Changes of serum-associated fucosylated glycoproteins and changes in glycosylation of IgA in human cirrhosis
Changes of serum-associated fucosylated glycoproteins and changes in glycosylation of IgA in human cirrhosis
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DOI：
10.1002/prca.200800213
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发表时间：
2009-05-01
影响因子：
2
通讯作者：
Morelle, Willy
中科院分区：
文献类型：
--
作者：
Carre, Yoann;Klein, Andre;Morelle, Willy
在肝硬化中已经证实了许多N-糖基化修饰。这些修饰对应于平分核心α（1，6）-岩藻糖基化双层聚糖的增加、核心岩藻糖基化的增加以及肝硬化患者血清中存在重要的中性低聚糖群体。本研究采用凝集素亲和层析、MALDI-TOF MS、一维和二维PAGE、电喷雾离子化四极杆离子阱（ESI-QIT）质谱等技术对肝硬化患者血清岩藻糖基化糖蛋白进行鉴定。采用这种方法，我们已经表明，伊加是一个主要的蛋白质，是负责观察到的糖基化修饰的糖尿病患者的血清N-糖。据我们所知，这是第一次，异常的N-糖基化IgA肝硬化的描述。
Many modifications in N-glycosylation have been demonstrated in hepatic cirrhosis. These modifications correspond to an increase of a bisecting core alpha (1,6)-fucosylated biantermary glycan, an increase in core fucosylation, and the presence of an important population of neutral oligosaccharides in human serum of cirrhotic patients. In this study, a glycoproteomic approach which consists of lectin affinity chromatography, MALDI-TOF MS for the characterization of N-glycans released from glycoproteins, one- and 2-D PAGE, electrospray ionization quadrupole ion trap (ESI-QIT) MS was used to identify serum fucosylated glycoproteins related to cirrhosis. Employing this method, we have shown that IgA is one of the major proteins that is responsible of the glycosylation modifications observed in the serum N-glycome of cirrhotic patients. To our knowledge, this is the first time that aberrant N-glycosylation of IgA in cirrhosis is described.