THE UROKINASE RECEPTOR - STRUCTURE, REGULATION AND INHIBITOR-MEDIATEDINTERNALIZATION

Citation
F. Blasi et al., THE UROKINASE RECEPTOR - STRUCTURE, REGULATION AND INHIBITOR-MEDIATEDINTERNALIZATION, Fibrinolysis, 8, 1994, pp. 182-188
Citations number
88
Categorie Soggetti
Hematology
Journal title
ISSN journal
02689499
Volume
8
Year of publication
1994
Supplement
1
Pages
182 - 188
Database
ISI
SICI code
0268-9499(1994)8:<182:TUR-SR>2.0.ZU;2-F
Abstract
The receptor for urokinase plasminogen activator (uPAR) acts as an anc horage site for uPA on the cell surface where it stimulates pro-uPA ac tivation, allows the internalization of uPA:inhibitor and other comple xes and sends directly or indirectly signals into the cell that may pr omote migration, adhesion and growth. It is a GPI-anchored, three-doma in protein that belongs to the Ly6 family and is present at the focal and cell-to-cell contacts, where it concentrates uPA activity. Its act ivity appears to be important to regulate the invasiveness of human ca ncer cells both in vitro and in vivo, and its inhibition is now a targ et for antimetastatic: therapy.