4.5 Article

Glucuronic acid can extend O-linked core 1 glycans, but it contributes only weakly to the negative surface charge of Drosophila melanogaster Schneider-2 cells

期刊

FEBS LETTERS
卷 582, 期 11, 页码 1593-1598

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.04.003

关键词

glucuronic acid; glycoprotein; O-glycosylation; Drosophila melanogaster

向作者/读者索取更多资源

Previous studies of the mucin-type O-glycome of the fruit fly Drosophila melanogaster have revealed a restricted pattern of neutral core-type glycans corresponding to the Tn-(Gal-NAc alpha) and the T-antigen (Gal beta 1-3GalNAc alpha). In particular, no extension of the core 1 glycan with acidic sugars, like sialic acid, was detected. Here we report on the identification of an acidic O-linked trisaccharide expressed on secreted endogenous and recombinant glycoproteins of the embryonal hemocyte-like Drosophila Schneider-2 (S2) cell line. The glycan is composed of glucuronic acid, galactose and N-acetylgalactosamine and its structure was determined as GlcA1-3Gal1-3GalNAc. The O-linked trisaccharide resembles the peripheral structures of acidic D. melanogaster glycosphingolipids. Glucuronic acid may substitute for sialic acid in this organism, however its expression on the S2 cell surface may only marginally contribute to the negative surface charge as revealed by free-flow cell electrophoresis prior to and after beta-glucuronidase treatment of the cells. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据