The intact urokinase receptor is required for efficient vitronectin binding: receptor cleavage prevents ligand interaction
Research output: Contribution to journal › Journal article › Research › peer-review
The urokinase receptor (uPAR) is a receptor for both urokinase plasminogen activator (uPA) and the adhesion protein vitronectin. There are two forms of cell surface-bound uPAR; intact uPAR and a cleaved form, uPAR(2+3), which is formed by uPA-catalyzed cleavage of uPAR. In ligand-blotting experiments we found that vitronectin binds uPAR but not uPAR(2+3). In real-time biomolecular interaction analysis using recombinant, soluble uPAR (suPAR) both plasma and multimeric forms of vitronectin bound to intact, antibody-immobilized suPAR. Monoclonal antibodies against domain 1 of uPAR blocked suPAR binding to vitronectin and vitronectin did not interact with suPAR(2+3). Both suPAR(2+3) and the isolated domain 1 failed to compete with the intact suPAR in binding to vitronectin. We therefore conclude that the intact receptor is required for efficient vitronectin binding.
Original language | English |
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Journal | FEBS Letters |
Volume | 420 |
Issue number | 1 |
Pages (from-to) | 79-85 |
Number of pages | 7 |
ISSN | 0014-5793 |
Publication status | Published - 22 Dec 1997 |
Externally published | Yes |
- Antibodies, Monoclonal, Binding, Competitive, Biosensing Techniques, Humans, Ligands, Neuraminidase, Plasminogen Activator Inhibitor 1, Receptors, Cell Surface, Receptors, Urokinase Plasminogen Activator, Solubility, Urokinase-Type Plasminogen Activator, Vitronectin, Journal Article, Research Support, Non-U.S. Gov't
Research areas
ID: 178215833