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Effect of purified, soluble urokinase receptor on the plasminogen-prourokinase activation system

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The extracellular proteolytic pathway mediated by the urokinase plasminogen activator (uPA) is a cascade system, initiated by activation of the zymogen, pro-uPA. Pro-uPA as well as uPA binds to the cellular uPA receptor (uPAR) which has a central function in cell-dependent acceleration of the cascade system. This role of uPAR is generally assumed to be a positioning effect since uPAR-expressing cells exclusively stimulate the activation of cell surface-bound plasminogen (Ellis et al. (1993) Methods Enzymol. 223, 223-233). However, it was recently reported that a recombinant, soluble uPAR (suPAR) was capable of accelerating plasminogen activation in solution (Higazi et al. (1995) J. Biol. Chem. 270, 17375-17380). In this work we show that suPAR as such has no accelerative role. In contrast, the progress of the activation reactions in a soluble system with pro-uPA and plasminogen was found to be attenuated by suPAR. This delay of the activation system was shown to include a partial inhibition of the plasmin-mediated activation of pro-uPA as well as of the uPA-mediated activation of plasminogen.

Original languageEnglish
JournalF E B S Letters
Volume393
Issue number1
Pages (from-to)31-6
Number of pages6
ISSN0014-5793
Publication statusPublished - 9 Sep 1996

    Research areas

  • Animals, CHO Cells, Cricetinae, Enzyme Activation, Humans, Plasminogen, Plasminogen Activators, Protein Precursors, Receptors, Cell Surface, Receptors, Urokinase Plasminogen Activator, Recombinant Fusion Proteins, Urokinase-Type Plasminogen Activator

ID: 46435161