Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor

FEBS Lett. 1991 Aug 19;288(1-2):233-6. doi: 10.1016/0014-5793(91)81042-7.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal
  • Cell Line
  • Chymotrypsin / metabolism
  • Epitopes / immunology
  • Fibrinolysin / analysis
  • Humans
  • Kinetics
  • Plasminogen / metabolism*
  • Plasminogen Activators / metabolism*
  • Precipitin Tests
  • Receptors, Cell Surface / immunology
  • Receptors, Cell Surface / metabolism*
  • Receptors, Urokinase Plasminogen Activator
  • Structure-Activity Relationship


  • Antibodies, Monoclonal
  • Epitopes
  • PLAUR protein, human
  • Receptors, Cell Surface
  • Receptors, Urokinase Plasminogen Activator
  • Plasminogen
  • Plasminogen Activators
  • Chymotrypsin
  • Fibrinolysin