ArticleJournal of proteome research2021
Identification and Quantification of Glutathionylated Cysteines under Ischemic Stress.
Article in Journal of proteome research, 2021. 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, 9 citations in OpenAlex.
- ARHGEF7 S-glutathionylation promotes cancer cell migration through Rac1 activation.bioRxiv : the preprint server for biology · 2026Article
- Redox regulation of cell migration via Nischarin S-glutathionylation.Free radical biology & medicine · 2026Article
- Redox Regulation of Cell Migration via Nischarin S-glutathionylation.bioRxiv : the preprint server for biology · 2025Article
- Protein phosphatase PP2Cα S-glutathionylation regulates cell migration.The Journal of biological chemistry · 2024Article
- Chemoproteomic strategy identified p120-catenin glutathionylation regulates E-cadherin degradation and cell migration.Cell chemical biology · 2023Article
- Clickable Glutathione-Based Identification of Cysteine Glutathionylation.Current protocols · 2023Article
- Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue.Antioxidants (Basel, Switzerland) · 2023Article
- Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022Review
- Regulation of Retroviral and SARS-CoV-2 Protease Dimerization and Activity through Reversible Oxidation.Antioxidants (Basel, Switzerland) · 2022Review
- Human Umbilical Vein Endothelial Cells Survive on the Ischemic TCA Cycle under Lethal Ischemic Conditions.Journal of proteome research · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ischemia reperfusion injury contributes to adverse cardiovascular diseases in part by producing a burst of reactive oxygen species that induce oxidations of many muscular proteins. Glutathionylation is one of the major protein cysteine oxidations that often serve as molecular mechanisms behind the pathophysiology associated with ischemic stress. Despite the biological significance of glutathionylation in ischemia reperfusion, identification of specific glutathionylated cysteines under ischemic stress has been limited. In this report, we have analyzed glutathionylation under oxygen-glucose deprivation (OGD) or repletion of nutrients after OGD (OGD/R) by using a clickable glutathione approach that specifically detects glutathionylated proteins. Our data find that palmitate availability induces a global level of glutathionylation and decreases cell viability during OGD/R. We have then applied a clickable glutathione-based proteomic quantification strategy, which enabled the identification and quantification of 249 glutathionylated cysteines in response to palmitate during OGD/R in the HL-1 cardiomyocyte cell line. The subsequent bioinformatic analysis found 18 glutathionylated cysteines whose genetic variants are associated with muscular disorders. Overall, our data report glutathionylated cysteines under ischemic stress that may contribute to adverse outcomes or muscular disorders.
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