Syndecans as cell surface receptors: Unique structure equates with functional diversity

被引:121
作者
Choi, Youngsil [1 ]
Chung, Heesung [1 ]
Jung, Heyjung [1 ]
Couchman, John R. [2 ]
Oh, Eok-Soo [1 ]
机构
[1] Ewha Womans Univ, Dept Life Sci, Div Life & Pharmaceut Sci, Ctr Cell Signaling & Drug Discovery Res, Seoul 120750, South Korea
[2] Univ Copenhagen, Dept Biomed Sci, Fac Hlth Sci, DK-2200 Copenhagen N, Denmark
基金
新加坡国家研究基金会; 英国医学研究理事会;
关键词
HEPARAN-SULFATE CHAINS; GLAND EPITHELIAL-CELLS; CYTOSKELETAL ORGANIZATION; TRANSMEMBRANE DOMAIN; CHONDROITIN SULFATE; SOLUBLE SYNDECAN-1; CRYSTAL-STRUCTURE; BINDING DOMAIN; GROWTH-FACTORS; FACTOR-ALPHA;
D O I
10.1016/j.matbio.2010.10.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
An increasing number of functions for syndecan cell surface heparan sulfate proteoglycans have been proposed over the last decade. Moreover, aberrant syndecan regulation has been found to play a critical role in multiple pathologies, including cancers, as well as wound healing and inflammation. As receptors, they have much in common with other molecules on the cell surface. Syndecans are type I transmembrane molecules with cytoplasmic domains that link to the actin cytoskeleton and can interact with a number of regulators. However, they are also highly complex by virtue of their external glycosaminoglycan chains, especially heparan sulfate. This heterodisperse polysaccharide has the potential to interact with many ligands from diverse protein families. Here, we relate the structural features of syndecans to some of their known functions. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:93 / 99
页数:7
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