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

FEBS Letters

Preissner, Klaus T²  Høyer-Hansen, Gunilla¹  Behrendt, Niels¹  Danø, Keld¹  Ploug, Michael¹ 

[1] Finsen Laboratory, Rigshospitalet, Strandboulevarden 49, DK-2100 Copenhagen Ø., Denmark;Max-Planck-Institut, Haemostasis Research Unit, Kerckhoff-Klinik, D-61231 Bad Nauheim, Germany

关键词: Receptor cleavage;    Urokinase;    Urokinase receptor;    Vitronectin;    Real-time biomolecular interaction analysis;    uPA;    urokinase-type plasminogen activator;    pro-uPA;    pro-enzyme form of uPA;    uPAR;    uPA receptor;    uPAR(2+3);    uPAR containing only domains 2 and 3;    suPAR;    soluble form of uPAR;    PAI-1;    plasminogen activator inhibitor 1;    DFP;    diisopropyl fluorophosphate;    RU;    resonance unit;    Mab;    monoclonal antibody;   

DOI  :  10.1016/S0014-5793(97)01491-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown