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Cys34-Cysteinylated Human Serum Albumin Is a Sensitive Plasma Marker in Oxidative Stress-Related Chronic Diseases
Open accessAbstract
The degree of oxidized cysteine (Cys) 34 in human serum albumin (HSA), as determined by high performance liquid chromatography (HPLC), is correlated with oxidative stress related pathological conditions. In order to further characterize the oxidation of Cys34-HSA at the molecular level and to develop a suitable analytical method for a rapid and sensitive clinical laboratory analysis, the use of electrospray ionization time-of-flight mass spectrometer (ESI-TOFMS) was evaluated. A marked increase in the cysteinylation of Cys34 occurs in chronic liver and kidney diseases and diabetes mellitus. A significant positive correlation was observed between the Cys-Cys34-HSA fraction of plasma samples obtained from 229 patients, as determined by ESI-TOFMS, and the degree of oxidized Cys34-HSA determined by HPLC. The Cys-Cys34-HSA fraction was significantly increased with the progression of liver cirrhosis, and was reduced by branched chain amino acids (BCAA) treatment. The changes in the Cys-Cys34-HSA fraction were significantly correlated with the alternations of the plasma levels of advanced oxidized protein products, an oxidative stress marker for proteins. The binding ability of endogenous substances (bilirubin and tryptophan) and drugs (warfarin and diazepam) to HSA purified from chronic liver disease patients were significantly suppressed but significantly improved by BCAA supplementation. Interestingly, the changes in this physiological function of HSA in chronic liver disease were correlated with the Cys-Cys34-HSA fraction. In conclusion, ESI-TOFMS is a suitable high throughput method for the rapid and sensitive quantification of Cys-Cys34-HSA in a large number of samples for evaluating oxidative stress related chronic disease progression or in response to a treatment.
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“Elevated levels of cysteinylated albumin detected by MS have been associated with kidney diseases and diabetes, and in addition, hepatic diseases (Nagumo et al. 2014).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Nagumo et al. 2014
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Diagnosis and Classification of Diabetes Mellitus
American Diabetes Association (2010) · Diabetes Care · doi:10.2337/dc11-s062 · Cited by 14,094
Diagnosis and classification of diabetes mellitus
American Diabetes Association (2013) · Diabetes Care · doi:10.2337/dc13-s067 · Cited by 2,245
Advanced oxidation protein products as a novel marker of oxidative stress in uremia
Witko‐Sarsat, V., Friedlander, M. A., Capeillère‐Blandin, C., Nguyen‐Khoa, T., Nguyen, A., Zingraff, J., Jungers, P., & Descamps‐Latscha, B. (1996) · Kidney International · doi:10.1038/ki.1996.186 · Cited by 2,000
Bardoxolone Methyl and Kidney Function in CKD with Type 2 Diabetes
Pergola, P. E., Raskin, P., Toto, R. D., Meyer, C. J., Huff, J. W., Grossman, E. B., Krauth, M., Ruiz, S., Audhya, P., Christ-Schmidt, H., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1105351 · Cited by 890
Pathogenesis of liver fibrosis: role of oxidative stress
Poli, G. (2000) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(00)00004-2 · Cited by 633
Albumin–drug interaction and its clinical implication
Yamasaki, K., Chuang, V. T. G., Maruyama, T., & Otagiri, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.005 · Cited by 464
Self-citationOettl, K., & Stauber, R. E. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707251 · Cited by 359
Branched-chain amino acids as pharmacological nutrients in chronic liver disease
Kawaguchi, T., Izumi, N., Charlton, M., & Sata, M. (2011) · Hepatology · doi:10.1002/hep.24412 · Cited by 333
Sulfenic Acid Formation in Human Serum Albumin by Hydrogen Peroxide and Peroxynitrite
Carballal, S., Radí, R., KIRK, M. C., Barnes, S., Freeman, B. Α., & Álvarez, B. (2003) · Biochemistry · doi:10.1021/bi027434m · Cited by 312
Redox properties of serum albumin
Anraku, M., Chuang, V. T. G., Maruyama, T., & Otagiri, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.036 · Cited by 258
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Batalova, A. A., Samodurova, K. V., Vovk, M. A., Belinskaia, D. A., Jenkins, R. O., & Goncharov, N. V. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27219687
Metadata
- Authors
- Nagumo, K., Tanaka, M., Chuang, V. T. G., Setoyama, H., Watanabe, H., Yamada, N., Kubota, K., Tanaka, M., Matsushita, K., Yoshida, A., Jinnouchi, H., Anraku, M., Kadowaki, D., Ishima, Y., Sasaki, Y., Otagiri, M., & Maruyama, T.
- Affiliations
- Kumamoto University (JP)
- Akebono Clinic (JP)
- Curtin University (AU)
- Ajinomoto (Japan) (JP)
- Sojo University (JP)
- Corresponding author
- Maruyama, Toru
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2014-01-08
- Volume
- 9
- Issue
- 1
- Pages
- e85216
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3885702
- OpenAlex
- W2031985670
- Cited by
- 201
- References
- 41
- Citations by year
- 2026: 13 · 2025: 10 · 2024: 13 · 2023: 17 · 2022: 19 · 2021: 29 · 2020: 22 · 2019: 18 · 2018: 15 · 2017: 14 · 2016: 15 · 2015: 12 · 2014: 4
- FWCI
- 6.15
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eSpace (Curtin University) (submittedVersion, cc-by)
- Funders
- Japan Society for the Promotion of Science (23790211, 25460190)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- human serum albumin, oxidative stress, plasma biomarkers, chronic liver disease, liver cirrhosis, branched-chain amino acids, drug binding, warfarin, diazepam, bilirubin, tryptophan, diabetes mellitus, chronic kidney disease
- MeSH terms
- Aged, Amino Acids, Branched-Chain, Bilirubin, Chronic Disease, Cysteine, Diabetes Mellitus, Diazepam, Female, Humans, Liver Cirrhosis, Male, Middle Aged, Models, Molecular, Oxidation-Reduction, Protein Binding, Serum Albumin, Tryptophan, Warfarin, Biomarkers, Glycation End Products, Advanced, Oxidative Stress, Spectrometry, Mass, Electrospray Ionization, Renal Insufficiency
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