, Volume 90, Issue 12, pp 1357-1359
Date: 17 Nov 2012

uPAR signaling is under par for the podocyte course

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The urokinase receptor, also known as uPAR or cluster of differentiation (CD) 87, is a multidomain glycoprotein tethered to the cell membrane with a glycosylphosphatidylinositol anchor. uPAR was originally identified as the binding site for the extracellular protease urokinase-type plasminogen activator (uPA) on the cell surface. However, uPAR interacts with many other proteins such as vitronectin, the uPAR-associated protein, and integrins [1]. uPAR is a part of the plasminogen activation system, which is not only involved in hemostasis but also in tissue reorganization including mammary gland involution and wound healing. The plasminogen activation system is important in reorganizing tissues through proteolysis. uPAR restricts plasminogen activation to the immediate vicinity of the cell membrane. Coordination of extracellular matrix (ECM) proteolysis and cell signaling underlies uPAR’s important function in cell migration, proliferation, and survival. As a result, various pharmaceuti