BACKGROUND The urokinase plasminogen activator receptor (uPAR, or PLAUR) has been implicated in the growth, metastasis, and angiogenesis of several solid and hemotologic malignancies. uPAR/PLAUR is part of a cell surface system that also consists of the serine protease uPA and several specific inhibitors (plasminogen activator inhibitors 1 and 2).1 This system has classically been thought to drive tumor progression by mediating directed extracellular proteolysis on the surface of migrating or invading cells. uPA can bind to uPAR/PLAUR leading to the subsequent activation of plasminogen to plasmin. Plasmin is a promiscuous protease that initiates several extracellular proteolytic cascades. The binding of uPA to uPAR/PLAUR increases the efficiency of plasminogen activation and also serves to localize these proteolytic cascades to the migrating or invading edge of cells. This proteolysis is tightly controlled by PAI-1 and PAI-2, and the PAI-uPA- uPAR/PLAUR complex can be internalized with uPAR/PLAUR being recycled to the cell surface.2 Thus, uPA, uPAR/PLAUR, and PAI-1 can all potentially be targeted for cancer therapy. In addition to mediating proteolysis, this receptor appears to also mediate cell signaling, proliferation, and survival.
1. Blasi, F. & Carmeliet, P.: Nat. Rev. Mol. Cell. Biol. 3:932-43, 2002
2. Mazar, A.P. : Clin Cancer Res. 14:5649-55, 2008
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