Source:http://linkedlifedata.com/resource/pubmed/id/16251193
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
51
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pubmed:dateCreated |
2005-12-19
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pubmed:abstractText |
Membrane type-1 matrix metalloproteinase (MT1-MMP) exhibits distinctive and important pericellular cleavage functions. Recently, we determined that MT1-MMP was trafficked to the centrosomes in the course of endocytosis. Our data suggested that the functionally important, integral, centrosomal protein, pericentrin-2, was a cleavage target of MT1-MMP in human and in canine cells and that the sequence of the cleavage sites were ALRRLLG1156 downward arrow L1157FG and ALRRLLS2068 downward arrow L2069FG, respectively. The presence of Asp-948 at the P1 position inactivated the corresponding site (ALRRLLD948-L949FGD) in murine pericentrin. To confirm that MT1-MMP itself cleaves pericentrin directly, rather than indirectly, we analyzed the cleavage of the peptides that span the MT1-MMP cleavage site. In addition, we analyzed glioma U251 cells, which co-expressed MT1-MMP with the wild type murine pericentrin and the D948G mutant. We determined that the D948G mutant that exhibited the cleavage sequence of human pericentrin was sensitive to MT1-MMP, whereas unmodified murine pericentrin was resistant to proteolysis. Taken together, our results confirm that MT1-MMP cleaves pericentrin-2 in humans but not in mice and that mouse models of cancer probably cannot be used to critically examine MT1-MMP functionality.
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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/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 14,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases...,
http://linkedlifedata.com/resource/pubmed/chemical/Mmp14 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/pericentrin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
42237-41
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16251193-Animals,
pubmed-meshheading:16251193-Antigens,
pubmed-meshheading:16251193-Base Sequence,
pubmed-meshheading:16251193-Cell Line, Tumor,
pubmed-meshheading:16251193-Cell Transformation, Neoplastic,
pubmed-meshheading:16251193-Centrosome,
pubmed-meshheading:16251193-DNA Primers,
pubmed-meshheading:16251193-Humans,
pubmed-meshheading:16251193-Hydrolysis,
pubmed-meshheading:16251193-Matrix Metalloproteinase 14,
pubmed-meshheading:16251193-Matrix Metalloproteinases,
pubmed-meshheading:16251193-Matrix Metalloproteinases, Membrane-Associated,
pubmed-meshheading:16251193-Mice
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pubmed:year |
2005
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pubmed:articleTitle |
Centrosomal pericentrin is a direct cleavage target of membrane type-1 matrix metalloproteinase in humans but not in mice: potential implications for tumorigenesis.
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pubmed:affiliation |
Cancer Research Center, The Burnham Institute for Medical Research, La Jolla, California 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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