scholarly journals An Anti-Urokinase Plasminogen Activator Receptor Antibody (ATN-658) Blocks Prostate Cancer Invasion, Migration, Growth, and Experimental Skeletal Metastasis In Vitro and In Vivo

Neoplasia ◽  
2010 ◽  
Vol 12 (10) ◽  
pp. 778-788 ◽  
Author(s):  
Shafaat A. Rabbani ◽  
Bushra Ateeq ◽  
Ani Arakelian ◽  
Maria Luisa Valentino ◽  
David E. Shaw ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Plasminogen Activator ◽  
Skeletal Metastasis ◽  
Urokinase Plasminogen Activator ◽  
Cancer Invasion ◽  
Urokinase Plasminogen Activator Receptor ◽  
Receptor Antibody ◽  
Plasminogen Activator Receptor

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.

Plasma levels of intact and cleaved urokinase plasminogen activator receptor (uPAR) in men with clinically localised prostate cancer

2017 ◽  
Vol 70 (12) ◽  
pp. 1063-1068
Author(s):  
Gitte Kristensen ◽  
Kasper Drimer Berg ◽  
Solvej Lippert ◽  
Ib Jarle Christensen ◽  
Klaus Brasso ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Plasminogen Activator ◽  
Plasma Levels ◽  
Specific Antigen ◽  
Roc Curves ◽  
Urokinase Plasminogen Activator ◽  
Clinicopathological Parameters ◽  
Prognostic Information ◽  
Urokinase Plasminogen Activator Receptor ◽  
Plasminogen Activator Receptor

AimsLymph node metastasis (N1) is an adverse prognostic factor for men with clinically localised prostate cancer (PCa), but the prediction of N1 disease remains difficult. Urokinase plasminogen activator receptor (uPAR) plays an important role in angiogenesis and tumorigenesis. We analysed whether plasma levels of the soluble uPAR forms uPAR(I-III), uPAR(II-III) and uPAR(I) were associated with the risk of N1 disease in men with clinically localised PCa.MethodsThe present study includes all men (n=518) who underwent radical prostatectomy (RP) for clinically localised PCa, 29 of whom had N1 disease. Soluble uPAR forms were measured using three time-resolved fluorescence immunoassays. The prognostic value of the different uPAR forms together with clinicopathological parameters for N1 disease were analysed using logistic regression, receiver operating characteristic (ROC) regression analysis and quantified using the areas under the ROC curve (AUC).ResultsAll soluble uPAR levels were significantly (p=0.03) higher in patients with N1 disease compared with patients with N0/x disease. ROC curves including clinical tumour stage, biopsy Gleason score, prostate-specific antigen and percent positive biopsies had an AUC of 87.7% for prediction of N1 disease. With the addition of uPAR(I) to the model, the AUC increased to 88.4%.ConclusionsAddition of uPAR(I) level to known diagnostic parameters did not increase the prediction of N1 disease following RP in men with clinically localised PCa. Our results indicate that the plasma levels at diagnosis of the different uPAR forms do not hold important predictive or prognostic information in men with clinically localised PCa.

scholarly journals Selective abrogation of the uPA-uPAR interaction in vivo reveals a novel role in suppression of fibrin-associated inflammation

Blood ◽  
2010 ◽  
Vol 116 (9) ◽  
pp. 1593-1603 ◽  
Author(s):  
Brian M. Connolly ◽  
Eun Young Choi ◽  
Henrik Gårdsvoll ◽  
Alexandra L. Bey ◽  
Brooke M. Currie ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Tissue Regeneration ◽  
Urokinase Plasminogen Activator ◽  
Amino Acid Substitutions ◽  
Fibrin Deposition ◽  
Urokinase Plasminogen Activator Receptor ◽  
Plasminogen Activator Receptor ◽  
Multiple Ligands

The urokinase plasminogen activator receptor (uPAR) has emerged as a potential regulator of cell adhesion, cell migration, proliferation, differentiation, and cell survival in multiple physiologic and pathologic contexts. The urokinase plasminogen activator (uPA) was the first identified ligand for uPAR, but elucidation of the specific functions of the uPA-uPAR interaction in vivo has been difficult because uPA has important physiologic functions that are independent of binding to uPAR and because uPAR engages multiple ligands. Here, we developed a new mouse strain (PlauGFDhu/GFDhu) in which the interaction between endogenous uPA and uPAR is selectively abrogated, whereas other functions of both the protease and its receptor are retained. Specifically, we introduced 4 amino acid substitutions into the growth factor domain (GFD) of uPA that abrogate uPAR binding while preserving the overall structure of the domain. Analysis of PlauGFDhu/GFDhu mice revealed an unanticipated role of the uPA-uPAR interaction in suppressing inflammation secondary to fibrin deposition. In contrast, leukocyte recruitment and tissue regeneration were unaffected by the loss of uPA binding to uPAR. This study identifies a principal in vivo role of the uPA-uPAR interaction in cell-associated fibrinolysis critical for suppression of fibrin accumulation and fibrin-associated inflammation and provides a valuable model for further exploration of this multifunctional receptor.

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