Accessibility of receptor-bound urokinase to type-1 plasminogen activator inhibitor
Proceedings of the National Academy of Sciences of the United States of America, ISSN: 0027-8424, Vol: 86, Issue: 13, Page: 4828-4832
1989
- 185Citations
- 18Captures
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Metrics Details
- Citations185
- Citation Indexes184
- 184
- CrossRef111
- Patent Family Citations1
- Patent Families1
- Captures18
- Readers18
- 18
Article Description
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 I-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. Preformed I-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.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0024349195&origin=inward; http://dx.doi.org/10.1073/pnas.86.13.4828; http://www.ncbi.nlm.nih.gov/pubmed/2544876; https://pnas.org/doi/full/10.1073/pnas.86.13.4828; https://dx.doi.org/10.1073/pnas.86.13.4828; https://www.pnas.org/content/86/13/4828
Proceedings of the National Academy of Sciences
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