Interaction between kringle and growth-factor-like domains in the urokinase molecule: possible role in stimulation of chemotaxis.
The results presented in this paper suggest the presence of an interaction between the kringle- and the growth-factor-like urokinase domains. This interaction regulates chemotactic properties of urokinase. We also show that interaction of urokinase with its "classical" receptor (uPAR) has a "permissive" effect on the interactions between the kringle domain and other targets on the cell surface. On the basis of our data we can suggest that uPAR serves as an "adaptor" for urokinase, and the binding of urokinase kringle domain to its receptor causes immediate activation of intracellular signaling and induction of cell migration.
Stepanova
V V
VV
Russian Cardiology Research Center, Ministry of Health of Russian Federation, Moscow, Russia.
Beloglazova
I B
IB
Gursky
Y G
YG
Bibilashvily
R S
RS
Parfyonova
Y V
YV
Tkachuk
V A
VA
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D002633:Chemotaxis / Q000187:drug effects; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins / Q000737:chemistry; D018082:Kringles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism; D055293:Receptors, Urokinase Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology
D036341:Intercellular Signaling Peptides and Proteins; C524898:PLAUR protein, human; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator