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The intact urokinase receptor is required for efficient vitronectin binding: receptor cleavage prevents ligand interaction

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  1. Characterization of the contractile P2Y14 receptor in mouse coronary and cerebral arteries

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  2. Structural features of peptoid-peptide hybrids in lipid-water interfaces

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  3. Structure of a dimeric fungal α-type carbonic anhydrase

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  4. AKAP 18 alpha and gamma have opposing effects on insulin release in INS-1E cells

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  1. Tumor cell MT1-MMP is dispensable for osteosarcoma tumor growth, bone degradation and lung metastasis

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  2. Chylomicronemia From GPIHBP1 Autoantibodies Successfully Treated With Rituximab: A Case Report

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  3. Chylomicronemia from GPIHBP1 autoantibodies

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  4. Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

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  5. ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain

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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 languageEnglish
JournalF E B S Letters
Volume420
Issue number1
Pages (from-to)79-85
Number of pages7
ISSN0014-5793
Publication statusPublished - 22 Dec 1997

    Research areas

  • 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

ID: 46435290