ArticleThe Journal of biological chemistry2008
Mammals reduce methionine-S-sulfoxide with MsrA and are unable to reduce methionine-R-sulfoxide, and this function can be restored with a yeast reductase.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- Site-specific methionine oxidation alters structure and phase separation of TDP-43 C-terminal domain.bioRxiv : the preprint server for biology · 2025Article
- Response to oxidative stress of AML12 hepatocyte cells with knockout of methionine sulfoxide reductases.Free radical biology & medicine · 2023Article
- The Potential of a Protein Model Synthesized Absent of Methionine.Molecules (Basel, Switzerland) · 2022Review
- TRPV2: A Key Player in Myelination Disorders of the Central Nervous System.International journal of molecular sciences · 2022Article
- Selenomethionine: A Pink Trojan Redox Horse with Implications in Aging and Various Age-Related Diseases.Antioxidants (Basel, Switzerland) · 2021Review
- X-ray absorption spectroscopy of organic sulfoxides.RSC advances · 2020Article
- Function of the evolutionarily conserved plant methionine-S-sulfoxide reductase without the catalytic residue.Protoplasma · 2018Article
- Myeloperoxidase oxidation of methionine associates with early cystic fibrosis lung disease.The European respiratory journal · 2018Observational
- Expression of the methionine sulfoxide reductase lost during evolution extends Drosophila lifespan in a methionine-dependent manner.Scientific reports · 2018Article
- Monitoring of Methionine Sulfoxide Content and Methionine Sulfoxide Reductase Activity.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Practical guide for dynamic monitoring of protein oxidation using genetically encoded ratiometric fluorescent biosensors of methionine sulfoxide.Methods (San Diego, Calif.) · 2016Review
- Selenoprotein H is an essential regulator of redox homeostasis that cooperates with p53 in development and tumorigenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1.Antioxidants & redox signaling · 2015Review
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
- Methionine restriction extends lifespan of Drosophila melanogaster under conditions of low amino-acid status.Nature communications · 2014Article
- Article
- Diversity of plant methionine sulfoxide reductases B and evolution of a form specific for free methionine sulfoxide.PloS one · 2013Article
- Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding.The Journal of biological chemistry · 2012Article
- Oxidative stress and diabetes: what can we learn about insulin resistance from antioxidant mutant mouse models?Free radical biology & medicine · 2012Review
- Selective reduction of methylsulfinyl-containing compounds by mammalian MsrA suggests a strategy for improved drug efficacy.ACS chemical biology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Methionine is an essential amino acid in mammals at the junction of methylation, protein synthesis, and sulfur pathways. However, this amino acid is highly susceptible to oxidation, resulting in a mixture of methionine-S-sulfoxide and methionine-R-sulfoxide. Whether methionine is quantitatively regenerated from these compounds is unknown. Here we report that SK-Hep1 hepatocytes grew on methionine-S-sulfoxide and consumed this compound by import and methionine-S-sulfoxide reductase (MsrA)-dependent reduction, but methionine-R-sulfoxide reductases were not involved in this process, and methionine-R-sulfoxide could not be used by the cells. However, SK-Hep1 cells expressing a yeast free methionine-R-sulfoxide reductase proliferated in the presence of either sulfoxide, reduced them, and showed increased resistance to oxidative stress. Only methionine-R-sulfoxide was detected in the plasma of wild type mice, but both sulfoxides were in the plasma of MsrA knock-out mice. These results show that mammals can support methionine metabolism by reduction of methionine-S-sulfoxide, that this process is dependent on MsrA, that mammals are inherently deficient in the reduction of methionine-R-sulfoxide, and that expression of yeast free methionine-R-sulfoxide reductase can fully compensate for this deficiency.
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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.