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Cell‐induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH 2 ‐terminal domain of the urokinase receptor
Author(s) -
Rønne Ebbe,
Behrendt Niels,
Ellis Vincent,
Ploug Michael,
Danø Keld,
Høyer-Hansen Gunilla
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81042-7
Subject(s) - monoclonal antibody , long term potentiation , terminal (telecommunication) , chemistry , urokinase receptor , microbiology and biotechnology , receptor , biophysics , urokinase , antibody , biochemistry , biology , immunology , computer science , genetics , telecommunications
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 [ 125 I]‐u‐PA to U937 cells, is directed against the u‐PA binding NH 2 ‐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.