scholarly journals EphA2 receptor tyrosine kinase regulates endothelial cell migration and vascular assembly through phosphoinositide 3-kinase-mediated Rac1 GTPase activation

2004 ◽  
Vol 117 (10) ◽  
pp. 2037-2049 ◽  
Author(s):  
D. M. Brantley-Sieders
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Endothelial Cell Migration ◽  
Rac1 Gtpase ◽  
Gtpase Activation ◽  
Phosphoinositide 3 Kinase

Role of protein tyrosine kinase in thrombin-induced endothelial cell migration

2000 ◽  
Vol 151 (1) ◽  
pp. 215
Author(s):  
H.J. Kruse ◽  
I. Wieczorek ◽  
G. Bauriedel ◽  
S. Schellong
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Endothelial Cell Migration ◽  
Protein Tyrosine

scholarly journals Semaphorin 4D/Plexin-B1 Induces Endothelial Cell Migration through the Activation of PYK2, Src, and the Phosphatidylinositol 3-Kinase-Akt Pathway

2005 ◽  
Vol 25 (16) ◽  
pp. 6889-6898 ◽  
Author(s):  
John R. Basile ◽  
Talayeh Afkhami ◽  
J. Silvio Gutkind
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Tyrosine Kinase ◽  
Axonal Guidance ◽  
Endothelial Cell Migration ◽  
Akt Pathway ◽  
Tyrosine Kinase Domain ◽  
Phosphatidylinositol 3 Kinase ◽  
Semaphorin 4D ◽  
Phosphatidylinositol 3

ABSTRACT Semaphorins are cell surface and secreted proteins that provide axonal guidance in neuronal tissues and regulate cell motility in many cell types. They act by binding a family of transmembrane receptors known as plexins, which belong to the c-Met family of scatter factor receptors but lack an intrinsic tyrosine kinase domain. Interestingly, we have recently shown that Plexin-B1 is highly expressed in endothelial cells and that its activation by Semaphorin 4D elicits a potent proangiogenic response (J. R. Basile, A. Barac, T. Zhu, K. L. Guan, and J. S. Gutkind, Cancer Res. 64:5212-5224, 2004). In searches for the underlying molecular mechanism, we observed that Semaphorin 4D-stimulated endothelial cell migration requires the activation of the phosphatidylinositol 3-kinase (PI3K)-Akt pathway. Surprisingly, we found that Plexin-B1 stimulates PI3K-Akt through the activation of an intracellular tyrosine kinase cascade that involves the sequential activation of PYK2 and Src. This results in the tyrosine phosphorylation of Plexin-B1, the rapid recruitment of a multimeric signaling complex that includes PYK2, Src, and PI3K to Plexin-B1 and the activation of Akt. These findings suggest that Plexin-B1 may achieve its numerous physiological functions through the direct activation of intracellular tyrosine kinase cascades.

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