June 2015
Volume 56, Issue 7
Free
ARVO Annual Meeting Abstract  |   June 2015
Role of acetylation in the pathogenesis of proliferative vitreoretinopathy
Author Affiliations & Notes
  • Elaine D Por
    Ocular Trauma, USAISR, JBSA - Fort Sam Houston, TX
  • Whitney Greene
    Ocular Trauma, USAISR, JBSA - Fort Sam Houston, TX
  • Anthony James Johnson
    Ocular Trauma, USAISR, JBSA - Fort Sam Houston, TX
  • Heuy-Ching Hetty Wang
    Ocular Trauma, USAISR, JBSA - Fort Sam Houston, TX
  • Footnotes
    Commercial Relationships Elaine Por, None; Whitney Greene, None; Anthony Johnson, None; Heuy-Ching Wang, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science June 2015, Vol.56, 195. doi:
  • Views
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      Elaine D Por, Whitney Greene, Anthony James Johnson, Heuy-Ching Hetty Wang; Role of acetylation in the pathogenesis of proliferative vitreoretinopathy. Invest. Ophthalmol. Vis. Sci. 2015;56(7 ):195.

      Download citation file:


      © ARVO (1962-2015); The Authors (2016-present)

      ×
  • Supplements
Abstract

Purpose: Proliferative vitreoretinopathy (PVR) is a blinding disorder that results as a consequence of aberrant wound healing following a retinal tear or detachment. Although activation of the retinal pigmented epithelium (RPE) has been implicated in PVR, the mechanisms leading to enhanced proliferation, migration and contraction of RPE cells remains largely unknown. This study utilized an in vitro model of PVR to investigate the role of acetylation in the activation of RPE and its contribution to the progression of this disease.

Methods: ARPE19 and induced pluripotent stem cell-derived RPE (iPS-RPE) were cultured as previously described (Muniz A, et al., IVOS 2013). Cells treated with the histone deacetylase (HDAC) inhibitor, Trichostatin A (TSA; 0.1μM) were assessed for contraction and migration via collagen contraction and scratch assays, respectively. Co-immunoprecipitation, Western blotting and immunofluorescence analysis was performed to assess α-smooth muscle actin, β-catenin and myosin IIa expression following TSA treatment alone or in the presence of histone acetyltransferase (HAT) inhibitors.

Results: TSA (0.1μM) significantly increased contraction of ARPE19 cells in collagen matrix alone and this effect was potentiated in the presence of TGFβ-2 (10ng/μL). Moreover, co-treatment with HAT inhibitors curcumin (5μM), garcinol (5μM) and plumbagin (1μM) attenuated TSA-mediated collagen contraction. Scratch assays to investigate the contribution of acetylation on wound healing revealed TSA did not affect iPS-RPE cell migration. Immunofluorescence analysis of TSA-treated iPS-RPE wounded monolayers revealed decreased α-smooth muscle actin expression and reduced β-catenin at the plasma membrane as compared to control.

Conclusions: Our findings indicate a role of acetylation in the activation of RPE. Specifically, the HDAC inhibitor TSA enhanced RPE cell contraction and induced β-catenin translocation to the nucleus, indicating epithelial-mesenchymal transition (EMT) activation. Further investigation of pharmacological compounds that modulate acetylation may hold potential as therapeutic agents for the treatment of PVR.

×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×