Source:http://linkedlifedata.com/resource/pubmed/id/19136391
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2009-5-27
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pubmed:abstractText |
Membrane type-1 matrix metalloproteinase (MT1-MMP) is a multidomain transmembrane endopeptidase with a major role in physiological and pathological processes through proteolysis of extracellular matrix and other pericellular proteins. We examined cell surface function of MT1-MMP in PC-3 human prostate tumor cells selected for metastasis in nude mice (PC-3-LN4), or transfected with the full-length wild-type (WT) MT1-MMP or with the mutant form lacking the cytoplasmic tail (Delta C-MT1-MMP). Enhanced cell surface MT1-MMP was determined by fluorescence-activated cell sorting analysis and evidenced mechanistically by increased activation of proMMP-2 and invasion into type-I collagen gels. PC-3 cells overexpressing MT1-MMP grew faster than mock-transfected control cells subcutaneously in nude mice. MT1-MMP localized in caveolae, as judged by immunofluorescence microscopy and sucrose-gradient, detergent-resistant cell fractionation. Delta C-MT1-MMP was strongly associated with caveolae, whereas the WT form was present in both caveolae and noncaveolae fractions. The role of plasma membrane MT1-MMP was supported by localization of MT1-MMP by immunofluorescence microscopy at the cell surface of tumor cells in primary prostate cancers. Increased plasma membrane localization of MT1-MMP, either in caveolae or in other lipid raft structures, is a mechanism to localize this proteinase in contact with extracellular matrix and other pericellular proteins, the cleavage of which can facilitate prostate cancer cell invasion and metastasis.
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pubmed:grant | |
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:issn |
1939-4640
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
259-74
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pubmed:meshHeading |
pubmed-meshheading:19136391-Animals,
pubmed-meshheading:19136391-Blotting, Western,
pubmed-meshheading:19136391-Caveolae,
pubmed-meshheading:19136391-Cell Line, Tumor,
pubmed-meshheading:19136391-Flow Cytometry,
pubmed-meshheading:19136391-Fluorescent Antibody Technique,
pubmed-meshheading:19136391-Humans,
pubmed-meshheading:19136391-Immunoprecipitation,
pubmed-meshheading:19136391-Male,
pubmed-meshheading:19136391-Matrix Metalloproteinase 14,
pubmed-meshheading:19136391-Mice,
pubmed-meshheading:19136391-Mice, Nude,
pubmed-meshheading:19136391-Microscopy, Confocal,
pubmed-meshheading:19136391-Neoplasm Invasiveness,
pubmed-meshheading:19136391-Prostatic Neoplasms,
pubmed-meshheading:19136391-Transfection
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pubmed:articleTitle |
Increased aggressiveness of human prostate PC-3 tumor cells expressing cell surface localized membrane type-1 matrix metalloproteinase (MT1-MMP).
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pubmed:affiliation |
Department of Pharmacology, University of Minnesota, Minneapolis, Minnesota, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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