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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5323
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pubmed:dateCreated |
1997-7-30
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pubmed:abstractText |
Structural changes in the extracellular matrix are necessary for cell migration during tissue remodeling and tumor invasion. Specific cleavage of laminin-5 (Ln-5) by matrix metalloprotease-2 (MMP2) was shown to induce migration of breast epithelial cells. MMP2 cleaved the Ln-5 gamma2 subunit at residue 587, exposing a putative cryptic promigratory site on Ln-5 that triggers cell motility. This altered form of Ln-5 is found in tumors and in tissues undergoing remodeling, but not in quiescent tissues. Cleavage of Ln-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Collagenases,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinolysin,
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/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thiophenes,
http://linkedlifedata.com/resource/pubmed/chemical/batimastat,
http://linkedlifedata.com/resource/pubmed/chemical/kalinin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
225-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9211848-Animals,
pubmed-meshheading:9211848-Breast,
pubmed-meshheading:9211848-Cell Adhesion,
pubmed-meshheading:9211848-Cell Adhesion Molecules,
pubmed-meshheading:9211848-Cell Division,
pubmed-meshheading:9211848-Cell Line,
pubmed-meshheading:9211848-Cell Movement,
pubmed-meshheading:9211848-Cell Size,
pubmed-meshheading:9211848-Collagenases,
pubmed-meshheading:9211848-Epithelial Cells,
pubmed-meshheading:9211848-Epithelium,
pubmed-meshheading:9211848-Extracellular Matrix,
pubmed-meshheading:9211848-Female,
pubmed-meshheading:9211848-Fibrinolysin,
pubmed-meshheading:9211848-Gelatinases,
pubmed-meshheading:9211848-Humans,
pubmed-meshheading:9211848-Matrix Metalloproteinase 2,
pubmed-meshheading:9211848-Matrix Metalloproteinase 9,
pubmed-meshheading:9211848-Metalloendopeptidases,
pubmed-meshheading:9211848-Mice,
pubmed-meshheading:9211848-Phenylalanine,
pubmed-meshheading:9211848-Protease Inhibitors,
pubmed-meshheading:9211848-Rats,
pubmed-meshheading:9211848-Recombinant Fusion Proteins,
pubmed-meshheading:9211848-Skin Neoplasms,
pubmed-meshheading:9211848-Thiophenes
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pubmed:year |
1997
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pubmed:articleTitle |
Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5.
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pubmed:affiliation |
Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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