Structure and Functions of the Urokinase Receptor
The receptor (uPAR) for the urokinase-type plasminogen activator (uPA) was firstly identified in 1985 on the surface of monocyte-like cells but only in 1990 uPAR protein was purified and cDNA cloned and sequenced. The first role proposed for uPAR was the focusing of the uPA proteolytic activity on the cell membrane, thus allowing cell migration through the extracellular matrix (ECM), without affecting the general architecture of the tissue. Since then, a large body of evidence clearly showed various roles for uPAR, independent of uPA enzymatic activity. In fact, uPAR is able to transduce proliferation, differentiation, adhesion, and migration signals into the cells, despite the absence of a transmembrane region and a cytosolic tail. However, the ability of uPAR to focus uPA activity on the cell membrane attributed to this specific receptor a key role in the plasminogen...
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