Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor
Research output: Contribution to journal › Journal article › Research › peer-review
We have raised four monoclonal antibodies recognizing different epitopes within the human cell-surface receptor for urokinase-type plasminogen activator (u-PA). One of these antibodies completely abolishes the potentiation of plasmin generation observed upon incubation of the zymogens pro-u-PA and plasminogen with U937 cells. This antibody, which is also the only one to completely inhibit the binding of DFP-inactivated [125I]-u-PA to U937 cells, is directed against the u-PA binding NH2-terminal domain of u-PAR, a well-defined fragment formed by limited chymotrypsin digestion of purified u-PAR, demonstrating the functional independence of the u-PA binding domain as well as the critical role of u-PAR in the assembly of the cell-surface plasminogen activation system.
Original language | English |
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Journal | FEBS Letters |
Volume | 288 |
Issue number | 1-2 |
Pages (from-to) | 233-6 |
Number of pages | 4 |
ISSN | 0014-5793 |
Publication status | Published - 19 Aug 1991 |
- Antibodies, Monoclonal, Cell Line, Chymotrypsin, Epitopes, Fibrinolysin, Humans, Kinetics, Plasminogen, Plasminogen Activators, Precipitin Tests, Receptors, Cell Surface, Receptors, Urokinase Plasminogen Activator, Structure-Activity Relationship, Journal Article, Research Support, Non-U.S. Gov't
Research areas
ID: 178215086