Abstract
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 |
Keywords
- 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