Results 191 to 200 of about 27,307 (240)

The kringle stabilizes urokinase binding to the urokinase receptor

Blood, 2003
AbstractThe structural basis of the interaction between single-chain urokinase-type plasminogen activator (scuPA) and its receptor (uPAR) is incompletely defined. Several observations indicated the kringle facilitates the binding of uPA to uPAR. A scuPA variant lacking the kringle (ΔK-scuPA) bound to soluble uPAR (suPAR) with the similar “on-rate” but ...
Khalil, Bdeir, Alice, Kuo, Bruce S, Sachais, Ann H, Rux, Yasmina, Bdeir, Andrew, Mazar, Abd Al-Roof, Higazi, Douglas B, Cines   +7 more
openaire   +2 more sources

The receptor for urokinase‐plasminogen activator

Journal of Cellular Biochemistry, 1986
AbstractMany human cells and cell lines possess a specific receptor that binds urokinase plasminogen activator (uPA) with an affinity of about 10−10 M. Bound enzyme is not internalized, is slowly dissociated, and retains its enzymatic activity. The amino acid sequence of uPA responsible for receptor binding is located within the first 35 aminoterminal ...
Francesco Blasi, M. Patrizia Stoppelli, CUBELLIS, MARIA VITTORIA   +2 more
openaire   +3 more sources

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
openaire   +2 more sources

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, Ying, Wei, Harold A, Chapman   +2 more
openaire   +2 more sources

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; id_orcid 0000-0001-6422-6736, Petersen, Claus Munck, Christensen, Erik Ilsø, Davidsen, Ole, Gliemann, J   +4 more
openaire   +3 more sources

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, EA Robinson, Ullrich SJ, Stoppelli MP, CORTI , ANGELO, Cassani G, Blasi F.   +6 more
openaire   +2 more sources

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, K, Bdeir, E, Hiss, S, Arad, A, Kuo, I, Barghouti, D B, Cines   +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
openaire   +2 more sources

The urokinase receptor and integrins in cancer progression

Cellular and Molecular Life Sciences, 2008
Enhanced levels of expression of urokinase receptor (uPAR) and certain integrins have been linked to cancer cell progression. This has classically been attributed to matrix degradation via the activation of the urokinase (uPA)/plasmin system and modulation of cell motility and survival through integrin engagement.
C-H, Tang, Y, Wei
openaire   +2 more sources