scholarly journals PLAUR (plasminogen activator, urokinase receptor)

2011 ◽  
Author(s):  
B Jacobsen ◽  
M Illemann ◽  
M Ploug
Keyword(s):  
Plasminogen Activator ◽  
Urokinase Receptor

Recombinant soluble urokinase receptor as a scavenger for urokinase-type plasminogen activator (uPA)

FEBS Letters ◽  
1994 ◽  
Vol 337 (2) ◽  
pp. 131-134 ◽  
Author(s):  
O. Wilhelm ◽  
U. Weidle ◽  
S. Höhl ◽  
P. Rettenberger ◽  
M. Schmitt ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Urokinase Receptor ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator

scholarly journals Concurrent Upregulation of Urokinase Plasminogen Activator Receptor and CD11b during Tuberculosis and Experimental Endotoxemia

2001 ◽  
Vol 69 (8) ◽  
pp. 5182-5185 ◽  
Author(s):  
Nicole P. Juffermans ◽  
Pascale E. P. Dekkers ◽  
Annelies Verbon ◽  
Peter Speelman ◽  
Sander J. H. van Deventer ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Healthy Volunteers ◽  
Plasminogen Activator ◽  
Urokinase Plasminogen Activator ◽  
Urokinase Receptor ◽  
Urokinase Plasminogen Activator Receptor ◽  
Cd11b Expression ◽  
Experimental Endotoxemia ◽  
Plasminogen Activator Receptor

ABSTRACT Patients with tuberculosis had higher expression of monocyte urokinase receptor (uPAR) and CD11b than controls. In vitro, lipoarabinomannan and lipopolysaccharide (LPS) from Escherichia coli shared the ability to enhance uPAR and CD11b expression on monocytes and granulocytes. In healthy volunteers, LPS induced increases in monocyte and granulocyte uPAR and CD11b.

scholarly journals Vitronectin Concentrates Proteolytic Activity on the Cell Surface and Extracellular Matrix by Trapping Soluble Urokinase Receptor-Urokinase Complexes

Blood ◽  
1998 ◽  
Vol 91 (7) ◽  
pp. 2305-2312 ◽  
Author(s):  
Triantafyllos Chavakis ◽  
Sandip M. Kanse ◽  
Barbara Yutzy ◽  
H. Roger Lijnen ◽  
Klaus T. Preissner
Keyword(s):  
Monoclonal Antibody ◽  
Extracellular Matrix ◽  
Cell Surface ◽  
Plasminogen Activator ◽  
Umbilical Vein ◽  
Urokinase Receptor ◽  
Enzyme Linked Immunosorbent Assay ◽  
Tissue Remodelling ◽  
Amino Terminal ◽  
Plasminogen Activator Activity

Abstract Urokinase-type-plasminogen activator (uPA) and its receptor are localized in the vessel wall where they are involved in cellular activation and remodelling processes. Besides the cell surface glycolipid (GPI)-anchored urokinase receptor (uPAR), which binds uPA with high affinity, recent evidence points to the existence of soluble uPAR (suPAR), as well. In the present study, the origin, binding mechanism, and cellular effects of suPAR were examined. Under basal conditions human vascular smooth muscle cells (HVSMC), human umbilical vein endothelial cells (HUVEC), and monocytic cells released 0.1 to 2 ng/mL suPAR, which was increased twofold to fivefold after phorbol ester (PMA) stimulation, as measured by a function-dependent enzyme-linked immunosorbent assay (ELISA). suPAR alone did not bind to HVSMC or HUVEC, but reduced cellular uPA binding by 50% to 70%. However, after removal of GPI-uPAR with phosphatidylinositol-specific phospholipase C, suPAR dose-dependently increased uPA binding by fourfold to fivefold. This increase in binding was completely inhibited by vitronectin (VN) and by a monoclonal antibody against VN, but not by other matrix proteins or antibodies. Thus, VN-mediated uPA binding to cells was regulated by the ratio of soluble to surface-associated uPAR. In a uPAR-deficient cell line (LM-TK−), suPAR increased uPA binding up to 10-fold, whereas the truncated receptor lacking the amino-terminal uPA-binding domain was ineffective. The formation of a ternary uPA/suPAR/VN-complex on the cell surface and the free extracellular matrix could be inhibited by a monoclonal antibody against VN, as well as by plasminogen activator inhibitor-1 (PAI-1). Moreover, VN-mediated binding of the uPA/suPAR-complex led to a fivefold increase in plasminogen activator activity. Through this novel pathway, VN concentrates the uPA/suPAR-complex to cell surfaces and extracellular matrix sites, leading to the accumulation of plasminogen activator activity required for cell migration and tissue remodelling processes.

scholarly journals Enhancement of the Enzymatic Activity of Single-chain Urokinase Plasminogen Activator by Soluble Urokinase Receptor

1995 ◽  
Vol 270 (29) ◽  
pp. 17375-17380 ◽  
Author(s):  
Abd Al-Roof Higazi ◽  
Robert L. Cohen ◽  
Jack Henkin ◽  
Douglas Kniss ◽  
Bradford S. Schwartz ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Plasminogen Activator ◽  
Urokinase Plasminogen Activator ◽  
Urokinase Receptor ◽  
Single Chain

Influence of the extraction procedure on plasminogen activator inhibitor-2 (PAI-2) and urokinase receptor (uPAR) assays in breast cancer tissues

1996 ◽  
Vol 41 (2) ◽  
pp. 141-146 ◽  
Author(s):  
Cécile Bouchet-Bernet ◽  
Frédérique Spyratos ◽  
Catherine Andrieu ◽  
Stephanie Deytieux ◽  
Veronique Bécette ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Plasminogen Activator ◽  
Extraction Procedure ◽  
Plasminogen Activator Inhibitor ◽  
Urokinase Receptor ◽  
Cancer Tissues ◽  
Activator Inhibitor
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