Source:http://linkedlifedata.com/resource/pubmed/id/10502306
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-11-22
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pubmed:abstractText |
Matrix metalloproteinases are proteolytic enzymes which play a major role in resorption of collagen and other components of the extracellular matrix. They are controlled by specific inhibitors, so-called tissue inhibitors of metalloproteinases (TIMPs). The balance between matrix metalloproteinases and TIMPs seems to play a major role in controlling extracellular matrix homeostasis and cell migration. The influence of TIMP-1 on migration behaviour was explored in human hepatoma cells transiently and stably transfected with mouse TIMP-1, and incubated with biologically active TIMP-1. Transfection and biosynthesis were verified by Northern blotting, Western blotting, metabolic labeling, and reverse zymography. Overexpression of and incubation with TIMP-1 resulted in suppressed migration and seemed to enhance cell-cell contact. Using gelatin zymography and Western blotting we measured a significant increase of matrix metalloproteinases-2 and matrix metalloproteinases-9 in cells transfected with TIMP-1. This new phenomenon may be of important physiological significance in modulating TIMP and MMP expression. Our results indicate a functional involvement of TIMP-1 in matrix homeostasis and some automatic control in matrix turnover.
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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/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Gelatinases,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 9,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0730-2312
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
346-55
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10502306-Animals,
pubmed-meshheading:10502306-Blotting, Northern,
pubmed-meshheading:10502306-Blotting, Western,
pubmed-meshheading:10502306-Carcinoma, Hepatocellular,
pubmed-meshheading:10502306-Cell Movement,
pubmed-meshheading:10502306-DNA, Complementary,
pubmed-meshheading:10502306-Extracellular Matrix,
pubmed-meshheading:10502306-Gelatinases,
pubmed-meshheading:10502306-Homeostasis,
pubmed-meshheading:10502306-Humans,
pubmed-meshheading:10502306-Matrix Metalloproteinase 2,
pubmed-meshheading:10502306-Matrix Metalloproteinase 9,
pubmed-meshheading:10502306-Mice,
pubmed-meshheading:10502306-RNA,
pubmed-meshheading:10502306-Tissue Inhibitor of Metalloproteinase-1,
pubmed-meshheading:10502306-Transfection,
pubmed-meshheading:10502306-Tumor Cells, Cultured
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pubmed:year |
1999
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pubmed:articleTitle |
Increased TIMP-1 activity results in increased expression of gelatinases and altered cell motility.
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pubmed:affiliation |
Medizinische Klinik III, 52057 Aachen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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