| pubmed-article:10652225 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10652225 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10652225 | lifeskim:mentions | umls-concept:C0014833 | lld:lifeskim |
| pubmed-article:10652225 | lifeskim:mentions | umls-concept:C0025543 | lld:lifeskim |
| pubmed-article:10652225 | lifeskim:mentions | umls-concept:C0036734 | lld:lifeskim |
| pubmed-article:10652225 | lifeskim:mentions | umls-concept:C2717971 | lld:lifeskim |
| pubmed-article:10652225 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10652225 | lifeskim:mentions | umls-concept:C0246551 | lld:lifeskim |
| pubmed-article:10652225 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10652225 | pubmed:dateCreated | 2000-3-1 | lld:pubmed |
| pubmed-article:10652225 | pubmed:abstractText | Treatment of human uterine cervical fibroblasts with commercial lipopolysaccharide (LPS) preparations from different serotypes of Escherichia coli effectively augmented the processing of mammalian progelatinase A/promatrix metalloproteinase (proMMP)-2 to a 62-kDa form of MMP-2. When purified proMMP-2 was incubated with LPS preparations, the proenzyme was similarly processed into the 62-kDa active MMP-2 in a time- and dose-dependent manner. By contrast, progelatinase B/proMMP-9 and prostromelysin 1/proMMP-3 were not activated. A serine proteinase inhibitor, phenylmethylsulfonyl fluoride, completely interfered with this LPS-mediated activation of proMMP-2. This is novel evidence that E. coli serine proteinase is a specific activator of proMMP-2. Thus, it is very likely that E. coli infection plays a crucial role in the degradation of connective tissues via the activation of proMMP-2, and the resultant active MMP-2 participates in the dysfunction of connective tissues such as in the preterm rupture of fetal membranes. | lld:pubmed |
| pubmed-article:10652225 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10652225 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10652225 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10652225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10652225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10652225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10652225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10652225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10652225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10652225 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10652225 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10652225 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:10652225 | pubmed:author | pubmed-author:SatoTT | lld:pubmed |
| pubmed-article:10652225 | pubmed:author | pubmed-author:ItoAA | lld:pubmed |
| pubmed-article:10652225 | pubmed:author | pubmed-author:TakedaMM | lld:pubmed |
| pubmed-article:10652225 | pubmed:author | pubmed-author:ImadaKK | lld:pubmed |
| pubmed-article:10652225 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
| pubmed-article:10652225 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10652225 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:10652225 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:10652225 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10652225 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10652225 | pubmed:pagination | 128-32 | lld:pubmed |
| pubmed-article:10652225 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
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| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
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| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
| pubmed-article:10652225 | pubmed:meshHeading | pubmed-meshheading:10652225... | lld:pubmed |
| pubmed-article:10652225 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10652225 | pubmed:articleTitle | Activation of human progelatinase A/promatrix metalloproteinase 2 by Escherichia coli-derived serine proteinase. | lld:pubmed |
| pubmed-article:10652225 | pubmed:affiliation | Department of Pharmacy, Tsukuba University Hospital, Amakubo, Tsukuba, Ibaraki, 305-8756, Japan. | lld:pubmed |
| pubmed-article:10652225 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10652225 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10652225 | lld:pubmed |
