Proteolytically inactive recombinant forms of urokinase suppress migration of endothelial cells.
Proteolytically inactive recombinant forms of urokinase (uPAHQ and amino-terminal fragment) inhibit spontaneous migration of endothelial cells; amino-terminal fragment also suppresses angiogenesis stimulated by basic fibroblast growth factor in vitro. These findings suggest the possibility of using synthesized proteolytically inactive recombinant forms of urokinase for the regulation of endothelial cell migration and suppression of neoangiogenesis.
Russian Cardiology Research-and-Production Complex, Ministry of Health of the Russian Federation, Moscow, Russia.
I B
IB
Beloglazova
E S
ES
Zubkova
D V
DV
Stambol'skii
O S
OS
Plekhanova
M Yu
MY
Men'shikov
Zh A
ZhA
Akopyan
R Sh
RSh
Bibilashvili
E V
EV
Parfenova
V A
VA
Tkachuk
D002465:Cell Movement / Q000187:drug effects*; D002478:Cells, Cultured; D042783:Endothelial Cells / Q000378:metabolism*; D004730:Endothelium, Vascular / Q000378:metabolism; D016222:Fibroblast Growth Factor 2 / Q000378:metabolism; D061307:Human Umbilical Vein Endothelial Cells / Q000378:metabolism; D006801:Humans; D009389:Neovascularization, Pathologic / Q000517:prevention & control*; D011994:Recombinant Proteins / Q000494:pharmacology*; D014568:Urokinase-Type Plasminogen Activator / Q000494:pharmacology*
D011994:Recombinant Proteins; D016222:Fibroblast Growth Factor 2; D014568:Urokinase-Type Plasminogen Activator