Monoglucosylated glycans in the secreted human complement component C3: implications for protein blosynthesis and structure
Monoglucosylated glycans in the secreted human complement component C3: implications for protein blosynthesis and structure
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DOI：
10.1016/j.febslet.2004.04.045
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发表时间：
2004-05-21
期刊：
影响因子：
3.5
通讯作者：
Rudd, PM
中科院分区：
文献类型：
--
作者：
Crispin, MDM;Ritchie, GE;Rudd, PM
单糖基化的N-连接低聚糖(GLC(1)Man(9)GlcNAc(2))是内质网钙粘蛋白-钙网织蛋白质量控制途径的保留信号。我们在这里报道了这种单糖化的N-糖链存在于人类补体血清糖蛋白C3上。这一发现是首次报道来自非疾病个体的人血清糖蛋白上的单糖化多糖。5%的人C3糖蛋白中存在葡萄糖部分，这表明这个糖基化位点被隔离在蛋白质中，这与之前的研究一致，该研究发现C3上有一个隐蔽的凝集素结合部位，当C3转化为IC3b时，该结合部位会暴露出来。(C)2004年欧洲生化学会联合会。爱思唯尔出版，版权所有。
The monoglucosylated oligomannose N-linked oligosaccharide (Glc(1) Man(9) GlcNAc(2)) is a retention signal for the calnexin-calreticulin quality control pathway in the endoplasmic reticulum. We report here the presence of such monoglucosylated N-glycans on the human complement serum glycoprotein C3. This finding represents the first report of monoglucosylated glycans on a human serum glycoprotein from non-diseased individuals. The presence of the glucose moiety in 5% of the human C3 glycoprotein suggests that this glycosylation site is sequestered within the protein and is consistent with previous studies identifying a cryptic conglutinin binding site on C3 that becomes exposed upon its conversion to iC3b. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.