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Quantitative screening of protein biomarkers of early glycation, advanced glycation, oxidation and nitrosation in cellular and extracellular proteins by tandem mass spectrometry multiple reaction monitoring
Abstract
Glycation of proteins forms fructosamines and AGEs (advanced glycation end products). Oxidative and nitrosative stress leads to the formation of oxidative and nitrosative modifications. The modified amino acid residues formed in these processes are biomarkers of protein damage: some are risk markers and some may be risk factors for disease development. We developed a method for the concurrent quantitative measurement of 16 biomarkers indicative of protein glycation, oxidation and nitrosation damage using LC-MS/MS (LC with tandem MS detection). Underivatized analytes were detected free in physiological fluids and in enzymatic hydrolysates of cellular and extracellular proteins. Hydroimidazolones were the most important glycation biomarkers, and methionine sulphoxide was the most important oxidative biomarker quantitatively; 3-nitrotyrosine was the biomarker of nitrosation. Quantitative screening showed high levels of AGEs in cellular protein and moderate levels in protein of blood plasma. Levels of 3-nitrotyrosine were typically 100-fold lower than this. The major glycation adducts in blood plasma had high renal clearances in normal healthy human subjects, whereas methionine sulphoxide and 3-nitrotyrosine had low renal clearances due to further metabolism. Physiological AGEs in blood plasma were eliminated from the circulation in the kidney and not in the liver. LC-MS/MS peptide mapping was also used to locate the protein biomarkers. These studies reveal that advanced glycatio…
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“In contrast to the non-enzymatic oxidation of methionine to methionine sulfoxide, the reduction is catalyzed by methionine sulfoxide reductases [20]. Further oxidation results in methionine sulfone formation, which is not targeted by methionine sulfoxide reductases and has to be considered as a stable modification [21].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [21]
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Segovia, A. S. R., Wróbel, K., Aguilar, F. J. A., Escobosa, A. R. C., & Wróbel, K. (2016) · Metallomics · doi:10.1039/c6mt00235h · Cited by 14
Choe, I.-H., Jeon, H. J., Eom, S., Han, Y.-K., Kim, Y. S., & Lee, S. (2016) · Food & Function · doi:10.1039/c5fo01557j · Cited by 14
Országhová, Z., Uličná, O., Liptáková, A., Žitňanová, I., Muchová, J., Watała, C. W., & Ďuračková, Z. (2012) · Redox Report · doi:10.1179/1351000211y.0000000016 · Cited by 13
Application of Aptamers in Therapeutics and for Small-Molecule Detection
Menger, M., Glökler, J., & Rimmele, M. (2006) · Springer eBooks · doi:10.1007/3-540-27262-3_18 · Cited by 13
Ruan, E. D., Wang, H., Ruan, Y., & Juarez, M. M. (2013) · European Journal of Mass Spectrometry · doi:10.1255/ejms.1237 · Cited by 12
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Gibson, B. W. (2004) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2004.11.pe12 · Cited by 12
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Skandarajah, A. R., Moritz, R. L., Tjandra, J. J., & Simpson, R. J. (2005) · Expert Review of Proteomics · doi:10.1586/14789450.2.5.681 · Cited by 12
Martínez‐García, I., Cavero‐Redondo, I., Pascual‐Morena, C., Otero-Luis, I., Fenoll-Morante, M., Lever‐Megina, C. G., Rodríguez‐Gutiérrez, E., & Saz‐Lara, A. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14020474 · Cited by 12
Transition Metals and Other Forms of Oxidative Protein Damage in Renal Disease
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Antiglycative and anti-inflammatory effects of lipophilized tyrosol derivatives
Hu, X., Wang, M., & Shahidi, F. (2020) · Food Production Processing and Nutrition · doi:10.1186/s43014-020-00041-x · Cited by 10
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Boteva, E., & Mironova, R. (2019) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2019.1590160 · Cited by 9
Repairing Extracellular Aging and Glycation
Furber, J. D. (2010) · Springer eBooks · doi:10.1007/978-90-481-3999-6_19 · Cited by 9
Li, M., Cheng, W., Li, S., Wang, J., Chen, Y.-R., Liang, L., & Yang, G. F. (2025) · Frontiers in Pediatrics · doi:10.3389/fped.2024.1343870 · Cited by 8
Maillard reaction and immunogenicity of protein therapeutics
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Perceived facial age and biochemical indicators of glycemia in adult men and women
Żelaźniewicz, A., Nowak, J., Osochocka, A., & Pawłowski, B. (2022) · Scientific Reports · doi:10.1038/s41598-022-14555-6 · Cited by 6
Ghorbanizamani, F., Moulahoum, H., Bayır, E., Zihnioğlu, F., & Tımur, S. (2021) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-021-10291-z · Cited by 6
Bansal, S., Kare, P. K., Tripathi, A. K., & Madhu, S. V. (2019) · Springer eBooks · doi:10.1007/978-981-13-8273-4_20 · Cited by 6
Choe, I.-H., Jeon, H. J., Eom, S., Han, Y.-K., Kim, Y. S., & Lee, S. (2016) · Food & Function · doi:10.1039/c6fo90026g · Cited by 6
Evidence for the Presence of Glycation Adducts in Protein Therapeutics
Bozhinov, A., Boyanova, M., Niwa, T., Ivanov, I., & Mironova, R. (2010) · Biotechnology & Biotechnological Equipment · doi:10.2478/v10133-010-0036-0 · Cited by 5
Multidimensional scaling method for prediction of lysine glycation sites
Li, T., Yin, Q., Song, R., Gao, M., & Chen, Y. (2019) · Computing · doi:10.1007/s00607-019-00710-x · Cited by 6
The Application of Biomarker Data to the Study of Social Determinants of Health
Shih, R. A., Fernandes, M., & Bird, C. E. (2010) · Vanderbilt University Press eBooks · doi:10.2307/j.ctv16h2n9s.26 · Cited by 5
Lin, G., & Liu, X. (2024) · PLoS ONE · doi:10.1371/journal.pone.0307205 · Cited by 4
Multiple endogenous aldehydes amplify acetaminophen-induced liver injury
Pan, H., Luo, Q., Jing, Q., Chen, L., Li, N., Fang, C., & Shi, F. (2025) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2025.111619 · Cited by 4
Bone Quality in Type 2 Diabetes Mellitus
Farr, J. N., & Khosla, S. (2015) · Springer eBooks · doi:10.1007/978-3-319-16402-1_10 · Cited by 4
Nonenzymatic glycation of plasma proteins in smokers.
Venkatesan, A. M., Hemalatha, A., Bobby, Z., Selvaraj, N., & Sathiyapriya, V. (2006) · PubMed · Cited by 4
Pluskota‐Karwatka, D., Matysiak, D., Makarewicz, M., & Krönberg, L. (2012) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201200436 · Cited by 3
Mechanistic study of lysozyme glycation by fructose and modulation by curcumin derivatives
Nikoo, S., Maghari, A., Habibi-Rezaei, M., & Moosavi‐Movahedi, A. A. (2021) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2021.117917 · Cited by 3
Nikray, N., Abharian, N., Ashtiani, S. J., Kobarfard, F., & Faizi, M. (2024) · Iranian journal of pharmaceutical research · doi:10.5812/ijpr-153322 · Cited by 3
Comparison Between LC–MS and Ligand‐Binding Assay Approaches for Biomarker Quantification
Wang, Q., Guo, L., & Blair, I. A. (2017) · Wiley eBooks · doi:10.1002/9781119413073.ch5 · Cited by 3
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Malik, P., Rani, R., & Mukherjee, T. K. (2025) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815322521125010006 · Cited by 2
Proteomics in Drug Discovery and Development
Wang, M., & Witzmann, F. A. (2012) · Encyclopedia of Drug Metabolism and Interactions · doi:10.1002/9780470921920.edm080 · Cited by 2
Tchaikovski, V., & Waltenberger, J. L. (2007) · Springer eBooks · doi:10.1007/1-4020-5955-8_3 · Cited by 2
Hu, Z., Shen, R., Li, J., & Wu, X. (2026) · Journal of Research in Medical Sciences · doi:10.4103/jrms.jrms_277_25 · Cited by 1
Characterization of Glycated Lysine in Peptide–Sugar System
Ruan, D., Wang, H., & Cheng, F. (2018) · Springer briefs in molecular science · doi:10.1007/978-3-030-04777-1_3 · Cited by 1
Individual Glycation Sites as Biomarkers of Type 2 Diabetes Mellitus
Soboleva, A., Vashurina, N., & Frolov, A. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.95532 · Cited by 1
Naß, N., Weissenberg, K., Somoza, V., Ruhs, S., Silber, R., & Simm, A. (2013) · International Journal of Food Sciences and Nutrition · doi:10.3109/09637486.2013.839631 · Cited by 1
Oxidatively Damaged DNA and Inflammation
Dedon, P. C., & Barth, M. C. (2007) · Springer eBooks · doi:10.1007/978-0-387-72974-9_15 · Cited by 1
Turóczy, Z. (2011) · SZTE Repository of Dissertations (University of Szeged) · doi:10.14232/phd.946 · Cited by 1
Oushah, H. (2026) · e-space (Manchester Metropolitan University) · doi:10.83056/mmu.32439042 · Cited by 1
The analysis of advanced glycation endproducts
Scheijen (2017) · Research Publications (Maastricht University) · doi:10.26481/dis.20170621js · Cited by 1
Aljwaid, H. (2015) · PEARL (University of Plymouth) · doi:10.24382/2587
Activation of receptors for advanced glycation endproducts (RAGEs) in human monocytes
Ivanova, N. (2005) · OPen Access Repositorium der Universität Ulm (OPARU) (Ulm University) · doi:10.18725/oparu-658
Mechanistic and Biological Insights into Carbohydrate and Lipid Modifications of Proteins
Zhang, J. (2011) · OhioLink ETD Center (Ohio Library and Information Network)
Chapter 2: Transition Metals and Other Forms of Oxidative Protein Damage in Renal Disease
Monnier, M., Nemet, I., Sell, R. D., & Weiss, F. (2011)
Advanced Glycation End Products: Origins and Role in Aging
Khan, M. N. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11460-6
Advanced glycation end-products associate with podocytopathy in type II diabetic patientsPreprint
Nishad, R., Tahaseen, S. V., Motrapu, M., Kavvuri, R., Kodali, K., & Pasupulati, A. K. (2021) · Research Square · doi:10.21203/rs.3.rs-192615/v1
Current literature in mass spectrometry
(2004) · Journal of Mass Spectrometry · doi:10.1002/jms.665
Polyphenol loaded nanoparticles as antiglycating agents: A case study with human serum albumin
Ghosh, P., Chaudhury, S., Parveen, S., & Dasgupta, S. (2023) · doi:10.51167/acm00041
Srithongchai, Y., Harashima, A., Munesue, S., Kimura, K., Oshima, Y., Tanaka, M., Takahashi, H., Sakulsak, P., Uramoto, C., Leerach, N., et al. (2026) · Frontiers in Clinical Diabetes and Healthcare · doi:10.3389/fcdhc.2026.1854214 · Cited by 1
Glucose induced toxicity to cells: protective effects of momordica charantia
Aljohi, A. O. (2026) · e-space (Manchester Metropolitan University) · doi:10.83056/mmu.32435085
Metadata
- Authors
- Ahmed, N., & Thornalley, P. J.
- Affiliations
- University of Essex (GB)
- ORCID
- Thornalley, P.J.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2003-12-01
- Volume
- 31
- Issue
- 6
- Pages
- 1417-1422
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2136468934
- Cited by
- 152
- References
- 0
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 8 · 2020: 3 · 2019: 7 · 2018: 2 · 2017: 6 · 2016: 7 · 2015: 7 · 2014: 7 · 2013: 6 · 2012: 7
- FWCI
- 4.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- protein glycation, advanced glycation end products, oxidative stress, nitrosative stress, protein oxidation, nitrosation, protein biomarkers, hydroimidazolone, methionine sulfoxide, nitrotyrosine, fructosamine, blood plasma, renal clearance, peptide mapping, multiple reaction monitoring, proteasomal degradation, antioxidants
- MeSH terms
- Glucose, Nitroso Compounds, Oxidation-Reduction, Proteins, Mass Spectrometry, Biomarkers, Glycation End Products, Advanced
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