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The urokinase/urokinase-receptor system and cancer invasion.

Bailliere's clinical haematology, 1995
u-PA binds with high affinity to its specific GPI-anchored receptor on the cell surface. The binding has at least two important consequences: (1) it enhances the rate of plasminogen activation on the cell surface; and (2) it focuses the u-PA proteolytic activity at the leading front of migrating cells. Several recent findings suggest that surface-bound
CONESE, MASSIMO, F. Blasi
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Structure and Function of the Urokinase Receptor

Thrombosis and Haemostasis, 1999
SummaryThe binding of the urokinase plasminogen activator (uPA) to its receptor (uPAR) regulates cell adhesion, surface proteolysis, chemotaxis and cell extravasation in a number of experimental systems. Recent evidences have suggested that uPAR can by itself mediate chemotaxis of human monocytes and cause profound changes in cytoskeletal organization ...
A, Mondino, M, Resnati, F, Blasi
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Urokinase receptors in human monocytes

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1990
Receptors for the 54 kDa plasminogen activator urokinase were characterized in freshly isolated and 5-14 day cultured human monocytes. The half saturation constant was about 55 pM in freshly isolated monocytes at 4 degrees C and 140 pM at 37 degrees C.
Nykjaer, A   +4 more
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Urokinase Receptor and Integrin Interactions

Current Pharmaceutical Design, 2003
Urokinase receptors (uPAR) were initially thought to function simply as a mechanism to concentrate the urokinase/plasmin system toward the cell surface. However, extensive evidence has accumulated that this glycolipid-anchored receptor also functions in both the adhesive and signaling pathways of many migratory cells. Mechanisms by which uPAR exercises
Matthias C, Kugler   +2 more
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The Receptor-Binding Sequence of Urokinase

1987
uPA is the urokinase type of plasminogen activator that has been associated with cellular invasion and tissue involution. Specific uPA receptors have been recently described (1,2). The receptor-binding domain of uPA is located in the 17,000 dalton amino-terminal fragment (ATF) and it is completely independent of the catalytic domain.
Appella E   +6 more
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Lysis of Plasma Clots by Urokinase-Soluble Urokinase Receptor Complexes

Blood, 1998
AbstractSingle-chain urokinase plasminogen activator (scuPA), the unique form secreted by cells, expresses little intrinsic plasminogen activator activity. scuPA can be activated by proteolytic cleavage to form a two-chain enzyme (tcuPA), which is susceptible to inhibition by plasminogen activator inhibitor type I (PAI-1).
A A, Higazi   +6 more
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The Urokinase Receptor and Cell Migration

Seminars in Thrombosis and Hemostasis, 1996
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
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Regulation of Integrin Function by the Urokinase Receptor

Science, 1996
Integrin function is central to inflammation, immunity, and tumor progression. The urokinase-type plasminogen activator receptor (uPAR) and integrins formed stable complexes that both inhibited native integrin adhesive function and promoted adhesion to vitronectin via a ligand binding site on uPAR.
Y, Wei   +6 more
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Urokinase and urokinase receptor expression in somatic cell hybrids

Fibrinolysis, 1994
To study the mechanisms that control cell-bound urokinase (u-PA) activity we characterised the expression of u-PA and its cellular receptor (u-PAR) in somatic cell hybrids between mouse L fibroblasts that do not produce u-PA and human HT1080 fibrosarcoma cells that express high levels of u-PA and u-PAR. Although the hybrids possessed a number of copies
Mazzieri R.   +8 more
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