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• W1275631870 abstract "Purpose: Oxidative stress contributes to retinal light damage but the molecular mechanisms remain poorly understood. As part of ongoing efforts to better understand the role of protein oxidative modifications in retinal pathology, protein nitration in retina has been compared between rats exposed to damaging light or maintained in the dark. Methods: Albino rats maintained in a dark environment for 2-4 month were exposed to intense green light (1500 lux) for 3 hours and sacrificed immediately following light treatment. Proteomic and immunohistochemical analyses have been used to identify nitrated retinal proteins and their localization within the layers and cell types of the retina before and after light exposure. Results: Methodology for detecting nitrotyrosine containing proteins by Western analysis has been improved by incorporating chemical reduction of nitrotyrosine to aminotyrosine, allowing specific and nonspecific anti-nitrotyrosine antibody reactivity to be distinguished. Using 2D gel electrophoresis, Western and mass spectrometric analyses, several different nitrotyrosine immunoreactive proteins were identified in light exposed retina compared with those maintained in the dark. Immunocytochemical analyses of retina revealed that rats reared in darkness exhibited more nitrotyrosine immunoreactivity in the photoreceptor outer segments. After intense light exposure, immunoreactivity decreased in the outer segments and increased in the photoreceptor inner segments and retinal pigment epithelium. Conclusion: Light modulates retinal protein nitration in vivo. The present findings justify further consideration of nitration and nitric oxide as possible mediators in the light-induced biochemical sequela leading to photoreceptor cell death. CR: N. Supported in part by NIH grants EY06603, NS41644, EY01959, a Research Center Grant from The Foundation Fighting Blindness, and funds from the Cleveland Clinic Foundation. Summary and Conclusions 1. A LC MS/MS detection strategy was used that selects all possible nitrotyrosine peptides for MS/MS based on knowing the protein identity. Quantitative LC MS/MS analyses with tetranitromethane modified albumin demonstrated this approach capable of identifying sites of tyrosine nitration with detection limits of 4-33 fmol. 2. Reduction of nitrotyrosine to aminotyrosine with dithionite appears useful for distingusihing specific and non-specifiic recognition by anti-nitrotyrosine antibody in 2D Western analyses. 3. Using 2D gel electrophoresis, Western detection and mass spectrometric analyses, several different nitrotyrosine immunoreactive proteins were identified in light exposed rat retina compared with those maintained in the dark. 4. Immunocytochemical analyses of retina revealed that rats reared in darkness exhibited more nitrotyrosine immunoreactivity in the photoreceptor outer segments. After intense light exposure, immunoreactivity decreased in the outer segments and increased in the photoreceptor inner segments and retinal pigment epithelium. 5. These results suggest that light modulates retinal protein nitration in vivo and that nitration may participate in the biochemical sequela leading to light induced photoreceptor cell death. Furthermore, the identification of nitrotyrosine containing proteins from rats maintained in the dark, under non pathological conditions provides the first evidence of a possible role for protein nitration in normal retinal physiology. 6. Enrichment methods and/or higher senstivity will be needed to identify nitration sites in in vivo samples." @default.
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• W1275631870 date "2002-12-01" @default.
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• W1275631870 title "Protein Nitration in Rat Retina Before and After Light Damage" @default.
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