ArticleExperimental eye research2018
Quantification of thioether-linked glutathione modifications in human lens proteins.
Article in Experimental eye research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Lens aging and disease: Molecular mechanisms, functional consequences, and pharmacological implications.Progress in retinal and eye research · 2026Review
- Data-Independent Acquisition Parallel Accumulation-Serial Fragmentation (diaPASEF) Analysis of the Separated Zebrafish Lens Improves Identifications.Journal of the American Society for Mass Spectrometry · 2025Article
- Oxidation-Induced Mixed Disulfide and Cataract Formation: A Review.Antioxidants (Basel, Switzerland) · 2025Review
- Dehydroamino acids and their crosslinks in Alzheimer's disease aggregates.Brain communications · 2025Article
- Spatially Resolved Proteomics Reveals Lens Suture-Related Cell-Cell Junctional Protein Distributions.Investigative ophthalmology & visual science · 2023Article
- Dehydroalanine and dehydrobutyrine in aging and cataractous lenses reveal site-specific consequences of spontaneous protein degradation.Frontiers in ophthalmology · 2023Article
- Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022Review
- Discovery of Dehydroamino Acid Residues in the Capsid and Matrix Structural Proteins of HIV-1.Journal of proteome research · 2022Article
- Spontaneous Cleavage at Glu and Gln Residues in Long-Lived Proteins.ACS chemical biology · 2021Article
- New insights into the mechanisms of age-related protein-protein crosslinking in the human lens.Experimental eye research · 2021Review
- Spontaneous protein-protein crosslinking at glutamine and glutamic acid residues in long-lived proteins.The Biochemical journal · 2021Article
- Dehydroamino acid chemical biology: an example of functional group interconversion on proteins.RSC chemical biology · 2020Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Molecular Processes Implicated in Human Age-Related Nuclear Cataract.Investigative ophthalmology & visual science · 2019Review
- Cleavage C-terminal to Asp leads to covalent crosslinking of long-lived human proteins.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- γ-Crystallin redox-detox in the lens.The Journal of biological chemistry · 2018Article
- Spontaneous cross-linking of proteins at aspartate and asparagine residues is mediated via a succinimide intermediate.The Biochemical journal · 2018Article
Corrections and comments
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2 authors.
Funding
Abstract
Dehydroalanine (DHA) and dehydrobutyrine (DHB) intermediates, formed through β-elimination, induce protein irreversible glutathionylation and protein-protein crosslinking in human lens fiber cells. In total, irreversible glutathionylation was detected on 52 sites including cysteine, serine and threonine residues in 18 proteins in human lenses. In this study, the levels of GSH modification on three serine residues and four cysteine residues located in seven different lens proteins isolated from different regions and different aged lenses were quantified. The relative levels of modification (modified/nonmodified) were site-specific and age-related, ranging from less than 0.05% to about 500%. The levels of modification on all of the sites quantified in the lens cortex increased with age and GSH modification also increased from cortex to outer nucleus region suggesting an age-related increase of modification. The levels of modification on sites located in stable regions of the proteins such as Cys117 of βA3, Cys80 of βB1 and Cys27 of γS, continued increasing in inner nucleus, but modification on sites located in regions undergoing degradation with age decreased in the inner nucleus suggesting GSH modified proteins were more susceptible to further modification. Irreversible GSH modification in cataract lenses was typically higher than in age-matched normal lenses, but the difference did not reach statistical significance for a majority of sites, with the exception Cys117 of βA3 crystallin in WSF. Except for S59 of αA and αB crystallins, GSH modification did not induce protein insolubility suggesting a possible role for this modification in protection from protein-protein crosslinking.
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