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Cited by 384Redox biology and oxidative stressSulfur Compounds in BiologyAldose Reductase and Taurine

Regulation of cell function by methionine oxidation and reduction

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Hoshi, Toshinori, Heinemann, Stefan H.·2001·The Journal of Physiology
DOI 10.1111/j.1469-7793.2001.0001j.xPMC PMC2278441
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Abstract

Reactive oxygen species (ROS) are generated during normal cellular activity and may exist in excess in some pathophysiological conditions, such as inflammation or reperfusion injury. These molecules oxidize a variety of cellular constituents, but sulfur‐containing amino acid residues are especially susceptible. While reversible cysteine oxidation and reduction is part of well‐established signalling systems, the oxidation and the enzymatically catalysed reduction of methionine is just emerging as a novel molecular mechanism for cellular regulation. Here we discuss how the oxidation of methionine to methionine sulfoxide in signalling proteins such as ion channels affects the function of these target proteins. Methionine sulfoxide reductase, which reduces methionine sulfoxide to methionine in a thioredoxin‐dependent manner, is therefore not only an enzyme important for the repair of age‐ or degenerative disease‐related protein modifications. It is also a potential missing link in the post‐translational modification cycle involved in the specific oxidation and reduction of methionine residues in cellular signalling proteins, which may give rise to activity‐dependent plastic changes in cellular excitability.

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  • Oxidation of methionine is a two-step process, in which the methionine residue is first oxidised to the sulfoxide and then irreversibly oxidised to the sulfone.

    “Oxidation of methionine is a two-step process, in which the methionine residue is first oxidised to the sulfoxide and then irreversibly oxidised to the sulfone [30].”

    From Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase (2021) · cites this paper as [30]

    The passage labeled Abstract (page unavailable) describes oxidation of methionine to methionine sulfoxide, followed by further oxidation to methionine sulfone in the presence of a strong oxidant. It does not say that the second step is irreversible, and the claim omits the strong-oxidant condition. (LLM, conf=0.84)

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Cited by

Sorted by citations

Authors
Hoshi, T., & Heinemann, S. H.
Affiliations
  • University of Iowa (US)
  • Friedrich Schiller University Jena (DE)
Corresponding author
Heinemann, Stefan H.
ORCID
Venue
The Journal of Physiology
Publisher
Wiley
Published
2001-02
Volume
531
Issue
1
Pages
1-11
ISSN
  • 0022-3751 (ISSN-L)
  • 1469-7793
DOI
10.1111/j.1469-7793.2001.0001j.x
PMC
PMC2278441
OpenAlex
W2135110724
Cited by
384
References
2
Citations by year
2026: 7 · 2025: 12 · 2024: 19 · 2023: 16 · 2022: 16 · 2021: 17 · 2020: 14 · 2019: 19 · 2018: 14 · 2017: 14 · 2016: 14 · 2015: 15 · 2014: 10 · 2013: 28 · 2012: 23
FWCI
1.38
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations
  • The Journal of Physiology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Heart, Lung, and Blood Institute (HL-14388, P01HL014388, HL 64645)
  • National Institute of General Medical Sciences (R01GM057654, GM 57654)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
Keywords
methionine oxidation, methionine sulfoxide, methionine sulfoxide reductase, reactive oxygen species, cysteine oxidation, post-translational modification, ion channels, thioredoxin, protein oxidation, signal transduction, ischemia-reperfusion injury, inflammation, cell excitability
MeSH terms
Animals, Cell Physiological Phenomena, Humans, Methionine, Oxidation-Reduction, Reactive Oxygen Species

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