encoding a number of adhesion and immunemolecules. Nineteen genes were found to be up-regulated and 20 genes be down-regulated.The genes which were up-regulated included CD11a, CD54, CD82, CD24, CD11c, intgrinα-7, CD103, TNFSF9, IL-1R and IL-2Rγ. They were related to cell-cell adhesion. The datafrom DNA chip study were confirmed by the RT-PCR and the immunofluorescencestaining analysis. Among the genes mentioned, CD54 and CD11a are the most important.Thus, this study concentrated on the role played by them in the adhesion enhancementamong AS cells. In comparing to the controls, the wild-type cell (W) and the M cell, AScell showed an enhancement of adhesion to the plate coated with CD54 molecules. Inaddition, the blocking CD11a antibody could block the adhesion and the adhesion amongthe Jurkat cells. These data demonstrated the role played by the enhancement of CD54 andCD11a expression in the adhesion enhancement among AS cells. In addition, an increase ofaffinity in CD11a molecule was also observed in AS cell. Moreover, cytoskeleton in AScell was found to be rearranged. Since cell-cell adhesion is also related to cytoskeleton, itcould be suggested that the rearrangement would play roles in the enhancement of AS celladhesion. Adhesion between heterogeneous cells also plays important roles in life activities, such as immune response etc. Adhesion between AS cell and Raji cell was observed to beenhanced in comparison to that between the control and Raji cell. At the presence of thesuperantigen SEB, immune synapse was formed between Jurkat cell and Raji cell.
The function ofα-mannosidase is to trim the mannoses in the N-glycan ofglycoproteins. The high mannose structure in the N-glycan is the receptor of ConA. Thus,ConA binding assay could be used to detect the extent of mannose trimming byα-mannosidase in the N-glycan of glycoproteins. In my study, an enhancement of ConAbinding to the AS cells was observed. Of course, the mechanisms of the effect of thealternation of glycosylation resulted from the inhibition of 6A8α-mannosidase expressionon the adhesiveness of Jurkat cells remains to be discovered in the future.
引文
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