| pubmed-article:14583471 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14583471 | lifeskim:mentions | umls-concept:C0003995 | lld:lifeskim |
| pubmed-article:14583471 | lifeskim:mentions | umls-concept:C0623362 | lld:lifeskim |
| pubmed-article:14583471 | lifeskim:mentions | umls-concept:C0912013 | lld:lifeskim |
| pubmed-article:14583471 | lifeskim:mentions | umls-concept:C1422507 | lld:lifeskim |
| pubmed-article:14583471 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:14583471 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:14583471 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:14583471 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:14583471 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:14583471 | pubmed:dateCreated | 2003-10-29 | lld:pubmed |
| pubmed-article:14583471 | pubmed:abstractText | Leukolysin/membrane-type 6 matrix metalloproteinase (leukolysin/MT6-MMP), a glycosylphosphatidylinositol-anchored neutrophil matrix metalloproteinase, is also abnormally expressed in brain cancer tissues. Yet, little is known about its role in cancer progression. Here we show that MT6-MMP is capable of activating proMMP-2, an enzyme implicated in tumor invasion and metastasis. Although MT6-MMP is only 10% as active as MT5-MMP in mediating proMMP-2 activation, it generates a higher ratio of mature/intermediate forms of MMP-2 than MT5-MMP. Consistently, purified CAT of MT6-MMP converts proMMP-2 into mostly the mature form. Using the catalytically inactive mutant MMP-2EA (the E404A mutant of proMMP-2), which cannot autocatalytically mature from the intermediate form into the mature one, we show that MT6-MMP cleaves not only the known MT-MMP-processing site at Asn(66)-Leu but also the previously unsuspected Asn(109)-Tyr to yield a fully mature molecule. Despite their difference in mediating proMMP-2 activation in transfected cells, the CAT of MT6-MMP appears to be as efficient as that of MT5-MMP in cleaving proMMP-2EA in buffer, suggesting that its CAT is a strong proMMP-2 activator. Indeed, the CAT of MT6-MMP can partially substitute the CAT of prototypical MT1-MMP in mediating proMMP-2 activation. Taken these facts together, we conclude that MT6-MMP may participate in tumor invasion and metastasis by directly converting proMMP-2 into active form. | lld:pubmed |
| pubmed-article:14583471 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14583471 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14583471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14583471 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14583471 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14583471 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:14583471 | pubmed:issn | 0008-5472 | lld:pubmed |
| pubmed-article:14583471 | pubmed:author | pubmed-author:PeiDuanqingD | lld:pubmed |
| pubmed-article:14583471 | pubmed:author | pubmed-author:NieJingJ | lld:pubmed |
| pubmed-article:14583471 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14583471 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:14583471 | pubmed:volume | 63 | lld:pubmed |
| pubmed-article:14583471 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14583471 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14583471 | pubmed:pagination | 6758-62 | lld:pubmed |
| pubmed-article:14583471 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:14583471 | pubmed:meshHeading | pubmed-meshheading:14583471... | lld:pubmed |
| pubmed-article:14583471 | pubmed:meshHeading | pubmed-meshheading:14583471... | lld:pubmed |
| pubmed-article:14583471 | pubmed:meshHeading | pubmed-meshheading:14583471... | lld:pubmed |
| pubmed-article:14583471 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14583471 | pubmed:articleTitle | Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond. | lld:pubmed |
| pubmed-article:14583471 | pubmed:affiliation | Department of Pharmacology, University of Minnesota, Minneapolis, Minnesota 55455, USA. | lld:pubmed |
| pubmed-article:14583471 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14583471 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14583471 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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