Inhibition of α-smooth muscle actin expression and migration of pterygium fibroblasts by coculture with amniotic mesenchymal stem cells

Curr Eye Res. 2014 Nov;39(11):1081-9. doi: 10.3109/02713683.2014.900806. Epub 2014 Apr 21.

Abstract

Purpose: Epithelial-mesenchymal transition (EMT) of normal conjunctival tissues is a major reason of pterygium generation; α-smooth muscle actin (α-SMA) is a maker in EMT. In this study, we investigated if human amniotic mesenchymal stem cells (hAMSCs) can inhibit α-SMA expression and migration of human pterygium fibroblasts (hPFs) in vitro.

Materials and methods: Coculture of hAMSCs and hPFs was completed by using a Transwell coculture system. The α-SMA expression of hPFs was detected by immunocytochemistry and western blot analysis. The migration ability of hPFs was measured by means of a migration assay. Immunoreactivity for α-SMA was detected in all pterygium fibroblasts examined.

Results: The expression of α-SMA in cocultured hPFs was significantly lower than in hPFs. Similar result was demonstrated in western blot analysis. In addition, migration assay showed that hAMSCs reduce the migration of hPFs.

Conclusions: These results suggested that hAMSCs have the potential to inhibit the generation and invasiveness of pterygium in vitro.

Keywords: coculture; human amniotic mesenchymal stem cells; human pterygium fibroblasts; migration; α-smooth muscle actin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Adipocytes / cytology
  • Adipocytes / physiology
  • Adult
  • Amnion / cytology*
  • Blotting, Western
  • Cell Differentiation
  • Cell Migration Assays
  • Cell Migration Inhibition / physiology*
  • Coculture Techniques
  • Down-Regulation
  • Female
  • Fibroblasts / metabolism
  • Fibroblasts / pathology*
  • Flow Cytometry
  • Fluorescent Antibody Technique, Indirect
  • Humans
  • Mesenchymal Stem Cells / physiology*
  • Osteoblasts / cytology
  • Osteoblasts / physiology
  • Pterygium / metabolism
  • Pterygium / pathology*

Substances

  • ACTA2 protein, human
  • Actins