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

Youngsil Choi, Heesung Chung, Heyjung Jung, John R. Couchman, Eok Soo Oh

Research output: Contribution to journalArticlepeer-review

132 Scopus citations


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.

Original languageEnglish
Pages (from-to)93-99
Number of pages7
JournalMatrix Biology
Issue number2
StatePublished - Mar 2011

Bibliographical note

Funding Information:
This study was supported by a grant of the Korea Healthcare technology R&D Projects, Ministry for Health, Welfare, and Family Affairs, Republic of Korea ( A084292 ). JRC is supported by the Danish National Research Foundation , the Danish Medical Research Council , the Lundbeck Foundation , Fabrikant Vilhelm Pedersen og Hustrus Legat through Novo Nordisk Fonden , the Mizutani Foundation and the Department of Biomedical Sciences at The University of Copenhagen .


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