Protein oxidation: role in signalling and detection by mass spectrometry
Abstract
Proteins can undergo a wide variety of oxidative post-translational modifications (oxPTM); while reversible modifications are thought to be relevant in physiological processes, non-reversible oxPTM may contribute to pathological situations and disease. The oxidant is also important in determining the type of oxPTM, such as oxidation, chlorination or nitration. The best characterized oxPTMs involved in signalling modulation are partial oxidations of cysteine to disulfide, glutathionylated or sulfenic acid forms that can be reversed by thiol reductants. Proline hydroxylation in HIF signalling is also quite well characterized, and there is increasing evidence that specific oxidations of methionine and tyrosine may have some biological roles. For some proteins regulated by cysteine oxidation, the residues and molecular mechanism involved have been extensively studied and are well understood, such as the protein tyrosine phosphatase PTP1B and MAP3 kinase ASK1, as well as transcription factor complex Keap1-Nrf2. The advances in understanding of the role oxPTMs in signalling have been facilitated by advances in analytical technology, in particular tandem mass spectrometry techniques. Combinations of peptide sequencing by collisionally induced dissociation and precursor ion scanning or neutral loss to select for specific oxPTMs have proved very useful for identifying oxidatively modified proteins and mapping the sites of oxidation. The development of specific labelling and enrichment…
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Reversible protein modifications are relevant in physiological processes and constitute signaling mechanisms (redox signaling), while non-reversible modifications may contribute to pathological situations and several diseases.
“Reversible modifications are relevant in physiological processes and constitute signaling mechanisms (“redox signaling”), while non-reversible modifications may contribute to pathological situations and several diseases.”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [9]
Cites
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Yang, H., Lundbäck, P., Ottosson, L., Erlandsson-Harris, H., Venereau, E., Bianchi, M. E., Al-Abed, Y., Andersson, U., Tracey, K. J., & Antoine, D. J. (2012) · Molecular Medicine · doi:10.2119/molmed.2011.00389 · Cited by 407 · see citing works
RetractedProtein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
“It has been established that reversible modifications are thought to be relevant in physiological processes and constitute signaling mechanisms under appropriate conditions (“redox signaling”), while non-reversible modifications may contribute to pathological situations and several diseases [9].”
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- Authors
- Spickett, C. M., & Pitt, A. R.
- Affiliations
- University of Strathclyde (GB)
- University of Glasgow (GB)
- Corresponding author
- Spickett, Corinne M.
- Venue
- Amino Acids
- Published
- 2010-04-18
- Volume
- 42
- Issue
- 1
- Pages
- 5-21
- ISSN
- 0939-4451 (ISSN-L)
- 1438-2199
- OpenAlex
- W2059072962
- Cited by
- 65
- References
- 9
- Citations by year
- 2025: 1 · 2024: 7 · 2023: 2 · 2022: 3 · 2021: 5 · 2020: 4 · 2019: 3 · 2018: 2 · 2016: 4 · 2015: 8 · 2014: 4 · 2013: 11 · 2012: 7
- FWCI
- 0.62
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Amino Acids (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council (BB/E015727/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- protein oxidation, oxidative post-translational modifications, cysteine oxidation, disulfide bond formation, sulfenic acid, glutathionylation, proline hydroxylation, methionine oxidation, tyrosine nitration, nitrotyrosine, S-nitrosylation, PTP1B, ASK1, MAP3K, collision-induced dissociation, neutral loss scanning, tandem mass spectrometry
- MeSH terms
- Humans, Oxidation-Reduction, Proteins, Mass Spectrometry, Signal Transduction
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