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S.-W. Chang, T.-C. Chen, T.-Y. Wang, J.-L. Chang; Mitomycin C Inhibits Corneal Fibroblast Migration Through Dephosphorylation of FAK/Paxillin Signaling. Invest. Ophthalmol. Vis. Sci. 2009;50(13):4550.
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To investigate how Mitomycin C (MMC) retards corneal fibroblast migration.
Primary human corneal fibroblasts were treated with MMC 0.05, 0.1 and 0.2 mg/ml for 5 minutes. Migration rate of MMC-treated corneal fibroblasts was studied using migration assay with culture inserts and documented by phase-contrast microscopy for 48 hours. Focal adhesion kinase (FAK) and paxillin transcript and expression relative to migratory proteins and adhesion proteins were determined by quantitative real-time PCR and Western blotting, respectively. The change of FAK and paxillin distribution in the MMC-treated corneal cell migration was documented by molecular imaging analysis.
Migration assay revealed that MMC treatment significantly retarded corneal fibroblast migration. MMC reduced the intracellular mRNA and protein expressions of FAK but enhanced paxillin expression in a MMC dose-dependent manner. Immunoprecipitation assay illustrated that MMC blocked FAK and paxillin phosphorylation at tyrosine sites. Molecular imaging analysis demonstrated that MMC treatment induced FAK translocation to the terminal of F-actin filament from lamellipodia/filopodia regions to cytosol.
MMC might prohibit corneal fibroblast migration by dephosphorylation and translocation of FAK and paxillin.
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