Source:http://linkedlifedata.com/resource/pubmed/id/15713888
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-2-16
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pubmed:abstractText |
Apolipoprotein E (apoE) in a human fetal brain cDNA library was identified, using the expression cloning method, as a gene product that formed a complex with latent matrix metalloproteinase (MMP)-2. Co-expression of membrane-type MMP-1 (MT1-MMP) with apoE in HEK293T cells reduced the amount of apoE secreted into the culture medium, whereas cell-associated apoE core protein was not affected. Incubation of native apoE protein with recombinant MT1-MMP resulted in the cleavage of apoE. Recombinant apoE protein fused to glutathione S-transferase (apoE-GST) was cleaved by MT1-MMP at the following peptide bonds; T(85)-M(86), K(93)-S(94), R(246)-L(247), A(255)-E(256) and G(296)-L(297). HT1080 cells transfected with the apoE gene, which express endogenous MT1-MMP, secreted a low level of apoE protein and its cleaved fragments, and treatment with MMP inhibitor BB94 induced accumulation of apoE and retardation of cell proliferation. Addition of apoE-GST protein to the culture of HEK293T cells suppressed cell proliferation, and stable transfection of the MT1-MMP gene partly abrogated the suppression. These results suggest that cleavage of apoE protein by MT1-MMP abrogates apoE-mediated suppression of cell proliferation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases...,
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/Thiophenes,
http://linkedlifedata.com/resource/pubmed/chemical/batimastat
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
137
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
95-9
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:15713888-Apolipoproteins E,
pubmed-meshheading:15713888-Cell Line,
pubmed-meshheading:15713888-Cell Proliferation,
pubmed-meshheading:15713888-Gene Expression,
pubmed-meshheading:15713888-Humans,
pubmed-meshheading:15713888-Matrix Metalloproteinases, Membrane-Associated,
pubmed-meshheading:15713888-Metalloendopeptidases,
pubmed-meshheading:15713888-Phenylalanine,
pubmed-meshheading:15713888-Protease Inhibitors,
pubmed-meshheading:15713888-Thiophenes
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pubmed:year |
2005
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pubmed:articleTitle |
Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation.
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pubmed:affiliation |
Department of Molecular Virology and Oncology, Cancer Research Institute, Kanazawa University, 13-1 Takara-machi, Kanazawa 920-0934, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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