4.6 Article

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

Journal

MATRIX BIOLOGY
Volume 30, Issue 2, Pages 93-99

Publisher

ELSEVIER
DOI: 10.1016/j.matbio.2010.10.006

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Funding

  1. Ministry for Health, Welfare, and Family Affairs, Republic of Korea [A084292]
  2. Danish National Research Foundation
  3. Danish Medical Research Council
  4. Lundbeck Foundation
  5. Fabrikant Vilhelm Pedersen og Hustrus Legat through Novo Nordisk Fonden
  6. Mizutani Foundation
  7. Department of Biomedical Sciences at The University of Copenhagen
  8. Korea Health Promotion Institute [A084292] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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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.

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