Linked Life Data

10652225

Source:http://linkedlifedata.com/resource/pubmed/id/10652225

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-3-1
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
128-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Activation of human progelatinase A/promatrix metalloproteinase 2 by Escherichia coli-derived serine proteinase.
pubmed:affiliation
Department of Pharmacy, Tsukuba University Hospital, Amakubo, Tsukuba, Ibaraki, 305-8756, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't