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Glycosaminoglycans modulate C6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration

BACKGROUND: Adhesion to extracellular matrix (ECM) components has been implicated in the proliferative and invasive properties of tumor cells. We investigated the ability of C6 glioma cells to attach to ECM components in vitro and described the regulatory role of glycosaminoglycans (GAGs) on their a...

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Autores principales: Mendes de Aguiar, Claudia Beatriz Nedel, Lobão-Soares, Bruno, Alvarez-Silva, Marcio, Trentin, Andréa Gonçalves
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1201133/
https://www.ncbi.nlm.nih.gov/pubmed/16111491
http://dx.doi.org/10.1186/1471-2121-6-31
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author Mendes de Aguiar, Claudia Beatriz Nedel
Lobão-Soares, Bruno
Alvarez-Silva, Marcio
Trentin, Andréa Gonçalves
author_facet Mendes de Aguiar, Claudia Beatriz Nedel
Lobão-Soares, Bruno
Alvarez-Silva, Marcio
Trentin, Andréa Gonçalves
author_sort Mendes de Aguiar, Claudia Beatriz Nedel
collection PubMed
description BACKGROUND: Adhesion to extracellular matrix (ECM) components has been implicated in the proliferative and invasive properties of tumor cells. We investigated the ability of C6 glioma cells to attach to ECM components in vitro and described the regulatory role of glycosaminoglycans (GAGs) on their adhesion to the substrate, proliferation and migration. RESULTS: ECM proteins (type IV collagen, laminin and fibronectin) stimulate rat C6 glioma cell line adhesion in vitro, in a dose-dependent manner. The higher adhesion values were achieved with type IV collagen. Exogenous heparin or chondroitin sulfate impaired, in a dose-dependent manner the attachment of C6 glioma cell line to laminin and fibronectin, but not to type IV collagen. Dextran sulfate did not affect C6 adhesion to any ECM protein analyzed, indicating a specific role of GAGs in mediating glioma adhesion to laminin and fibronectin. GAGs and dextran sulfate did not induce C6 glioma detachment from any tested substrate suggesting specific effect in the initial step of cell adhesion. Furthermore, heparin and chondroitin sulfate impaired C6 cells proliferation on fibronectin, but not on type IV collagen or laminin. In contrast, both GAGs stimulate the glioma migration on laminin without effect on type IV collagen or fibronectin. CONCLUSION: The results suggest that GAGs and proteoglycans regulate glioma cell adhesion to ECM proteins in specific manner leading to cell proliferation or cell migration, according to the ECM composition, thus modulating tumor cell properties.
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spelling pubmed-12011332005-09-10 Glycosaminoglycans modulate C6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration Mendes de Aguiar, Claudia Beatriz Nedel Lobão-Soares, Bruno Alvarez-Silva, Marcio Trentin, Andréa Gonçalves BMC Cell Biol Research Article BACKGROUND: Adhesion to extracellular matrix (ECM) components has been implicated in the proliferative and invasive properties of tumor cells. We investigated the ability of C6 glioma cells to attach to ECM components in vitro and described the regulatory role of glycosaminoglycans (GAGs) on their adhesion to the substrate, proliferation and migration. RESULTS: ECM proteins (type IV collagen, laminin and fibronectin) stimulate rat C6 glioma cell line adhesion in vitro, in a dose-dependent manner. The higher adhesion values were achieved with type IV collagen. Exogenous heparin or chondroitin sulfate impaired, in a dose-dependent manner the attachment of C6 glioma cell line to laminin and fibronectin, but not to type IV collagen. Dextran sulfate did not affect C6 adhesion to any ECM protein analyzed, indicating a specific role of GAGs in mediating glioma adhesion to laminin and fibronectin. GAGs and dextran sulfate did not induce C6 glioma detachment from any tested substrate suggesting specific effect in the initial step of cell adhesion. Furthermore, heparin and chondroitin sulfate impaired C6 cells proliferation on fibronectin, but not on type IV collagen or laminin. In contrast, both GAGs stimulate the glioma migration on laminin without effect on type IV collagen or fibronectin. CONCLUSION: The results suggest that GAGs and proteoglycans regulate glioma cell adhesion to ECM proteins in specific manner leading to cell proliferation or cell migration, according to the ECM composition, thus modulating tumor cell properties. BioMed Central 2005-08-19 /pmc/articles/PMC1201133/ /pubmed/16111491 http://dx.doi.org/10.1186/1471-2121-6-31 Text en Copyright © 2005 de Aguiar et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Mendes de Aguiar, Claudia Beatriz Nedel
Lobão-Soares, Bruno
Alvarez-Silva, Marcio
Trentin, Andréa Gonçalves
Glycosaminoglycans modulate C6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration
title Glycosaminoglycans modulate C6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration
title_full Glycosaminoglycans modulate C6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration
title_fullStr Glycosaminoglycans modulate C6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration
title_full_unstemmed Glycosaminoglycans modulate C6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration
title_short Glycosaminoglycans modulate C6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration
title_sort glycosaminoglycans modulate c6 glioma cell adhesion to extracellular matrix components and alter cell proliferation and cell migration
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1201133/
https://www.ncbi.nlm.nih.gov/pubmed/16111491
http://dx.doi.org/10.1186/1471-2121-6-31
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