April 2009
Volume 50, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2009
Mitomycin C Inhibits Corneal Fibroblast Migration Through Dephosphorylation of FAK/Paxillin Signaling
Author Affiliations & Notes
  • S.-W. Chang
    Dept of Ophthal and Medical Research, Far Eastern Memorial Hospital, Ban-Chiao, Taiwan
  • T.-C. Chen
    Dept of Ophthal and Medical Research, Far Eastern Memorial Hospital, Ban-Chiao, Taiwan
  • T.-Y. Wang
    Dept of Ophthal and Medical Research, Far Eastern Memorial Hospital, Ban-Chiao, Taiwan
  • J.-L. Chang
    Dept of Ophthal and Medical Research, Far Eastern Memorial Hospital, Ban-Chiao, Taiwan
  • Footnotes
    Commercial Relationships  S.-W. Chang, None; T.-C. Chen, None; T.-Y. Wang, None; J.-L. Chang, None.
  • Footnotes
    Support  NSC- 97-2314-B-418-005-MY3
Investigative Ophthalmology & Visual Science April 2009, Vol.50, 4550. doi:
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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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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: : To investigate how Mitomycin C (MMC) retards corneal fibroblast migration.

Methods: : 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.

Results: : 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.

Conclusions: : MMC might prohibit corneal fibroblast migration by dephosphorylation and translocation of FAK and paxillin.

Keywords: cornea: stroma and keratocytes • wound healing • cell adhesions/cell junctions 
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