The Role of Focal Adhesion Kinase in the TGF-β-Induced Myofibroblast Transdifferentiation of Human Tenon's Fibroblasts

Abstract

PurposeTo investigate the role of focal adhesion kinase (FAK) in transforming growth factor (TGF)-β-induced myofibroblast transdifferentiation of human Tenon's fibroblasts.MethodsPrimary cultured human Tenon's fibroblasts were exposed to TGF-β1 for up to 48 hours. The mRNA levels of FAK, α smooth muscle actin (αSMA), and β-actin were determined by quantitative real time reverse transcription polymerase chain reaction. The protein levels of collagen type I, FAK, phospho-FAK, αSMA, and β-actin were determined by Western immunoblots. After the small interfering RNA targeting FAK (siRNAFAK) molecules were delivered into the cells, the expressions of αSMA proteins were determined by Western immunoblots.ResultsIn human Tenon's fibroblasts, TGF-β1 significantly increased the mRNA and protein expressions of αSMA. However, when the action of FAK was inhibited using siRNAFAK, the TGF-β1-induced expression of αSMA was attenuated.ConclusionsOur data suggest that FAK may be associated with the TGF-β1-induced transdifferentiation of human Tenon's fibroblasts to myofibroblasts, which is the essential step of subconjunctival fibrosis.