Selective inhibition of polysialyltransferase ST8Siall by unnatural sialic acids

被引：41

作者：

Horstkorte, R

Mühlenhoff, M

Reutter, W

Nöhring, S

Zimmermann-Kordmann, M

Gerardy-Schahn, R

机构：

[1] Charite Univ Med Berlin, Inst Mol Biol & Biochem, D-14195 Berlin, Germany

[2] Hannover Med Sch, Abt Zellulare Chem, D-30625 Hannover, Germany

来源：

EXPERIMENTAL CELL RESEARCH | 2004年 / 298卷 / 01期

关键词：

polysialic acid; NCAM; polysialyltransterase;

D O I：

10.1016/j.yexcr.2004.04.014

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Polysialic acid (polySia) is a unique and highly regulated posttranslational modification of the neural cell adhesion molecule (NCAM). The presence of polySia affects NCAM-dependent cell adhesion and plays an important role during brain development, neural regeneration and plastic processes including learning and memory. Polysialylated NCAM is expressed on several neuroendocrine tumors of high malignancy and correlates with poor prognosis. Two closely related enzymes, the polysialyltransferases ST8SiaII and ST8SiaIV, catalyze the biosynthesis of polySia. However, the impact of each enzyme in NCAM polysialylation is not understood. Here, we describe the selective cell-based in vitro inhibition of ST8SiaII using synthetic sialic acid precursors. We provide evidence for different substrate affinities of ST8SiaII and ST8SiaIV. These data open the possibility to study the individual role of the two enzymes during various aspects of brain development and function and in tumorigenesis. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：268 / 274

页数：7

共 35 条

[1] Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide accepters by three distinct α2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III [J].