Proteomics of post-traumatic proliferative vitreoretinopathy in rabbit retina reveals alterations to a variety of functional proteins.

PURPOSE

The purpose of this study was to investigate the protein profiles and pathogenesis in rabbit retinas from normal and post-traumatic proliferative vitreoretinopathy (PVR).

MATERIALS AND METHODS

A modified rabbit model of post-traumatic PVR was modified used in the study. Two-dimensional gel electrophoresis (2-DE) coupled with mass spectrometry (MS) were utilized to identify the changes to the protein profiles of rabbit retina. The myosin light chains-2 (MLC2) was subsequently chosen as a target for its biggest difference in 2-DE gels using Western blot, immunohistochemistry and MTT assay.

RESULTS

Comparative gel analysis revealed that 20 spots were up-regulated or novel emerged and 12 were down-regulated or even disappeared in PVR retinas. The majority of changes could consist of the following functional groups of proteins including the cell skeleton proteins; the wound healing/cell adhesion proteins; the proteins involved in metabolism and in blood-retina barrier destruction; oxidative stress-related proteins and the ion channel proteins. Western blot analysis confirmed that MLC2 protein expression was upregulated in PVR retinas. MTT assay showed that the anti-MLC2 monoclonal antibody significantly decreased the proliferation in ARPE-19 cells stimulated with different concentrations and times in vitro experiment.

CONCLUSIONS

Our results suggested that PVR is a complicated pathology process with alterations in expression of a variety of functional proteins rather than a single key protein. The data reported may be useful for further studies on pathogenesis of human PVR and for the screening of biomarkers to develop new potential therapeutic approaches.