Involvement of stromal proteoglycans in tumour progression

Wegrowski, Yanusz; Maquart, François‐Xavier

doi:10.1016/j.critrevonc.2003.10.005

Cited by 63 publications

(49 citation statements)

References 138 publications

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“…The interaction of tumor cells with their stromal environment is a critical determinant of the growth of that tumor (34,35). Similarly, glioma invasiveness is modulated by cell-to-ECM interactions and ECM degradation by proteases, which are the key determinants of the nature of the tumor microenvironment.…”

Section: Discussionmentioning

confidence: 99%

Tenascin-C Stimulates Glioma Cell Invasion through Matrix Metalloproteinase-12

Sarkar¹,

Nuttall

Liu³

et al. 2006

Cancer Research

131

108

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The capacity of glioma cells to invade extensively within the central nervous system is a major cause of the high morbidity rate of primary malignant brain tumors. Glioma cell invasion involves the attachment of tumor cells to extracellular matrix (ECM), degradation of ECM components, and subsequent penetration into adjacent brain structures. These processes are accomplished in part by matrix metalloproteinases (MMP) within a three-dimensional milieu of the brain parenchyma. As the majority of studies have used a two-dimensional monolayer culture system, we have used a three-dimensional matrix of collagen type I gel to address glioma-secreted proteases, ECM, and invasiveness of glioma cells. We show that in a threedimensional collagen type I matrix, the presence of tenascin-C, commonly elevated in high-grade gliomas, increased the invasiveness of glioma cells. The tenascin-C-mediated invasiveness was blocked by metalloproteinase inhibitors, but this did not involve the gelatinases (MMP-2 and MMP-9) commonly implicated in two-dimensional glioma growth. A thorough analysis of 21 MMPs and six members of a disintegrin and metalloproteinase domain showed that MMP-12 was increased in gliomas by tenascin-C in three-dimensional matrix. Furthermore, examinations of resected specimens revealed high MMP-12 levels in the high-grade glioblastoma multiforme tumors. Finally, a function-blocking antibody as well as small interfering RNA to MMP-12 attenuated the tenascin-C-stimulated glioma invasion. These results identify a new factor, MMP-12, in regulating glioma invasiveness through interaction with tenascin-C. (Cancer Res 2006; 66(24): 11771-80)

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Section: Discussionmentioning

confidence: 99%

Tenascin-C Stimulates Glioma Cell Invasion through Matrix Metalloproteinase-12

Sarkar¹,

Nuttall

Liu³

et al. 2006

Cancer Research

131

108

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“…Biological importance of CS gives rise currently to substantial efforts for development, improvement and implementation of efficient protocols and methods for their expression, structure and noncovalent interaction determination, among which, mass spectrometry (MS) is considered one of the most valuable [10].…”

Section: Introductionmentioning

confidence: 99%

Discrimination of GalNAc (4S/6S) sulfation sites in chondroitin sulfate disaccharides by chip-based nanoelectrospray multistage mass spectrometry

et al. 2009

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Sulfation pattern within chondroitin sulfate (CS) glycosaminoglycan (GAG) chains is an important post-translational modification that regulates their interaction with proteins. In this context, development of highly efficient and reproducible analytical methods for the investigation of CS sulfation patterns is of high necessity. In this study we report a novel method for straightforward determination of N-acetylgalactosamine (GalNAc) sulfation sites in chondroitin sulfate disaccharides. Our protocol involves combining fully automated chip-based nanoelectrospray (nanoESI) for analyte infusion and ionization in negative ion mode with multistage (MS n ) collision-induced dissociation (CID) high capacity ion trap (HCT) mass spectrometry for generation of sequence ions diagnostic for identification of sulfate ester group position within GalNAc residues. The feasibility of this approach is here demonstrated on chondroitin 6-O-sulfate and chondroitin 4-O-sulfate disaccharides. Fragmentation patterns obtained by MS 2 and MS 3 sequencing stages provided first mass spectrometric data from which sulfation site(s) within GalNAc monosaccharide ring could be unequivocally deciphered. Hence, the method allowed discriminating 4S/6S sulfation sites solely on the basis of MS and multistage MS evidence. Warsaw and Springer-Verlag Berlin Heidelberg. © Versita

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“…The tumor microenvironment has been suggested to be an attractive therapeutic target for treatment of cancer (Hendrix et al, 2003(Hendrix et al, , 2007Wegrowski and Maquart, 2004;Kenny et al, 2007;LaBarge et al, 2007). Chondroitin sulfate as part of the tumor microenvironment accumulates in the stromal compartment of many solid tumors, including breast tumors (Olsen et al, 1988;Kovalszky et al, 1990;Alini and Losa, 1991;Ricciardelli et al, 1997Ricciardelli et al, , 1999Ricciardelli et al, , 2009Vijayagopal et al, 1998;Suwiwat et al, 2004;Pothacharoen et al, 2006;Sakko et al, 2008;Teng et al, 2008;Kalathas et al, 2009), the functional relevance of which had not been analyzed so far.…”

Section: Discussionmentioning

confidence: 99%

“…The tumor microenvironment has been suggested to be an attractive therapeutic target for treatment of cancers, as it is able to control tumor cell phenotype (Hendrix et al, 2003;Wegrowski and Maquart, 2004;Hendrix et al, 2007;Kenny et al, 2007;LaBarge et al, 2007). The glycosaminoglycan (GAG) chondroitin sulfate as part of the cellular microenvironment is comprised of long chains of alternating disaccharide units, attached to a tetrasaccharide linker region which links this GAG to serine residues of core proteins to form chondroitin sulfate-proteoglycans (CSPGs) (Habuchi, 2000;Kusche-Gullberg and Kjellen, 2003;Heinegard, 2009;Klüppel, 2010).…”

Section: Introductionmentioning

confidence: 99%

Elimination of breast tumor-associated chondroitin sulfate promotes metastasis

Prinz¹,

Willis²,

Viloria-Petit³

et al. 2011

Genet. Mol. Res.

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ABSTRACT. Breast cancer is one of the leading causes of cancer-related deaths amongst women in the USA. The tumor microenvironment has been suggested to be an attractive therapeutic target for treatment of cancers. The glycosaminoglycan chondroitin sulfate, as part of the cellular microenvironment, consists of long linear chains of repeating disaccharide units, which are covalently attached to core proteins to form chondroitin sulfate-proteoglycans. In vitro studies have implicated chondroitin sulfate in various aspects of carcinogenesis, whereas the in vivo roles of chondroitin sulfate are less clear. Drastically elevated levels of chondroitin sulfate have been observed within the stromal compartment of many solid tumors, including human breast carcinomas, the significance of which is unknown. We examined the role of tumor-associated chondroitin sulfate in breast cancer progression. Enzymatic elimination of endogenous chondroitin sulfate by intra-tumor injections of chondroitinase ABC leads to the development of secondary tumors and increased lung metastases, while primary orthotopic tumor growth was not affected. These results establish a metastasis-inhibiting effect of primary breast tumor-associated chondroitin sulfate, which may open novel carbohydrate-based therapeutic strategies to combat breast cancer.

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Involvement of stromal proteoglycans in tumour progression

Cited by 63 publications

References 138 publications

Tenascin-C Stimulates Glioma Cell Invasion through Matrix Metalloproteinase-12

Tenascin-C Stimulates Glioma Cell Invasion through Matrix Metalloproteinase-12

Discrimination of GalNAc (4S/6S) sulfation sites in chondroitin sulfate disaccharides by chip-based nanoelectrospray multistage mass spectrometry

Elimination of breast tumor-associated chondroitin sulfate promotes metastasis

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