Abstract
The role of integrin-linked kinase (ILK) in transforming growth factor β (TGFβ)-mediated epithelial to mesenchymal transition was investigated. A stable transfection of dominant-negative ILK results in the prevention of TGFβ-mediated E-cadherin delocalization. TGFβ-mediated phosphorylation of Akt at Ser-473 was inhibited by dominant-negative ILK and PI3K inhibitors, LY294002 and wortmannin. Treatment with TGFβ stimulated induction of Akt and ILK kinase activity in HaCat control cells. This increased ILK activity by TGFβ was lowered by PI3K inhibitor, LY294002. In addition, PI3K inhibitor, dominant-negative Akt, and dominant-negative ILK could not block TGFβ-mediated C-terminal phosphorylation of Smad2. Taken together, these data suggest that PI3K–ILK–Akt pathway that is independent of the TGFβ-induced Smad pathway is required for TGFβ-mediated epithelial to mesenchymal transition.
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