Identification of Cysteine, Methionine and Tryptophan Residues of Actin Oxidized In vivo during Oxidative Stress
Abstract
Increased levels of reactive oxygen species (ROS) cause oxidative stress and are believed to play a key role in the development of age-related diseases and mammalian aging in general by oxidizing proteins, lipids, and DNA. In this study, we have investigated the effects of ROS on actin in an established rat model of acute oxidative stress using short-term X-ray irradiation. Relative to the control, the actin functions studied in vitro were reduced for (i) actin polymerization to a minimum of 33% after 9 h and (ii) actin activated Mg(2+)-ATPase activity of myosin to 55% after 9 h. At 24 h, the activities had partially recovered to 64 and 80% of the control sample, respectively. The underlying oxidative modifications were also studied at the molecular level. The content of reactive carbonyl-groups increased 4-fold within the studied 24 h period. Among the five cysteine residues of actin, Cys(239) and Cys(259) were oxidized to sulfenic (Cys-SOH), sulfinic (Cys-SO(2)H), or sulfonic (Cys-SO(3)H) acids by increasing amounts over the time periods studied. The content of methionine sulfoxides also increased for 15 of the 16 methionine residues, with Met(44), Met(47), and Met(355) having the highest sulfoxide contents. Met(82) was also further oxidized to the sulfone. Among the four tryptophan residues present in actin, only Trp(79) and Trp(86) appeared to undergo oxidation. The relative contents of hydroxy-tryptophan, N-formyl-kynurenine, and kynurenine increased after irradiation, r…
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A mouse model of radiation-induced oxidative stress shows that methionine residues can oxidise to the sulfone in vivo.
“a mouse model of radiation-induced oxidative stress [37] shows that it is certainly possible for methionine residues to oxidise to the sulfone in vivo.”
From Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase (2021) · cites this paper as [37]
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References 55 · Cited by 65
- Authors
- Fedorova, M., Kuleva, N., & Hoffmann, R.
- Affiliations
- St Petersburg University (RU)
- Institute of Bioanalytical Chemistry, Center for Biotechnology and Biomedicine, Faculty of Chemistry and Mineralogy, Leipzig University, Deutscher Platz 5, 04103 Leipzig, Germany, and Department of Biochemistry, Faculty of Biology and Soil Science, St. Petersburg State University, Universitetskaya nab. 7/9, 199034 St. Petersburg, Russia
- Corresponding author
- Hoffmann, Ralf
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-01-28
- Volume
- 9
- Issue
- 3
- Pages
- 1598-1609
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W1965310997
- Cited by
- 65
- References
- 55
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 5 · 2023: 2 · 2022: 4 · 2021: 4 · 2020: 4 · 2019: 2 · 2018: 5 · 2017: 4 · 2016: 4 · 2015: 3 · 2014: 2 · 2013: 9 · 2012: 7
- FWCI
- 2.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Proteome Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Keywords
- actin oxidation, oxidative stress, reactive oxygen species, X-ray irradiation, cysteine oxidation, methionine sulfoxide, tryptophan oxidation, sulfenic acid, sulfonic acids, methionine sulfone, kynurenine, actin polymerization, protein carbonylation
- MeSH terms
- Actins, Amino Acid Sequence, Animals, Cysteine, Male, Methionine, Molecular Sequence Data, Peptide Fragments, Rabbits, Trypsin, Tryptophan, X-Rays, Rats, Wistar, Reactive Oxygen Species, Oxidative Stress, Muscle, Skeletal, Protein Carbonylation, Rats, Tandem Mass Spectrometry
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