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

E Rønne, N Behrendt, V Ellis, M Ploug, K Danø, G Høyer-Hansen

176 Citations (Scopus)

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 languageEnglish
JournalFEBS Letters
Volume288
Issue number1-2
Pages (from-to)233-6
Number of pages4
ISSN0014-5793
Publication statusPublished - 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

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