ArticleMolecular vision2013
Cataract-specific posttranslational modifications and changes in the composition of urea-soluble protein fraction from the rat lens.
Article in Molecular vision, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Lysine Malonylation and Its Links to Metabolism and Diseases.Aging and disease · 2023Review
- Some Aspects of Development and Histological Structure of the Visual System of Nothobranchius Guentheri.Animals : an open access journal from MDPI · 2021Article
- Lysine malonylation and propionylation are prevalent in human lens proteins.Experimental eye research · 2020Article
- Mechanisms of Small Heat Shock Proteins.Cold Spring Harbor perspectives in biology · 2019Review
- Rosmarinic Acid Restores Complete Transparency of Sonicated Human Cataract Ex Vivo and Delays Cataract Formation In Vivo.Scientific reports · 2018Article
- Protein Posttranslational Modifications: Roles in Aging and Age-Related Disease.Oxidative medicine and cellular longevity · 2017Review
- Biophysical chemistry of the ageing eye lens.Biophysical reviews · 2015Review
- Oxidation as an important factor of protein damage: Implications for Maillard reaction.Journal of biosciences · 2015Review
- Ameliorative effects of SkQ1 eye drops on cataractogenesis in senescence-accelerated OXYS rats.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTo determine age-related changes in the composition of the urea-soluble (US) protein fraction from lenses of senescence-accelerated OXYS (cataract model) and Wistar (control) rats and to establish posttranslational modifications (PTMs) occurring under enhanced oxidative stress in OXYS lenses.
methodsThe identity and the relative abundance of crystallins in the US fractions were determined using two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption ionization-time of flight mass spectrometry (MS). The identities and the positions of PTMs were established using MS/MS measurements.
resultsTwo-dimensional gel electrophoresis maps of US protein fractions were obtained for lenses of 3-, 12-, and 62-week-old Wistar and OXYS rats, and the relative abundance of different isoforms of α-, β-, and γ-crystallins was determined. β-Crystallins were the major contributor of the US fraction in 3-week-old lenses (above 50%), γ-crystallins in 12-week-old lenses (50-60%), and in 62-week-old lenses, the contributions from all three crystallin families leveled out. The major interstrain difference was the elevated level of α-crystallins in the US fraction from 12-week-old OXYS lenses. Spots with increased relative abundance in OXYS maps were attributed to the cataract-specific spots of interest. The crystallins from these spots were subjected to MS/MS analysis, and the positions of acetylation, oxidation, deamidation, and phosphorylation were established.
conclusionsThe increased relative abundance of α-crystallins in the US fraction from 12-week-old OXYS lenses points to the fast insolubilization of α-crystallins under oxidative stress. Most of the PTMs attributed to the cataract-specific modifications also correspond to α-crystallins. These PTMs include oxidation of methionine residues, deamidation of asparagine and glutamine residues, and phosphorylation of serine and threonine residues.
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Identifiers
24227915PMC3820433W2112324286What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.