Versican G3 domain enhances cellular adhesion and proliferation of bovine intervertebral disc cells cultured in vitro

Yang, Bing; Yang, Burton B.; Erwin, Mark; Ang, Lee Cyn; Finkelstein, Joel; Yee, Albert

doi:10.1016/j.lfs.2003.06.018

Cited by 27 publications

(21 citation statements)

References 54 publications

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“…Furthermore, we investigated the effect of TGF-β 1 on mRNA expression of versican that is a large aggregating proteoglycan mainly distributed in nucleus pulposus. It was reported that the carboxy-terminal G3 domain of versican appears to influence intervertebral disc cell adhesion and proliferation in vitro 18) .…”

Section: Objectivementioning

confidence: 99%

The Relation Between Sox9, TGF-β1, and Proteoglycan in Human Intervertebral Disc Cells

Lee

Kong

Song

et al. 2008

J Korean Neurosurg Soc

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Section: Objectivementioning

confidence: 99%

The Relation Between Sox9, TGF-β1, and Proteoglycan in Human Intervertebral Disc Cells

Lee

Kong

Song

et al. 2008

J Korean Neurosurg Soc

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“…RT-PCR assays were performed as previously described (Yang et al, 2003;Zheng et al, 2004a). Briefly, 2 g of total RNA was used to synthesize cDNA by reverse transcription, a portion of which (equal to 0.2 g of RNA) was used in a PCR with two appropriate primers.…”

Section: Rt-pcr and Pcrmentioning

confidence: 99%

Versican Mediates Mesenchymal-Epithelial Transition

Wang

Pierre

et al. 2006

MBoC

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“…The characteristic features of hyalectans, also termed lecticans, are their similar globular structures at both N-and C-termini [4,16], and their lectin-like activity [17]. This sub-group of proteoglycans contains multiple domains and mediates a variety of cell activities [10,[18][19][20][21][22].…”

Section: Introductionmentioning

confidence: 99%

The interaction of versican with its binding partners

et al. 2005

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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 β1, 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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Versican G3 domain enhances cellular adhesion and proliferation of bovine intervertebral disc cells cultured in vitro

Cited by 27 publications

References 54 publications

The Relation Between Sox9, TGF-β1, and Proteoglycan in Human Intervertebral Disc Cells

The Relation Between Sox9, TGF-β1, and Proteoglycan in Human Intervertebral Disc Cells

Versican Mediates Mesenchymal-Epithelial Transition

The interaction of versican with its binding partners

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