Interaction between kringle and growth-factor-like domains in the urokinase molecule: possible role in stimulation of
V V Stepanova1, I B Beloglazova, Y G Gursky
1Russian Cardiology Research Center, Ministry of Health of Russian Federation, Moscow, Russia.
Abstract:
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.
Related Concept Videos
Chemotaxis and Direction of Cell Migration
Enzyme-linked Receptors
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Intracellular Signaling Affects Focal Adhesions
Some...
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
Receptor Tyrosine Kinases
Mitogens and the Cell Cycle


