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Cited by 356Sulfur Compounds in BiologyRedox biology and oxidative stressAmino Acid Enzymes and Metabolism

Cysteine Metabolism in Neuronal Redox Homeostasis

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Paul, Bindu D., Sbodio, Juan I., Snyder, Solomon H.·2018·Trends in Pharmacological Sciences
DOI 10.1016/j.tips.2018.02.007PMC PMC5912966
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Abstract

Besides its essential role in protein synthesis, cysteine plays vital roles in redox homeostasis, being a component of the major antioxidant glutathione (GSH) and a potent antioxidant by itself. In addition, cysteine undergoes a variety of post-translational modifications that modulate several physiological processes. It is becoming increasingly clear that redox-modulated events play important roles not only in peripheral tissues but also in the brain where cysteine disposition is central to these pathways. Dysregulated cysteine metabolism is associated with several neurodegenerative disorders. Accordingly, restoration of cysteine balance has therapeutic benefits. This review discusses metabolic signaling pathways pertaining to cysteine disposition in the brain under normal and pathological conditions, highlighting recent findings on cysteine metabolism during aging and in neurodegenerative conditions such as Huntington's disease (HD) and molybdenum cofactor (MoCo) deficiency (MoCD) among others.

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  • Cysteine and its oxidized forms, such as cystine and further cysteine disulfide species, are considered potential biomarkers of protein oxidation in human disease.

    “Thus, cysteine and its oxidized forms, such as cystine and further cysteine disulfide species, are considered as potential biomarkers of protein oxidation in human disease [120,121].”

    From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [120]

    The 'Cysteine and redox homeostasis' section (page unavailable) says cysteine is readily oxidized to cystine and describes oxidation of cysteine residues. The paper does not identify cysteine, cystine, or other cysteine disulfides as potential biomarkers of protein oxidation in human disease. (LLM, conf=0.82)

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Cited by

Sorted by citations

Authors
Paul, B. D., Sbodio, J. I., & Snyder, S. H.
Affiliations
Johns Hopkins University (US)
Corresponding author
  • Paul, Bindu D.
  • Snyder, Solomon H.
ORCID
Venue
Trends in Pharmacological Sciences
Publisher
Elsevier BV
Published
2018-05
Volume
39
Issue
5
Pages
513-524
ISSN
0165-6147 (ISSN-L)
DOI
10.1016/j.tips.2018.02.007
PMC
PMC5912966
OpenAlex
W2793610547
Cited by
356
References
10
Citations by year
2026: 46 · 2025: 59 · 2024: 59 · 2023: 49 · 2022: 41 · 2021: 41 · 2020: 39 · 2019: 18 · 2018: 4
FWCI
2.54
Type
journal article
Language
en
Open access
Licence
Locations
  • Trends in Pharmacological Sciences (acceptedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of Mental Health (R01MH018501)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords
cysteine metabolism, glutathione, cysteine post-translational modification, neurodegenerative diseases, aging, Huntington's disease, molybdenum cofactor deficiency, antioxidant metabolism
MeSH terms
Animals, Autophagy, Cysteine, Glutathione, Homeostasis, Humans, Neurons, Oxidation-Reduction, Protein Processing, Post-Translational, Neurodegenerative Diseases

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