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  • Title: The urokinase receptor and cell migration.
    Author: Blasi F.
    Journal: Semin Thromb Hemost; 1996; 22(6):513-6. PubMed ID: 9122717.
    Abstract:
    The receptor (u-PAR) for urokinase plasminogen activator (u-PA) is a three-domain protein, GPI-anchored to the cell surface, which focuses the enzymatic activity of u-PA, and allows the cell surface activation of plasminogen. Regulation of the activity of u-PA is also mediated by u-PAR. In fact, while active u-PA is not internalized or degraded, rather remaining active at the cell surface, serpin-inactivated u-PA is internalized, through the intervention of a second molecule, the alpha 2-macroglobulin receptor (LRP). In the process u-PAR too is internalized and possibly recycles back to the cell surface. In addition, u-PAR occupancy can also directly transduce migratory signals, like chemotaxis, that do not require the protease activity of u-PA. Occupancy of u-PAR activates tyrosine kinases, in particular of p56/p59hck, through an as yet undefined transmembrane adaptor.
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