ArticleInvestigative ophthalmology & visual science2012
Redox proteomic identification of visual arrestin dimerization in photoreceptor degeneration after photic injury.
Article in Investigative ophthalmology & visual science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Mass spectrometry-based retina proteomics.Mass spectrometry reviews · 2023Review
- Disulfide Dimerization of Neuronal Calcium Sensor-1: Implications for Zinc and Redox Signaling.International journal of molecular sciences · 2021Article
- Rational Design of "Three-in-One" Ratiometric Nanoprobes: Protein-Caged Dityrosine, CdS Quantum Dots, and Gold Nanoclusters.ACS omega · 2020Article
- Suppression of Light-Induced Oxidative Stress in the Retina by Mitochondria-Targeted Antioxidant.Antioxidants (Basel, Switzerland) · 2018Article
- Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization.Frontiers in molecular neuroscience · 2018Article
- Borane-protected phosphines are redox-active radioprotective agents for endothelial cells.Redox biology · 2015Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
purposeLight-induced oxidative stress is an important risk factor for age-related macular degeneration, but the downstream mediators of photoreceptor and retinal pigment epithelium cell death after photic injury are unknown. Given our previous identification of sulfhydryl/disulfide redox status as a factor in photoreceptor survival, we hypothesized that formation of one or more disulfide-linked homo- or hetero-dimeric proteins might signal photoreceptor death after light-induced injury.
methodsTwo-dimensional (non-reducing/reducing) gel electrophoresis of Wistar rat retinal homogenates after 10 hours of 10,000 lux (4200°K) light in vivo, followed by mass spectrometry identification of differentially oxidized proteins.
resultsThe redox proteomic screen identified homodimers of visual arrestin (Arr1; S antigen) after toxic levels of light injury. Immunoblot analysis revealed a light duration-dependent formation of Arr1 homodimers, as well as other Arr1 oligomers. Immunoprecipitation studies revealed that the dimerization of Arr1 due to photic injury was distinct from association with its physiological binding partners, rhodopsin and enolase1. Systemic delivery of tris(2-carboxyethyl)phosphine, a specific disulfide reductant, both decreased Arr1 dimer formation and protected photoreceptors from light-induced degeneration in vivo.
conclusionsThese findings suggest a novel arrestin-associated pathway by which oxidative stress could result in cell death, and identify disulfide-dependent dimerization as a potential therapeutic target in retinal degeneration.
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