Source:http://linkedlifedata.com/resource/pubmed/id/19956866
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-12-3
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pubmed:abstractText |
MMP-26 is a novel member of the MMP family and is widely expressed in cancer cells of epithelial origin. Published research shows that MMP-26 contributes to tumor development and to the restoration of tissue injury. In this study, in order to identify the functions of MMP-26 that contribute to the biological phenotype and behavior of non-epithelial human glioma U251 cells, we established an MMP-26 overexpressing tumor cell model using gene transfection. We then used these cells to investigate the role of MMP-26 in tumor progression. Adherence and spreading assay, wound healing assay, Boyden chamber invasion assay, and in vivo tumorigenicity assay were performed to analyze the invasion ability of MMP-26 transfected U251 cells. Microvessel density analysis and tumor cell induced angiogenesis assay were employed to detect the function of MMP-26 in angiogenesis. Results showed that the spreading cell ratio of MMP-26 transfected cells was significantly higher than parental U251 cells. The relative migration distance of MMP-26 transfected cells on Matrigel was significantly higher than that of parental U251 cells. The Boyden chamber assay showed that MMP-26 could significantly enhance the ability of U251 cells to invade through Matrigel. MMP-26 could also enhance the local invasion ability of U251 cells in vivo. There was a significant increase of the microvessel density of tumor tissue derived from MMP-26 transfected U251 cells. The vessel numbe induced by MMP-26 transfected U251 cells in nude mice was also significantly higher than that induced by parental U251 cells. In conclusion, we successfully established an MMP-26 overexpressing cell model and confirmed that MMP-26 contributed to U251 cell invasion and migration in vitro. We also demonstrated that MMP-26 plays an important role in local invasion, and angiogenesis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Drug Combinations,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/MMP26 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases, Secreted,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/matrigel
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1791-2431
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
69-78
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pubmed:meshHeading |
pubmed-meshheading:19956866-Animals,
pubmed-meshheading:19956866-Brain Neoplasms,
pubmed-meshheading:19956866-Cell Line, Tumor,
pubmed-meshheading:19956866-Collagen,
pubmed-meshheading:19956866-Drug Combinations,
pubmed-meshheading:19956866-Female,
pubmed-meshheading:19956866-Fibronectins,
pubmed-meshheading:19956866-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:19956866-Glioma,
pubmed-meshheading:19956866-Humans,
pubmed-meshheading:19956866-Laminin,
pubmed-meshheading:19956866-Matrix Metalloproteinases, Secreted,
pubmed-meshheading:19956866-Mice,
pubmed-meshheading:19956866-Mice, Nude,
pubmed-meshheading:19956866-Neoplasm Invasiveness,
pubmed-meshheading:19956866-Neoplasm Transplantation,
pubmed-meshheading:19956866-Proteoglycans,
pubmed-meshheading:19956866-Wound Healing
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pubmed:year |
2010
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pubmed:articleTitle |
Expression of Matrix Metalloproteinase-26 promotes human glioma U251 cell invasion in vitro and in vivo.
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pubmed:affiliation |
The Key Laboratory of Pathobiology, Ministry of Education, Norman Bethune College of Medicine, Jilin University, Changchun, P.R. China.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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