The urokinase receptor: Focused cell surface proteolysis, cell adhesion and signaling

Plasma membrane urokinase-type plasminogen activator (uPA)-receptor (uPAR) is a GPI-anchored protein that binds with high-affinity and activates the serine protease uPA, thus regulating proteolytic activity at the cell surface. In addition, uPAR is a signaling receptor that often does not require it...

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Bibliographic Details
Published in:FEBS letters Vol. 584; no. 9; pp. 1923 - 1930
Main Authors: Blasi, Francesco, Sidenius, Nicolai
Format: Journal Article
Language:English
Published: England Elsevier B.V 03.05.2010
Subjects:
Animals
Cell Adhesion
Cell migration
Cell proliferation
Humans
Membrane Glycoproteins - chemistry
Membrane Glycoproteins - metabolism
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Models, Molecular
Molecular Conformation
Protein Binding - physiology
Protein Processing, Post-Translational
Receptors, Urokinase Plasminogen Activator - chemistry
Receptors, Urokinase Plasminogen Activator - metabolism
Receptors, Urokinase Plasminogen Activator - physiology
Signal Transduction - physiology
Signaling
Urokinase receptor uPAR
Cell proliferation
Signaling
Urokinase receptor uPAR
Cell migration
Cell adhesion
ISSN:0014-5793, 1873-3468, 1873-3468
Online Access:Get full text
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Summary:Plasma membrane urokinase-type plasminogen activator (uPA)-receptor (uPAR) is a GPI-anchored protein that binds with high-affinity and activates the serine protease uPA, thus regulating proteolytic activity at the cell surface. In addition, uPAR is a signaling receptor that often does not require its protease ligand or its proteolytic function. uPAR is highly expressed during tissue reorganization, inflammation, and in virtually all human cancers. Since its discovery, in vitro and in vivo models, as well as retrospective clinical studies have shown that over-expression of components of the uPA/uPAR-system correlates with increased proliferation, migration, and invasion affecting the malignant phenotype of cancer. uPAR regulates the cells–extracellular matrix interactions promoting its degradation and turnover through the plasminogen activation cascade.
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ISSN:0014-5793
1873-3468
1873-3468
DOI:10.1016/j.febslet.2009.12.039