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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1997-7-21
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pubmed:abstractText |
Tumor invasion into extracellular matrix (ECM) and basement membrane (BM) is a crucial step in the complex multistage process that leads to metastasis formation. GG6-10 galloylglucose, isolated from Galla Rhois, inhibited the invasion of metastatic HT-1080 cells into a reconstituted BM, such as a Matrigel/fibronectin (FN)-coated filter, in a concentration-dependent fashion. GG6-10 affected neither the tumor cell adhesion and haptotactic migration to ECM components (Matrigel and FN), nor the growth of HT-1080 cells. The gelatin zymography revealed that GG6-10 was able to inhibit not only the degradation of gelatin mediated by matrix metalloproteinases (MMP)-2 and -9 in conditioned medium of HT-1080 tumor cells but also the production of MMP from the tumor cells in a concentration-dependent manner. MMP production is well known to be positively regulated by various cytokines, such as tumor necrosis factor-alpha (TNF-alpha). Thus, we examined the effect of GG6-10 on the TNF-alpha-mediated translation of the MMP-9 gene using HT-1080 cells transfected with the MMP-9 promoter linked to the luciferase gene as a reporter. Similarly to prednisolone, GG6-10 was found to inhibit the TNF-alpha-inducible promoter activity. In keeping with these results, GG6-10 might inhibit tumor cell invasion by inhibiting the gelatinolysis mediated by MMP-2 and -9 and interfering with the production of MMP via inhibiting transcription of the promoter for MMP.
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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/Collagenases,
http://linkedlifedata.com/resource/pubmed/chemical/Gelatinases,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrolyzable Tannins,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Tannins,
http://linkedlifedata.com/resource/pubmed/chemical/glucogallin
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pubmed:status |
MEDLINE
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pubmed:issn |
0965-0407
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
503-11
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9160354-Cell Adhesion,
pubmed-meshheading:9160354-Cell Movement,
pubmed-meshheading:9160354-Collagen,
pubmed-meshheading:9160354-Collagenases,
pubmed-meshheading:9160354-Extracellular Matrix,
pubmed-meshheading:9160354-Gelatinases,
pubmed-meshheading:9160354-Humans,
pubmed-meshheading:9160354-Hydrolyzable Tannins,
pubmed-meshheading:9160354-Matrix Metalloproteinase 9,
pubmed-meshheading:9160354-Neoplasm Invasiveness,
pubmed-meshheading:9160354-Tannins,
pubmed-meshheading:9160354-Tumor Cells, Cultured
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pubmed:year |
1996
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pubmed:articleTitle |
Inhibition by galloylglucose (GG6-10) of tumor invasion through extracellular matrix and gelatinase-mediated degradation of type IV collagens by metastatic tumor cells.
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pubmed:affiliation |
Department of Pathogenic Biochemistry, Toyama Medical and Pharmaceutical University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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