pubmed-article:10998420 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C0145988 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C0623362 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C1551336 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:10998420 | lifeskim:mentions | umls-concept:C0526871 | lld:lifeskim |
pubmed-article:10998420 | pubmed:issue | 52 | lld:pubmed |
pubmed-article:10998420 | pubmed:dateCreated | 2001-1-25 | lld:pubmed |
pubmed-article:10998420 | pubmed:abstractText | The membrane-type 1 matrix metalloproteinase (MT1-MMP) has been shown to be a key enzyme in tumor angiogenesis and metastasis. MT1-MMP hydrolyzes a variety of extracellular matrix components and is a physiological activator of pro-MMP-2, another MMP involved in malignancy. Pro-MMP-2 activation by MT1-MMP involves the formation of an MT1-MMP.tissue inhibitors of metalloproteinases 2 (TIMP-2). pro-MMP-2 complex on the cell surface that promotes the hydrolysis of pro-MMP-2 by a neighboring TIMP-2-free MT1-MMP. The MT1-MMP. TIMP-2 complex also serves to reduce the intermolecular autocatalytic turnover of MT1-MMP, resulting in accumulation of active MT1-MMP (57 kDa) on the cell surface. Evidence shown here in Timp2-null cells demonstrates that pro-MMP-2 activation by MT1-MMP requires TIMP-2. In contrast, a C-terminally deleted TIMP-2 (Delta-TIMP-2), unable to form ternary complex, had no effect. However, Delta-TIMP-2 and certain synthetic MMP inhibitors, which inhibit MT1-MMP autocatalysis, can act synergistically with TIMP-2 in the promotion of pro-MMP-2 activation by MT1-MMP. In contrast, TIMP-4, an efficient MT1-MMP inhibitor, had no synergistic effect. These studies suggest that under certain conditions the pericellular activity of MT1-MMP in the presence of TIMP-2 can be modulated by synthetic and natural (TIMP-4) MMP inhibitors. | lld:pubmed |
pubmed-article:10998420 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998420 | pubmed:language | eng | lld:pubmed |
pubmed-article:10998420 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998420 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10998420 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10998420 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998420 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998420 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998420 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998420 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998420 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10998420 | pubmed:month | Dec | lld:pubmed |
pubmed-article:10998420 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:TschescheHH | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:BrownSS | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:FridmanRR | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:TothMM | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:WangZZ | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:DeClerckY AYA | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:MobasherySS | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:OverallC MCM | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:SolowayP DPD | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:BernardoM MMM | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:CheeM AMA | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:BiggH FHF | lld:pubmed |
pubmed-article:10998420 | pubmed:author | pubmed-author:GervasiD CDC | lld:pubmed |
pubmed-article:10998420 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10998420 | pubmed:day | 29 | lld:pubmed |
pubmed-article:10998420 | pubmed:volume | 275 | lld:pubmed |
pubmed-article:10998420 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10998420 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10998420 | pubmed:pagination | 41415-23 | lld:pubmed |
pubmed-article:10998420 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:10998420 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10998420 | pubmed:articleTitle | Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2. | lld:pubmed |
pubmed-article:10998420 | pubmed:affiliation | Departments of Pathology, Urology and Chemistry, Wayne State University, Detroit, Michigan 48201, USA. | lld:pubmed |
pubmed-article:10998420 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10998420 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10998420 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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