Effect of purified, soluble urokinase receptor on the plasminogen-prourokinase activation system
Research output: Contribution to journal › Journal article › Research › peer-review
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 language | English |
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Journal | FEBS Letters |
Volume | 393 |
Issue number | 1 |
Pages (from-to) | 31-6 |
Number of pages | 6 |
ISSN | 0014-5793 |
Publication status | Published - 9 Sep 1996 |
Externally published | Yes |
- 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, Journal Article, Research Support, Non-U.S. Gov't
Research areas
ID: 180823533