| pubmed-article:1911847 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1911847 | lifeskim:mentions | umls-concept:C0040300 | lld:lifeskim |
| pubmed-article:1911847 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:1911847 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:1911847 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:1911847 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1911847 | lifeskim:mentions | umls-concept:C0138526 | lld:lifeskim |
| pubmed-article:1911847 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1911847 | pubmed:dateCreated | 1991-10-30 | lld:pubmed |
| pubmed-article:1911847 | pubmed:abstractText | We report that monolayers of human fibroblasts stimulated with concanavalin A were able to activate 72 kDa progelatinase but not 95 kDa progelatinase. The activating capacity of fibroblasts appeared approx. 6 h after concanavalin A stimulation and was blocked by cycloheximide. The activation of 72 kDa progelatinase was readily inhibited by TIMP-2 but only poorly by TIMP-1. Plasma membranes isolated from the fibroblasts were capable of activating 72 kDa progelatinase. The cleavage products of the plasma membrane-mediated activation of 72 kDa progelatinase corresponded to those of organomercurial-induced self-cleavage. Only inhibitors of metalloproteinase self-cleavage inhibited the activating capacity of plasma membrane preparations, although the activating capacity was destroyed by trypsin and heat. As with the fibroblast monolayers, TIMP-2 was a potent inhibitor of the membrane-mediated activation whereas TIMP-1 was less so. | lld:pubmed |
| pubmed-article:1911847 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1911847 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1911847 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1911847 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1911847 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1911847 | pubmed:author | pubmed-author:ReynoldsJ JJJ | lld:pubmed |
| pubmed-article:1911847 | pubmed:author | pubmed-author:MurphyGG | lld:pubmed |
| pubmed-article:1911847 | pubmed:author | pubmed-author:WardR VRV | lld:pubmed |
| pubmed-article:1911847 | pubmed:author | pubmed-author:SlocombeP MPM | lld:pubmed |
| pubmed-article:1911847 | pubmed:author | pubmed-author:DochertyA JAJ | lld:pubmed |
| pubmed-article:1911847 | pubmed:author | pubmed-author:AtkinsonS JSJ | lld:pubmed |
| pubmed-article:1911847 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1911847 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:1911847 | pubmed:volume | 1079 | lld:pubmed |
| pubmed-article:1911847 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1911847 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1911847 | pubmed:pagination | 242-6 | lld:pubmed |
| pubmed-article:1911847 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:1911847 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1911847 | pubmed:articleTitle | Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes. | lld:pubmed |
| pubmed-article:1911847 | pubmed:affiliation | Cell and Molecular Biology Department, Strangeways Research Laboratory, Cambridge, U.K. | lld:pubmed |
| pubmed-article:1911847 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1911847 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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