Source:http://linkedlifedata.com/resource/pubmed/id/17618273
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2007-8-2
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pubmed:abstractText |
Invasive cell migration through tissue barriers requires pericellular remodelling of extracellular matrix (ECM) executed by cell-surface proteases, particularly membrane-type-1 matrix metalloproteinase (MT1-MMP/MMP-14). Using time-resolved multimodal microscopy, we show how invasive HT-1080 fibrosarcoma and MDA-MB-231 breast cancer cells coordinate mechanotransduction and fibrillar collagen remodelling by segregating the anterior force-generating leading edge containing beta1 integrin, MT1-MMP and F-actin from a posterior proteolytic zone executing fibre breakdown. During forward movement, sterically impeding fibres are selectively realigned into microtracks of single-cell calibre. Microtracks become expanded by multiple following cells by means of the large-scale degradation of lateral ECM interfaces, ultimately prompting transition towards collective invasion similar to that in vivo. Both ECM track widening and transition to multicellular invasion are dependent on MT1-MMP-mediated collagenolysis, shown by broad-spectrum protease inhibition and RNA interference. Thus, invasive migration and proteolytic ECM remodelling are interdependent processes that control tissue micropatterning and macropatterning and, consequently, individual and collective cell migration.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD29,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 14,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1465-7392
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
893-904
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pubmed:dateRevised |
2007-12-3
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pubmed:meshHeading |
pubmed-meshheading:17618273-Actins,
pubmed-meshheading:17618273-Animals,
pubmed-meshheading:17618273-Antigens, CD29,
pubmed-meshheading:17618273-Breast Neoplasms,
pubmed-meshheading:17618273-Cell Line, Tumor,
pubmed-meshheading:17618273-Cell Movement,
pubmed-meshheading:17618273-Cell Shape,
pubmed-meshheading:17618273-Collagen,
pubmed-meshheading:17618273-Extracellular Matrix,
pubmed-meshheading:17618273-Female,
pubmed-meshheading:17618273-Fibrosarcoma,
pubmed-meshheading:17618273-Humans,
pubmed-meshheading:17618273-Matrix Metalloproteinase 14,
pubmed-meshheading:17618273-Microscopy,
pubmed-meshheading:17618273-Neoplasm Invasiveness,
pubmed-meshheading:17618273-Protease Inhibitors,
pubmed-meshheading:17618273-RNA, Small Interfering,
pubmed-meshheading:17618273-Recombinant Fusion Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion.
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pubmed:affiliation |
Rudolf Virchow Center, DFG Research Center for Experimental Biomedicine and Department of Dermatology, University of Würzburg, Josef-Schneider-Strasse 2, 97080 Würzburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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