Volume 15, No 7, Jul 2005

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 15 Issue 7, July 2005: 483-494

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The interaction of versican with its binding partners

Yao Jiong WU^1,3, David P. LA PIERRE^1,3, Jin WU², Albert J. YEE¹, Burton B. YANG^{1, 3,*}

¹Sunnybrook & Women's College Health Sciences Centre, 2075 Bayview Avenue, Toronto M4N 3M5 Canada


²School of Chinese Medicine, The University of Hong Kong, Hong Kong SAR, China


³Department of Laboratory Medicine and Pathobiology, University of Toronto, Canada Correspondence: Burton B. YANG(Burton.Yang@sw.ca)

Versican belongs to the family of the large aggregating chondroitin sulfate proteoglycans located primarily within the extracellular matrix (ECM). Versican, like other members of its family, has unique N- and C-terminal globular regions, each with multiple motifs. A large glycosaminoglycan-binding region lies between them. This review will begin by outlining these structures, in the context of ECM proteoglycans. The diverse binding partners afforded to versican by virtue of its modular design will then be examined. These include ECM components, such as hyaluronan, type I collagen, tenascin-R, fibulin-1, and -2, fibrillin-1, fibronectin, P- and L-selectins, and chemokines. Versican also binds to the cell surface proteins CD44, integrin b1, epidermal growth factor receptor, and P-selectin glycoprotein ligand-1. These multiple interactors play important roles in cell behaviour, and the roles of versican in modulating such processes are discussed.

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