Versican/PG‐M G3 domain promotes tumor growth and angiogenesis

Zheng, Pan; Wen, Jianping; Ang, Lee Cyn; Wang, Sheng; Viloria-Petit, Alicia; Wang, Yelina; Wu, Yaojiong; Kerbel, Robert S.; Yang, Burton B.

doi:10.1096/fj.03-0545fje

Cited by 153 publications

(150 citation statements)

References 46 publications

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“…Previously, the versican G3 domain was found to be important in astrocytoma cell proliferation, glioma adhesion, tumour growth and angiogenesis (Wu et al, 2002(Wu et al, , 2004aZheng et al, 2004). Our results indicate that the V0/V1 isoforms modulate glioma migration through their common GAGb-domain.…”

Section: Discussionsupporting

confidence: 54%

“…Cleavage of brevican, another member of the lectican family by ADAMTS-5 is functionally involved in glioma invasion in vivo (Nakada et al, 2005). There is a strong likelihood that breakdown products of versican will also have biological activity in glioma probably paving the way for the invasion into tissue (Zheng et al, 2004). However, it is not entirely clear if proteolytic degradation of versican by MMP-2 and ADAMTS-1 and 4 induced by TGF-b2 has a pathophysiological role in glioma progression.…”

Section: Discussionmentioning

confidence: 99%

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The role of versican isoforms V0/V1 in glioma migration mediated by transforming growth factor-β2

et al. 2007

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Versican is a large chondroitin sulphate proteoglycan produced by several tumour cell types, including high-grade glioma. The increased expression of certain versican isoforms in the extracellular matrix (ECM) plays a role in tumour cell growth, adhesion and migration. Transforming growth factor-b2 (TGF-b2) is an important modulator of glioma invasion, partially by remodeling the ECM. However, it is unknown whether it interacts with versican during malignant progression of glioma cells. Here, we analysed the effect of TGF-b2 on the expression of versican isoforms. The expression of versican V0/V1 was upregulated by TGF-b2 detected by quantitative polymerase chain reaction and immunoprecipitation, whereas V2 was not induced. Using time-lapse scratch and spheroid migration assays, we observed that the glioma migration rate is significantly increased by exogenous TGF-b2 and inhibited by TGF-b2-specific antisense oligonucleotides. Interestingly, an antibody specific for the DPEAAE region of glycosaminoglycan-b domain of versican was able to reverse the effect of TGF-b2 on glioma migration in a dose-dependent manner. Taken together, we report here that TGF-b2 triggers the malignant phenotype of high-grade gliomas by induction of migration, and that this effect is, at least in part, mediated by versican V0/V1.

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Section: Discussionsupporting

confidence: 54%

Section: Discussionmentioning

confidence: 99%

The role of versican isoforms V0/V1 in glioma migration mediated by transforming growth factor-β2

et al. 2007

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“…46 In PyMT ϩ mammary tumors, the apoptotic index was lower in Adamts1 ϩ/ϩ than in Adamts1 Ϫ/Ϫ tumors, despite equivalent vascular density and cleaved versican accumulated in peritumoral stroma. The liberated G3 domain of cleaved versican has EGF-like activity [47][48][49] and might act as an EGF-like signal in the Adamts1 ϩ/ϩ tumor microenvironment, resulting in reduced apoptosis and increased tumor growth compared with null littermates.…”

Section: Discussionmentioning

confidence: 99%

The ADAMTS1 Protease Gene Is Required for Mammary Tumor Growth and Metastasis

Ricciardelli

Frewin

Tan

et al. 2011

The American Journal of Pathology

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The A disintegrin and metalloprotease with thrombospondin motifs (ADAMTS) family of proteins is composed of extracellular metalloproteases, including ADAMTS1, originally identified in cachexigenic colon cancer cells. 1,2 Mice with Adamts1-null mutation exhibit urogenital defects and female infertility because of impaired remodeling of ovarian extracellular matrix (ECM), but ovarian steroid production and lactation are normal. 3-5 A range of ECM proteins have been identified as potential ADAMTS1 substrates, including collagens, 6 nidogen, 7 and syndecan-4 8 ; however, the proteoglycans versican and aggrecan have been consistently shown to be key ADAMTS1 targets. 4,9,10 ADAMTS1 processing of versican is important in cell migration during wound healing, 11 endothelial cell invasion, 12 and remodeling of cardiac jelly ECM during heart morphogenesis. 13 These observations indicate that ADAMTS1 mediates acute regulated tissue remodeling processes that occur in development and in adult reproductive tissues, but also in cancer growth and metastasis.Emerging evidence associates ADAMTS1 expression with metastatic potential. Elevated expression of ADAMTS1 is characteristic of breast cancer cell lines 14,15 and human breast cancers with high bone metastatic potential. 16 Likewise, local invasion and lymph node metastasis of pancreatic cancer is associated with elevated Adamts1. 17 Overexpression of full-length ADAMTS1 in

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“…Recently, we have demonstrated that versican G3 domain enhances tumor growth and angiogenesis, perhaps through enhancement of fibronectin expression [71]. We then investigated the possibility that the G3 domain interacts with fibronectin.…”

Section: Versican Interaction With Fibronectinmentioning

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/PG‐M G3 domain promotes tumor growth and angiogenesis

Cited by 153 publications

References 46 publications

The role of versican isoforms V0/V1 in glioma migration mediated by transforming growth factor-β2

The role of versican isoforms V0/V1 in glioma migration mediated by transforming growth factor-β2

The ADAMTS1 Protease Gene Is Required for Mammary Tumor Growth and Metastasis

The interaction of versican with its binding partners

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