Syndecans as cell surface receptors: Unique structure equates with functional diversity
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Syndecans as cell surface receptors: Unique structure equates with functional diversity. / Choi, Youngsil; Chung, Heesung; Jung, Heyjung; Couchman, John R; Oh, Eok-Soo.
In: Matrix Biology, Vol. 30, No. 2, 01.03.2011, p. 93-9.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Syndecans as cell surface receptors: Unique structure equates with functional diversity
AU - Choi, Youngsil
AU - Chung, Heesung
AU - Jung, Heyjung
AU - Couchman, John R
AU - Oh, Eok-Soo
N1 - Copyright © 2010 International Society of Matrix Biology. Published by Elsevier B.V. All rights reserved.
PY - 2011/3/1
Y1 - 2011/3/1
N2 - 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.
AB - 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.
U2 - 10.1016/j.matbio.2010.10.006
DO - 10.1016/j.matbio.2010.10.006
M3 - Journal article
C2 - 21062643
VL - 30
SP - 93
EP - 99
JO - Matrix Biology
JF - Matrix Biology
SN - 0945-053X
IS - 2
ER -
ID: 33001609