Linked Life Data

9165065

Source:http://linkedlifedata.com/resource/pubmed/id/9165065

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1997-8-15
pubmed:abstractText
Matrix metalloproteinases (MMPs), also called matrixins, function in the turnover of extracellular matrix components. These enzymes are considered to play important roles in embryo development, morphogenesis and tissue remodeling, and in diseases such as arthritis, periodontitis, glomerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis. All MMPs are synthesized as preproenzymes and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is one of the critical steps that leads to extracellular matrix breakdown. This review describes recent progress made to elucidate the activation mechanisms of pro-matrixins which include extracellular stepwise activation common to most proMMPs, cell surface activation of progelatinase A and procollagenase 3, and intracellular activation of prostromelysin 3 and pro-membrane-type-1 MMP.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
378
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
151-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Activation mechanisms of matrix metalloproteinases.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City 66160, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review