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Urokinase plasminogen activator induces smooth muscle cell migration: key role of growth factor‐like domain
Author(s) -
Victoria Stepanova,
Alex Bobik,
Robert Bibilashvily,
A. A. Belogurov,
И. Н. Рыбалкин,
S.P. Domogatsky,
Peter J. Little,
Elena A. Goncharova,
Vsevolod A. Tkachuk
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00993-9
Subject(s) - chemotaxis , microbiology and biotechnology , plasminogen activator , recombinant dna , urokinase , chemistry , growth factor , cell migration , urokinase receptor , activator (genetics) , receptor , platelet derived growth factor receptor , cell , biology , endocrinology , biochemistry , gene , genetics
We defined the role of urokinase plasminogen activator (uPA) and its growth factor‐like domain (GFD) in stimulating smooth muscle cell (SMC) migration. Recombinant uPA (r‐uPA) stimulated migration approximately 3‐fold whilst the recombinant uPA mutant containing an altered GFD (r‐uPAmut) was ineffective. Both uPA variants bound to the same high affinity receptor in a competitive manner. FGF‐2‐ and PDGF‐BB‐induced migration was also dependent on uPA, their effects being antagonized by addition of a uPA‐neutralizing antibody or the r‐uPAmut. Thus r‐uPA is chemotactic for SMC and stimulation of cell migration by PDGF‐BB and FGF‐2 is dependent on uPA. The GFD of uPA is essential for its chemotactic effects.