Biochemical engineering of the N-acyl side chain of sialic acid leads to increased calcium influx from intracellular compartments and promotes differentiation of HL60 cells

被引：16

作者：

Horstkorte, R ^{[1
]}

Rau, K ^{[1
]}

Laabs, S ^{[1
]}

Danker, K ^{[1
]}

Reutter, W ^{[1
]}

机构：

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

来源：

FEBS LETTERS | 2004年 / 571卷 / 1-3期

关键词：

cell adhesion; sialic acid; signal transduction; calcium; galectin-3;

D O I：

10.1016/j.febslet.2004.06.067

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Sialylation of glycoconjugates is essential for mammalian cells. Sialic acid is synthesized in the cytosol from N-acetylmannosamine by several consecutive steps. Using N-propanoylmannosamine, a novel precursor of sialic acid, we are able to incorporate unnatural sialic acids with a prolonged N-acyl side chain (e.g., N-propanoylneuraminic acid) into glycoconjugates taking advance of the cellular sialylation machinery. Here, we report that unnatural sialylation of HL60-cells leads to an increased release of intracellular calcium after application of thapsigargin, an inhibitor of SERCA Ca2+-ATPases. Furthermore, this increased intracellular calcium concentration leads to an increased adhesion to fibronectin. Finally, we observed an increase of the lectin galectin-3, a marker of monocytic differentiation of HL60-cells. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：99 / 102

页数：4

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