COMMENTARY
See article on page 798
Urokinase receptor is a key player in tumour progression
| The first 150 words of the full text of this article appear below. |
Cell-cell and cell-extracellular matrix (ECM)
interactions are essential for cell migration, tissue remodelling,
angiogenesis, and tumorigenesis. Pericellular proteolysis of cell
surface molecules and ECM provides crucial information in the local
environment. Urokinase (uPA) plays an important role through the
activation of plasminogen to plasmin, which regulates degradation of
elements within the ECM, such as fibrin, fibronectin and lamin, and
proteolytic activation of growth factors including hepatocyte growth
factor (HGF), basic fibroblast growth factor (FGF-2) and transforming growth factor 
(TGF-). Plasmin also activates the proenzyme forms
of the matrix metalloproteinases (MMPs), such as MT1-MMP,1 MMP-2 and MMP-9.2 uPA activation is regulated by its
specific cell surface receptor, urokinase receptor (uPAR). Binding of
uPA to its receptor (uPAR) accelerates uPA activation from an inactive proenzyme (pro-uPA). The activity of plasminogen activators can be
regulated by the specific inhibitors, plasminogen activator inhibitor 1 (PAI-1) and plasminogen activator inhibitor 2 (PAI-2). The urokinase
system is
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Gut 1998 43: 798-805.[Abstract] [Full Text] [PDF]
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