rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1991-10-30
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Concanavalin A,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Gelatinases,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pepsin A,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/progelatinase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-3002
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
1079
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
242-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1911847-Binding Sites,
pubmed-meshheading:1911847-Cell Membrane,
pubmed-meshheading:1911847-Concanavalin A,
pubmed-meshheading:1911847-Cycloheximide,
pubmed-meshheading:1911847-Enzyme Activation,
pubmed-meshheading:1911847-Enzyme Precursors,
pubmed-meshheading:1911847-Fibroblasts,
pubmed-meshheading:1911847-Gelatinases,
pubmed-meshheading:1911847-Hot Temperature,
pubmed-meshheading:1911847-Metalloendopeptidases,
pubmed-meshheading:1911847-Neoplasm Proteins,
pubmed-meshheading:1911847-Pepsin A,
pubmed-meshheading:1911847-Recombinant Proteins,
pubmed-meshheading:1911847-Tissue Inhibitor of Metalloproteinase-2,
pubmed-meshheading:1911847-Trypsin
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pubmed:year |
1991
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pubmed:articleTitle |
Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes.
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pubmed:affiliation |
Cell and Molecular Biology Department, Strangeways Research Laboratory, Cambridge, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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