Cited by 127Redox biology and oxidative stressSulfur Compounds in BiologyAntioxidant Activity and Oxidative Stress

Implications of plasma thiol redox in disease

Oliveira, Percíllia V.S., Laurindo, Francisco R.M.·2018·Clinical Science

Abstract

Thiol groups are crucially involved in signaling/homeostasis through oxidation, reduction, and disulphide exchange. The overall thiol pool is the resultant of several individual pools of small compounds (e.g. cysteine), peptides (e.g. glutathione), and thiol proteins (e.g. thioredoxin (Trx)), which are not in equilibrium and present specific oxidized/reduced ratios. This review addresses mechanisms and implications of circulating plasma thiol/disulphide redox pools, which are involved in several physiologic processes and explored as disease biomarkers. Thiol pools are regulated by mechanisms linked to their intrinsic reactivity against oxidants, concentration of antioxidants, thiol-disulphide exchange rates, and their dynamic release/removal from plasma. Major thiol couples determining plasma redox potential ( E h ) are reduced cysteine (CyS)/cystine (the disulphide form of cysteine) (CySS), followed by GSH/disulphide-oxidized glutathione (GSSG). Hydrogen peroxide and hypohalous acids are the main plasma oxidants, while water-soluble and lipid-soluble small molecules are the main antioxidants. The thiol proteome and thiol-oxidoreductases are emerging investigative areas given their specific disease-related responses (e.g. protein disulphide isomerases (PDIs) in thrombosis). Plasma cysteine and glutathione redox couples exhibit pro-oxidant changes directly correlated with ageing/age-related diseases. We further discuss changes in thiol-disulphide redox state in specific groups…

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Crossref · 10.1042/cs20180157

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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].”
  • A 2018 review by Oliveira and Laurindo highlights the association of changes in the thiolred/thiolox redox couple with aging and age-related disease, including cancer, CVD, and neurodegenerative disease.

    “The use of cysteine modifications as biomarkers of aging has not been investigated in recent years, but a review by Oliveira and Laurindo in 2018 highlights the association of changes in the thiolred/thiolox redox couple in aging and age-related disease, including cancer, CVD, and neurodegenerative disease [121].”

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Authors
Oliveira, P. V. S., & Laurindo, F. R. M.
Affiliations
Universidade de São Paulo (BR)
Venue
Clinical Science
Published
2018-06-29
Volume
132
Issue
12
Pages
1257-1280
ISSN
  • 0143-5221 (ISSN-L)
  • 1470-8736
OpenAlex
W2810242058
Cited by
127
References
284
Citations by year
2026: 11 · 2025: 8 · 2024: 15 · 2023: 17 · 2022: 17 · 2021: 19 · 2020: 24 · 2019: 11 · 2018: 4
FWCI
1.42
Type
journal article
Language
en
Open access
closed
Locations
  • Clinical Science (publishedVersion)
  • PubMed (publishedVersion)
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
  • Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Keywords
thiol-disulfide exchange, cysteine, glutathione, glutathione disulfide, thioredoxin, protein disulfide isomerase, oxidative stress, disease biomarkers, antioxidants, hydrogen peroxide, hypohalous acids, thiol oxidoreductase, atherosclerosis, cardiovascular disease, cancer, neurodegenerative diseases, aging, thrombosis
MeSH terms
Antioxidants, Cardiovascular Diseases, Humans, Neoplasms, Oxidation-Reduction, Sulfhydryl Compounds, Biomarkers, Oxidants, Oxidative Stress, S-Nitrosothiols

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