A simple method to systematically study oxidatively modified proteins in biological samples and its applications
Open accessAbstract
Increased oxidative stress with elevated levels of reactive oxygen/nitrogen species (ROS/RNS) plays an important role in the pathophysiology of many disease states. Increased ROS/RNS can modulate the cellular macromolecules of DNA, lipids, and proteins, negatively affecting their normal functions. Numerous reports have described the properties and implications of oxidized DNA and lipids. However, oxidative modifications of proteins were not fully studied partially due to the requirement for specific reagents, the lack of methods to detect, purify, and identify oxidatively modified proteins, and the relatively late development of highly sensitive analytical instruments. This chapter describes the detailed procedure for systematically identifying oxidative-modified proteins in biological samples. Applications and other suggestions to this method are also described to understand the functional roles of oxidatively modified proteins in promoting endoplasmic reticulum (ER) stress and mitochondrial dysfunction, which ultimately contribute to organ damage.
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The actual number of oxidized proteins could be significantly higher than originally reported because of technical limitations in identification, purification and detection, especially for low-abundance proteins.
“However, we believe that the actual number of oxidized proteins could be significantly higher than the proteins originally reported [34], [38], [39], because of the technical limitations in the identification and purification of oxidized proteins and detection methods, especially for those proteins expressed in low abundance, as previously discussed [26], [33].”
Cys residues in adducts with reactive metabolites or lipid peroxides cannot be restored even in the presence of a strong reducing agent DTT and are considered irreversible.
“However, Cys residues in the adducts with reactive metabolites or lipid peroxides cannot be restored even in the presence of a strong reducing agent DTT and thus are considered irreversible, as discussed [26], [33].”
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References 43 · Cited by 18
- Authors
- Song, B.-J., Suh, S.-K., & Moon, K.-H.
- Affiliations
- National Institute on Alcohol Abuse and Alcoholism (US)
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 2010
- Volume
- 473
- Pages
- 251-264
- ISSN
- 0076-6879 (ISSN-L)
- PMC
- PMC2880834
- OpenAlex
- W1820288222
- Cited by
- 18
- References
- 43
- Citations by year
- 2021: 1 · 2017: 2 · 2016: 2 · 2015: 3 · 2014: 2 · 2013: 3 · 2012: 2
- FWCI
- 3.09
- Type
- book chapter
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (Z99‐AA999999)
- National Institute on Alcohol Abuse and Alcoholism (ZIAAA000036)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- oxidized proteins, protein oxidation, reactive oxygen species, reactive nitrogen species, oxidative stress, protein identification, protein purification, endoplasmic reticulum stress, mitochondrial dysfunction, organ damage
- MeSH terms
- Animals, Cysteine, Humans, Models, Biological, Oxidation-Reduction, Protein Processing, Post-Translational, Proteins, Clinical Laboratory Techniques, Proteomics
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