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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Vydané v:	FEBS letters Ročník 584; číslo 9; s. 1923 - 1930
Hlavní autori:	Blasi, Francesco, Sidenius, Nicolai
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	England Elsevier B.V 03.05.2010
Predmet:	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
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Popis
Shrnutí:	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.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23
ISSN:	0014-5793 1873-3468 1873-3468
DOI:	10.1016/j.febslet.2009.12.039