The urokinase receptor: Structure, regulation and inhibitor-mediated internalization

F. Blasi, M. Conese, L. B. Møller, N. Pedersen, U. Cavallaro, M. V. Cubellis, F. Fazioli, L. Hemandez-Marrero, P. Limongi, P. Munoz-Canoves, M. Resnati, L. Riittinen, N. Sidenius, E. Soravia, M. R. Soria, M. P. Stoppelli, D. Talarico, T. Teesalu, S. Valcamonica

Research output: Contribution to journalArticlepeer-review


The receptor for urokinase plasminogen activator (uPAR) acts as an anchorage site for uPA on the cell surface where it stimulates pro-uPA activation, allows the internalization of uPA:inhibitor and other complexes and sends directly or indirectly signals into the cell that may promote migration, adhesion and growth. It is a GPI-anchored, three-domain protein that belongs to the Ly6 family and is present at the focal and cell-to-cell contacts, where it concentrates uPA activity. Its activity appears to be important to regulate the invasiveness of human cancer cells both in vitro and in vivo, and its inhibition is now a target for antimetastatic therapy.

Original languageEnglish
Pages (from-to)182-188
Number of pages7
JournalFibrinolysis and Proteolysis
Issue numberSUPPL. 1
Publication statusPublished - 1994

ASJC Scopus subject areas

  • Hematology


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