scholarly journals Troglitazone attenuates epidermal growth factor receptor signaling independently of peroxisome proliferator-activated receptor in PC-3 cells

2010 ◽  
Vol 25 (1) ◽  
Author(s):  
Xu
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Peroxisome Proliferator ◽  
Receptor Signaling ◽  
Peroxisome Proliferator Activated Receptor ◽  
Epidermal Growth ◽  
Growth Factor Receptor Signaling

scholarly journals Uterine and Vaginal Organ Growth Requires Epidermal Growth Factor Receptor Signaling from Stroma*

Endocrinology ◽  
1998 ◽  
Vol 139 (3) ◽  
pp. 913-921 ◽  
Author(s):  
Yun Kit Hom ◽  
Peter Young ◽  
Jane F. Wiesen ◽  
Päivi J. Miettinen ◽  
Rik Derynck ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Receptor Signaling ◽  
Organ Growth ◽  
Epidermal Growth ◽  
Growth Factor Receptor Signaling

scholarly journals Integrin α1β1 Regulates Epidermal Growth Factor Receptor Activation by Controlling Peroxisome Proliferator-Activated Receptor γ-Dependent Caveolin-1 Expression

2010 ◽  
Vol 30 (12) ◽  
pp. 3048-3058 ◽  
Author(s):  
Xiwu Chen ◽  
Carrie Whiting ◽  
Corina Borza ◽  
Wen Hu ◽  
Stacey Mont ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Peroxisome Proliferator ◽  
Ros Production ◽  
Peroxisome Proliferator Activated Receptor ◽  
Caveolin 1 ◽  
Egfr Activation ◽  
Epidermal Growth

ABSTRACT Integrin α1β1 negatively regulates the generation of profibrotic reactive oxygen species (ROS) by inhibiting epidermal growth factor receptor (EGFR) activation; however, the mechanism by which it does this is unknown. In this study, we show that caveolin-1 (Cav-1), a scaffolding protein that binds integrins and controls growth factor receptor signaling, participates in integrin α1β1-mediated EGFR activation. Integrin α1-null mesangial cells (MCs) have reduced Cav-1 levels, and reexpression of the integrin α1 subunit increases Cav-1 levels, decreases EGFR activation, and reduces ROS production. Downregulation of Cav-1 in wild-type MCs increases EGFR phosphorylation and ROS synthesis, while overexpression of Cav-1 in the integrin α1-null MCs decreases EGFR-mediated ROS production. We further show that integrin α1-null MCs have increased levels of activated extracellular signal-regulated kinase (ERK), which leads to reduced activation of peroxisome proliferator-activated receptor γ (PPARγ), a transcription factor that positively regulates Cav-1 expression. Moreover, activation of PPARγ or inhibition of ERK increases Cav-1 levels in the integrin α1-null MCs. Finally, we show that glomeruli of integrin α1-null mice have reduced levels of Cav-1 and activated PPARγ but increased levels of phosphorylated EGFR both at baseline and following injury. Thus, integrin α1β1 negatively regulates EGFR activation by positively controlling Cav-1 levels, and the ERK/PPARγ axis plays a key role in regulating integrin α1β1-dependent Cav-1 expression and consequent EGFR-mediated ROS production.

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