ArticleOxidative medicine and cellular longevity2016
Basal Glutathionylation of Na,K-ATPase α-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis.
Article in Oxidative medicine and cellular longevity, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- The Brain at High Altitude: From Molecular Signaling to Cognitive Performance.International journal of molecular sciences · 2023Review
- Recent Advances in the Study of NaCells · 2022Review
- S-glutathionylation, friend or foe in cardiovascular health and disease.Redox biology · 2020Review
- A novel approach for predicting protein S-glutathionylation.BMC bioinformatics · 2020Article
- Bioinformatics research at SBB-2019.BMC bioinformatics · 2020Article
- Overview on solubilization and lipid reconstitution of Na,K-ATPase: enzyme kinetic and biophysical characterization.Biophysical reviews · 2020Review
- Glutathione-related substances maintain cardiomyocyte contractile function in hypoxic conditions.Scientific reports · 2019Article
- RNases Disrupt the Adaptive Potential of Malignant Cells: Perspectives for Therapy.Frontiers in pharmacology · 2019Article
- Cysteine residues 244 and 458-459 within the catalytic subunit of Na,K-ATPase control the enzyme's hydrolytic and signaling function under hypoxic conditions.Redox biology · 2017Article
- Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity.Biomolecules · 2017Article
- "Oxygen Sensing" by Na,K-ATPase: These Miraculous Thiols.Frontiers in physiology · 2016Review
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7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many viruses induce oxidative stress and cause S-glutathionylation of Cys residues of the host and viral proteins. Changes in cell functioning during viral infection may be associated with glutathionylation of a number of key proteins including Na,K-ATPase which creates a gradient of sodium and potassium ions. It was found that Na,K-ATPase α-subunit has a basal glutathionylation which is not abrogated by reducing agent. We have shown that acute hypoxia leads to increase of total glutathionylation level of Na,K-ATPase α-subunit; however, basal glutathionylation of α-subunit increases under prolonged hypoxia only. The role of basal glutathionylation in Na,K-ATPase function remains unclear. Understanding significance of basal glutathionylation is complicated by the fact that there are no X-ray structures of Na,K-ATPase with the identified glutathione molecules. We have analyzed all X-ray structures of the Na,K-ATPase α-subunit from pig kidney and found that there are a number of isolated cavities with unresolved electron density close to the relevant cysteine residues. Analysis of the structures showed that this unresolved density in the structure can be occupied by glutathione associated with cysteine residues. Here, we discuss the role of basal glutathionylation of Na,K-ATPase α-subunit and provide evidence supporting the view that this modification is cotranslational.
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