A Study on the Interactions Between Heparan Sulfate Proteoglycans and Wnt Proteins

被引：88

作者：

Fuerer, Christophe ^{[1
]}

Habib, Shukry J. ^{[1
]}

Nusse, Roel ^{[1
]}

机构：

[1] Stanford Univ, Sch Med, Dept Dev Biol, Howard Hughes Med Inst, Stanford, CA 94305 USA

来源：

DEVELOPMENTAL DYNAMICS | 2010年 / 239卷 / 01期

基金：

瑞士国家科学基金会;

关键词：

HSPG; Wnt; FBS; aggregation; solubility; XENOPUS-EMBRYOS; GASTRULATION MOVEMENTS; LIPOPROTEIN PARTICLES; INT-1; PROTOONCOGENE; GRADIENT FORMATION; AXIS FORMATION; DALLY-LIKE; WINGLESS; DROSOPHILA; HEDGEHOG;

D O I：

10.1002/dvdy.22067

中图分类号：

R602 [外科病理学、解剖学]; R32 [人体形态学];

学科分类号：

100101 ;

摘要：

The Wnt signaling pathway plays key roles in development and adult homeostasis. Wnt proteins are secreted, lipid-modified glycoproteins. They can form morphogen gradients that are regulated at the level of protein secretion, diffusion, and internalization. These gradients can only exist if the hydrophobic Wnt proteins are prevented from aggregating in the extracellular environment. Heparan sulfate proteoglycans (HSPGs) are necessary for proper activity of Wnt proteins and influence their distribution along the morphogenetic gradient. In this study, we show that HSPGs are able to maintain the solubility of Wnt proteins, thus stabilizing their signaling activity. Our results suggest that the role of HSPGs is not only to concentrate Wnt molecules at the cell surface but also to prevent them from aggregating in the extracellular environment. Developmental Dynamics 239:184-190, 2010. (C) 2009 Wiley-Liss, Inc.

引用

页码：184 / 190

页数：7

共 39 条

[1] QSulf1 remodels the 6-O sulfation states of cell surface heparan sulfate proteoglycans to promote Wnt signaling [J].