Source:http://linkedlifedata.com/resource/pubmed/id/15561768
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0023779,
umls-concept:C0025543,
umls-concept:C0178719,
umls-concept:C0331858,
umls-concept:C0332307,
umls-concept:C0596901,
umls-concept:C1514562,
umls-concept:C1704640,
umls-concept:C1706515,
umls-concept:C1709694,
umls-concept:C1879547,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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| pubmed:issue |
Pt 26
|
| pubmed:dateCreated |
2004-12-13
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| pubmed:abstractText |
The integral membrane type 1 matrix metalloprotease (MT1-MMP) is a pivotal protease in a number of physiological and pathological processes and confers both non-tumorigenic and tumorigenic cell lines with a specific growth advantage in a three-dimensional matrix. Here we show that, in a melanoma cell line, the majority (80%) of MT1-MMP is sorted to detergent-resistant membrane fractions; however, it is only the detergent-soluble fraction (20%) of MT1-MMP that undergoes intracellular processing to the mature form. Also, this processed MT1-MMP is the sole form responsible for ECM degradation in vitro. Finally, furin-dependent processing of MT1-MMP is shown to occur intracellularly after exit from the Golgi apparatus and prior to its arrival at the plasma membrane. It is thus proposed that the association of MT1-MMP with different membrane subdomains might be crucial in the control of its different activities: for instance in cell migration and invasion and other less defined ones such as MT1-MMP-dependent signaling pathways.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
|
| pubmed:issn |
0021-9533
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
117
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
6275-87
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15561768-Biotinylation,
pubmed-meshheading:15561768-Cell Compartmentation,
pubmed-meshheading:15561768-Cell Line, Tumor,
pubmed-meshheading:15561768-Cell Movement,
pubmed-meshheading:15561768-Enzyme Activation,
pubmed-meshheading:15561768-Extracellular Matrix,
pubmed-meshheading:15561768-Fluorescent Antibody Technique,
pubmed-meshheading:15561768-Furin,
pubmed-meshheading:15561768-Green Fluorescent Proteins,
pubmed-meshheading:15561768-Humans,
pubmed-meshheading:15561768-Immunohistochemistry,
pubmed-meshheading:15561768-Matrix Metalloproteinases, Membrane-Associated,
pubmed-meshheading:15561768-Melanoma,
pubmed-meshheading:15561768-Metalloendopeptidases,
pubmed-meshheading:15561768-Protein Processing, Post-Translational,
pubmed-meshheading:15561768-Protein Structure, Tertiary,
pubmed-meshheading:15561768-Protein Transport
|
| pubmed:year |
2004
|
| pubmed:articleTitle |
Intracellular processing and activation of membrane type 1 matrix metalloprotease depends on its partitioning into lipid domains.
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| pubmed:affiliation |
Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, S. Maria Imbaro, 66030, Chieti, Italy.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|