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Abstract
The urokinase-type plasminogen activator (uPA) system consists of a proteinase (the uPA), its receptor (the urokinase-type plasminogen activator receptor-uPAR or CD87) and two major inhibitors, the plasminogen activator inhibitor 1 (PAI-1) and the plasminogen activator inhibitor 2 (PAI-2).
The CD87 belongs to the Ly-6/uPAR/?-neurotoxin protein domain family. It is a single chain, heavily glycosylated cell-surface receptor, and is attached to the cell surface by glycosyl-phosphatidylinositol (GPI) anchor, thus it uses related transmembrane integrins as signal transduction devices.
When uPAR is released from the plasma membrane by cleavage of the GPI anchor, it is called soluble uPAR (suPAR).
The uPAR consists of three homologous internally disulphide-bonded domains (D1, D2 and D3), this multi-domain architecture of uPAR has proven to be sensitive to limited proteolysis, and particularly the linker region between domains D1 and D2.
The CD87 is measured by flow cytometry, immunoblots, immunohistochemistry, and radio-labeled uPA