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Structure and function of the urokinase receptor.

A Mondino1, M Resnati, F Blasi

  • 1Dipartimento di Patologia e Medicina Molecolare, Università Vita-Salute San Raffaele, Milan, Italy.

Thrombosis and Haemostasis
|March 1, 2000
PubMed
Summary
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The urokinase plasminogen activator receptor (uPAR) can independently guide monocyte migration by undergoing a conformational change. This process, triggered by enzymatic cleavage, involves cytoskeletal reorganization and tyrosine kinase activation, suggesting uPAR acts as a chemokine.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • The urokinase plasminogen activator receptor (uPAR) is known to regulate cell adhesion, proteolysis, and migration.
  • Emerging evidence suggests uPAR possesses intrinsic chemokine-like properties, mediating monocyte chemotaxis and cytoskeletal changes independently of urokinase plasminogen activator (uPA).

Purpose of the Study:

  • To investigate the mechanism by which uPAR mediates chemotaxis independently of uPA binding.
  • To explore the conformational changes in uPAR that lead to chemotactic activity.

Main Methods:

  • Enzymatic cleavage of recombinant uPAR with chymotrypsin to mimic uPA-induced conformational changes.
  • Assessing monocyte migration in response to cleaved uPAR in vitro.
  • Investigating the involvement of pertussis-toxin sensitive pathways, tyrosine kinases, and cytoskeletal reorganization.

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Main Results:

  • Chymotrypsin cleavage of uPAR between domain 1 and 2 generated a functional receptor capable of mediating monocyte migration.
  • This uPAR-mediated migration was independent of uPA binding.
  • The process was sensitive to pertussis toxin and involved tyrosine kinase activation and cytoskeletal reorganization.

Conclusions:

  • uPAR can act as a pleiotropic ligand, mediating monocyte migration through a mechanism involving conformational changes and activation of intracellular signaling pathways.
  • Upon uPA binding, uPAR undergoes a conformational shift exposing a chemotactically active epitope, which can be mimicked by enzymatic cleavage.
  • These findings highlight a novel role for uPAR beyond its receptor function, potentially involving interactions with other surface molecules.