scholarly journals MicroRNA-106b is involved in transforming growth factor β1–induced cell migration by targeting disabled homolog 2 in cervical carcinoma

2016 ◽  
Vol 35 (1) ◽  
Author(s):  
Yuan Cheng ◽  
Yanli Guo ◽  
Youyi Zhang ◽  
Ke You ◽  
Zijian Li ◽  
...  
Keyword(s):  
Cell Migration ◽  
Growth Factor ◽  
Cervical Carcinoma ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β1

scholarly journals Rapid Up-Regulation of α4 Integrin-mediated Leukocyte Adhesion by Transforming Growth Factor-β1

2003 ◽  
Vol 14 (1) ◽  
pp. 54-66 ◽  
Author(s):  
Rubén A. Bartolomé ◽  
Francisco Sanz-Rodrı́guez ◽  
Mar M. Robledo ◽  
Andrés Hidalgo ◽  
Joaquin Teixidó
Keyword(s):  
Cell Migration ◽  
Cell Adhesion ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Human Peripheral Blood ◽  
Transforming Growth Factor Β1 ◽  
Small Gtpase ◽  
Mitogen Activated Protein Kinase ◽  
Intracellular Camp ◽  
Tgf Β1

The α4 integrins (α4β1 and α4β7) are cell surface heterodimers expressed mostly on leukocytes that mediate cell-cell and cell-extracellular matrix adhesion. A characteristic feature of α4 integrins is that their adhesive activity can be subjected to rapid modulation during the process of cell migration. Herein, we show that transforming growth factor-β1 (TGF-β1) rapidly (0.5–5 min) and transiently up-regulated α4 integrin-dependent adhesion of different human leukocyte cell lines and human peripheral blood lymphocytes (PBLs) to their ligands vascular cell adhesion molecule-1 (VCAM-1) and connecting segment-1/fibronectin. In addition, TGF-β1 enhanced the α4 integrin-mediated adhesion of PBLs to tumor necrosis factor-α–treated human umbilical vein endothelial cells, indicating the stimulation of α4β1/VCAM-1 interaction. Although TGF-β1 rapidly activated the small GTPase RhoA and the p38 mitogen-activated protein kinase, enhanced adhesion did not require activation of both signaling molecules. Instead, polymerization of actin cytoskeleton triggered by TGF-β1 was necessary for α4 integrin-dependent up-regulated adhesion, and elevation of intracellular cAMP opposed this up-regulation. Moreover, TGF-β1 further increased cell adhesion mediated by α4 integrins in response to the chemokine stromal cell-derived factor-1α. These data suggest that TGF-β1 can potentially contribute to cell migration by dynamically regulating cell adhesion mediated by α4 integrins.

Ixodid tick salivary gland extracts suppress human transforming growth factor-β1 triggered signalling pathways in cervical carcinoma cells

Biologia ◽  
2018 ◽  
Vol 73 (11) ◽  
pp. 1109-1122 ◽  
Author(s):  
Viera Holíková ◽  
Iveta Štibrániová ◽  
Pavlína Bartíková ◽  
Mirko Slovák ◽  
Mária Kazimírová
Keyword(s):  
Salivary Gland ◽  
Growth Factor ◽  
Cervical Carcinoma ◽  
Transforming Growth Factor ◽  
Ixodid Tick ◽  
Transforming Growth Factor Β1 ◽  
Carcinoma Cells ◽  
Signalling Pathways
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