Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of beta-galactoside alpha 2,6-sialyltransferase.
Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of beta-galactoside alpha 2,6-sialyltransferase.
复制标题
DOI：
--
复制
发表时间：
1989-08
期刊：
影响因子：
--
通讯作者：
E. Lee;J. Rothb;J. Paulson
中科院分区：
文献类型：
--
作者：
E. Lee;J. Rothb;J. Paulson
在本报告中，我们描述了通过表达β -半乳糖苷α2,6 -唾液酸转移酶cDNA来改变中国仓鼠卵巢细胞糖蛋白的N -连接寡糖末端序列。野生型细胞通常产生以NeuAcα2,3Gal键连接终止的糖链，而表达的酶与内源性唾液酸转移酶竞争，连接一种替代的末端序列NeuAcα2,6Gal。通过凝集素 - 金电子显微镜对NeuAcα2,6Gal产物进行亚细胞定位，结果显示其在高尔基体顺面到反面、高尔基体后膜以及囊泡结构中均有定位。这些结果表明，通过“错误表达”与细胞正常产生的内源性酶竞争的末端糖基转移酶，在体内有目的地改变末端碳水化合物结构是有可能的。
In this report we describe the alteration of the N-linked oligosaccharide terminal sequences of Chinese hamster ovary cell glycoproteins by expression of a beta-galactoside alpha 2,6-sialyltransferase cDNA. While wild type cells normally produce sugar chains terminating in the NeuAc alpha 2,3Gal linkage, the expressed enzyme competes with the endogenous sialyltransferase to attach an alternative terminal sequence, NeuAc alpha 2,6Gal. Subcellular localization of the NeuAc alpha 2,6Gal product by lectin-gold electron microscopy revealed localization throughout the Golgi apparatus cis to trans, post-Golgi membranes and vesicular structures. The results demonstrate the potential for purposefully altering terminal carbohydrate structures in vivo by "mis-expressing" terminal glycosyltransferases that compete with the endogenous enzyme normally produced by the cells.