Spleen Tyrosine Kinase Mediates BEAS-2B Cell Migration and Proliferation and Human Rhinovirus-Induced Expression of Vascular Endothelial Growth Factor and Interleukin-8

2011 ◽  
Vol 340 (2) ◽  
pp. 277-285 ◽  
Author(s):  
Xiaomin Wang ◽  
Mirek Mychajlowycz ◽  
Christine Lau ◽  
Carlos Gutierrez ◽  
Jeremy A. Scott ◽  
...  
2019 ◽  
Vol 7 (27) ◽  
pp. 4272-4279 ◽  
Author(s):  
Xueli Ren ◽  
Jun Akimoto ◽  
Hideyuki Miyatake ◽  
Seiichi Tada ◽  
Liping Zhu ◽  
...  

VEGF isoforms immobilised by photo-reactive gelatin (AzPhe-gelatin) enhance cell migration and proliferation.


2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Cuneyt Kemal Buharalioglu ◽  
Fariborz A Yaghini ◽  
Chi Young Song ◽  
Hafiz U Ghafoor ◽  
Anne M Estes ◽  
...  

2006 ◽  
Vol 17 (8) ◽  
pp. 3508-3520 ◽  
Author(s):  
Fabrice Le Boeuf ◽  
François Houle ◽  
Mark Sussman ◽  
Jacques Huot

Focal adhesion kinase (FAK) is phosphorylated on tyrosine and serine residues after cell activation. In the present work, we investigated the relationship between tyrosine and serine phosphorylation of FAK in promoting endothelial cell migration in response to vascular endothelial growth factor (VEGF). We found that VEGF induces the activation of the Rho-dependent kinase (ROCK) downstream from vascular endothelial growth factor receptor (VEGFR) 2. In turn, activated ROCK directly phosphorylates FAK on Ser732. Proline-rich tyrosine kinase-2 (Pyk2) is also activated in response to VEGF. Its activation requires the clustering of integrin αvβ3 and triggers directly the phosphorylation of Tyr407 within FAK, an event necessary for cell migration. Interestingly, ROCK-mediated phosphorylation of Ser732 is essential for Pyk2-dependent phosphorylation of Tyr407, because the latter is abrogated in cells expressing a FAK mutant that is nonphosphorylatable on Ser732. We suggest that VEGF elicits the activation of the VEGFR2–ROCK pathway, leading to phosphorylation of Ser732 within FAK. In turn, phosphorylation of Ser732 would change the conformation of FAK, making it accessible to Pyk2 activated in response to its association with integrin β3. Then, activated Pyk2 triggers the phosphorylation of FAK on Tyr407, promoting cell migration.


2021 ◽  
Vol 157 ◽  
pp. 103186
Author(s):  
Avash Das ◽  
Somnath Mahapatra ◽  
Dhrubajyoti Bandyopadhyay ◽  
Santanu Samanta ◽  
Sandipan Chakraborty ◽  
...  

Science ◽  
1992 ◽  
Vol 255 (5047) ◽  
pp. 989-991 ◽  
Author(s):  
C de Vries ◽  
J. Escobedo ◽  
H Ueno ◽  
K Houck ◽  
N Ferrara ◽  
...  

2008 ◽  
Vol 44 (13) ◽  
pp. 1914-1921 ◽  
Author(s):  
Pedro M. Lacal ◽  
Veronica Morea ◽  
Federica Ruffini ◽  
Angela Orecchia ◽  
Annalisa S. Dorio ◽  
...  

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