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Di Ding, Mabel Enriquez Algeciras, Juan Torres, Vittorio Porciatti, Susan Udin, Sanjoy K Bhattacharya; Deimination is important for vision restoration in demyelinating diseases. Invest. Ophthalmol. Vis. Sci. 2016;57(12):2729.
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© ARVO (1962-2015); The Authors (2016-present)
To test deimination is important for general vision reorganization and for vision restoration in demyelinating diseases.
Animals used adhered to the ARVO statement for utilization of animals in vision research. Deimination refers to the post-translational modification of protein-bound arginine into citrulline catalyzed by peptidylarginine deiminases (PADs). The deimination level and neuronal growth has been examined in different model systems (frog optic tectum of eye rotation (n=4), a transgenic mouse model of multiple sclerosis ND4-SLICK hybrid (n=6), and neurons) using various techniques such as immunohistochemistry, mass spectrometry, and Western blot analysis. Neuron lysates from mice were subjected to immunoprecipitation (IP) using anti-PAD2 antibody, a major deiminase in the nervous system. Proteins that associate with translational systems in neurons were identified by mass spectrometry. Visual function after PAD2 overexpression was evaluated using pattern electroretinogram (PERG) and compared to the controls. All experiments were repeated three times and results were shown as mean ± SD.
We found increased deimination levels in rotated frog optic tectum during visual reorganization and neuronal outgrowth. PAD2 are associated with multiple factors that are components of RNA granules. The upregulation of PAD2 in vivo can increase protein synthesis and PERG amplitude in ND4-SLICK mice.
Deimination restores protein synthesis in degenerated neurons and is important for neuronal outgrowth. Therefore, deimination is a potential regulator for restoring vision function in demyelinating disease.
This is an abstract that was submitted for the 2016 ARVO Annual Meeting, held in Seattle, Wash., May 1-5, 2016.
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