| pubmed-article:2544876 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2544876 | lifeskim:mentions | umls-concept:C0042071 | lld:lifeskim |
| pubmed-article:2544876 | lifeskim:mentions | umls-concept:C0032145 | lld:lifeskim |
| pubmed-article:2544876 | lifeskim:mentions | umls-concept:C0814423 | lld:lifeskim |
| pubmed-article:2544876 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:2544876 | pubmed:dateCreated | 1989-8-10 | lld:pubmed |
| pubmed-article:2544876 | pubmed:abstractText | Urokinase plasminogen activator (uPA) interacts with a surface receptor and with specific inhibitors, such as plasminogen activator inhibitor type 1 (PAI-1). These interactions are mediated by two functionally independent domains of the molecule: the catalytic domain (at the carboxyl terminus) and the growth factor domain (at the amino terminus). We have now investigated whether PAI-1 can bind and inhibit receptor-bound uPA. Binding of 125I-labeled ATF (amino-terminal fragment of uPA) to human U937 monocyte-like cells can be competed for by uPA-PAI-1 complexes, but not by PAI-1 alone. Performed 125I-labeled uPA-PAI-1 complexes can bind to uPA receptor with the same binding specificity as uPA. PAI-1 also binds to, and inhibits the activity of, receptor-bound uPA in U937 cells, as shown in U937 cells by a caseinolytic plaque assay. Plasminogen activator activity of these cells is dependent on exogenous uPA, is competed for by receptor-binding diisopropyl fluorophosphate-treated uPA, and is inhibited by the addition of PAI-1. In conclusion, in U937 cells the binding to the receptor does not shield uPA from the action of PAI-1. The possibility that in adherent cells a different localization of PAI-1 and uPA leads to protection of uPA from PAI-1 is to be considered. | lld:pubmed |
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| pubmed-article:2544876 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2544876 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2544876 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2544876 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2544876 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2544876 | pubmed:author | pubmed-author:MayerMM | lld:pubmed |
| pubmed-article:2544876 | pubmed:author | pubmed-author:BlasiFF | lld:pubmed |
| pubmed-article:2544876 | pubmed:author | pubmed-author:DanøKK | lld:pubmed |
| pubmed-article:2544876 | pubmed:author | pubmed-author:RagnoPP | lld:pubmed |
| pubmed-article:2544876 | pubmed:author | pubmed-author:AndreasenPP | lld:pubmed |
| pubmed-article:2544876 | pubmed:author | pubmed-author:CubellisM VMV | lld:pubmed |
| pubmed-article:2544876 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2544876 | pubmed:volume | 86 | lld:pubmed |
| pubmed-article:2544876 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2544876 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2544876 | pubmed:pagination | 4828-32 | lld:pubmed |
| pubmed-article:2544876 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2544876 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2544876 | pubmed:articleTitle | Accessibility of receptor-bound urokinase to type-1 plasminogen activator inhibitor. | lld:pubmed |
| pubmed-article:2544876 | pubmed:affiliation | Institute of Microbiology, University of Copenhagen, Denmark. | lld:pubmed |
| pubmed-article:2544876 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2544876 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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