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.
Originalsprog | Engelsk |
---|---|
Tidsskrift | FEBS Letters |
Vol/bind | 288 |
Udgave nummer | 1-2 |
Sider (fra-til) | 233-6 |
Antal sider | 4 |
ISSN | 0014-5793 |
Status | Udgivet - 19 aug. 1991 |