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Mechanism of Protein Modification by Glyoxal and Glycolaldehyde, Reactive Intermediates of the Maillard Reaction
Open accessAbstract
The role of glyoxal and glycolaldehyde in protein cross-linking and N epsilon-(carboxymethyl)lysine (CML) formation during Maillard reaction under physiological conditions was investigated. Incubation of bovine serum albumin with these reagents lead to rapid formation of C-2-imine cross-links and CML. Initial CML formation rate from glyoxal was not dependent on oxidation, suggesting an intramolecular Cannizzaro reaction. CML formation from glucose/lysine or Amadori product of both was strongly dependent on oxidation. Blocking of Amadori product by boric acid totally suppressed CML formation from Amadori product, but only by 37% in the glucose/lysine system. Trapping of glyoxal with aminoguanidine hardly suppressed CML formation from Amadori product, whereas it blocked 50% of CML production in the glucose/lysine system. While these results would support a significant role for glucose autoxidation in CML formation, the addition of lysine to a glucose/aminoguanidine incubation system catalyzed glyoxal-triazine formation 7-fold, thereby strongly suggesting that glucose autoxidation is not a factor for glyoxal-mediated CML formation. Based on these results, it can be estimated that approximately 50% of the CML forming in a glucose/lysine system originates from oxidation of Amadori product, and 40-50% originates from a pre-Amadori stage largely independent from glucose autoxidation. This step may be related to the so-called Namiki pathway of the Maillard reaction.
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“CML was the first discovered glycoxidation product and is formed by oxidative degradation of fructoselysine (Amadori product) [35]. An alternative pathway is the reaction between the α-dicarbonyl compound glyoxal and lysine leading to CML formation via an isomerization mechanism [36].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [36]
Citations
Cites
Aminoguanidine Prevents Diabetes-Induced Arterial Wall Protein Cross-Linking
Brownlee, M., Vlassara, H., Kooney, A., Ulrich, P. C., & Cerami, A. (1986) · Science · doi:10.1126/science.3487117 · Cited by 1,146
Protein glycation and oxidative stress in diabetes mellitus and ageing
Wolff, S. P., Jiang, Z. Y., & Hunt, J. V. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90040-a · Cited by 886
Ahmed, M. U., Thorpe, S. R., & Baynes, J. W. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89188-3 · Cited by 864
Johnson, R. N., Metcalf, P., & Baker, J. R. (1983) · Clinica Chimica Acta · doi:10.1016/0009-8981(83)90078-5 · Cited by 763
Benson, J. R., & Hare, P. E. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.2.619 · Cited by 738
New Aspects of the Maillard Reaction in Foods and in the Human Body
Ledl, F., & Schleicher, E. D. (1990) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199005653 · Cited by 738
Grandhee, S. K., & Monnier, V. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99006-x · Cited by 459
Self-citationMcCance, D. R., Dyer, D. G., Dunn, J. A., Bailie, K., Thorpe, S. R., Baynes, J., & Lyons, T. J. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116482 · Cited by 444
Dunn, J. A., McCance, D. R., Thorpe, S. R., Lyons, T. J., & Baynes, J. (1991) · Biochemistry · doi:10.1021/bi00219a007 · Cited by 304
Dunn, J. A., Patrick, J. S., Thorpe, S. R., & Baynes, J. (1989) · Biochemistry · doi:10.1021/bi00450a033 · Cited by 250
Flagged first, then by citations
Research works printed but not linked: 5
- Baynes, 1989, Prog. Clin. Biol Res., 304, 1
- Portero-Otin, 1995, Biochim Biophys. Acta
- Hayashi, 1985, Agric. Biol. Chem., 49, 3131
- Cho, 1986, Agric. Biol. Chem., 50, 1373
- Chuyen, 1973, Agric. Biol. Chem., 37
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Glycation, Glycoxidation and other Maillard Reaction Products
Monnier, V. M., Fogarty, J. F., Monnier, C., & Sell, D. R. (1998) · CRC Press eBooks · doi:10.1201/b14256-37 · Cited by 14
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Metadata
- Authors
- Glomb, M. A., & Monnier, V. M.
- Affiliations
- Case Western Reserve University (US)
- Corresponding author
- Glomb, Marcus A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-04
- Volume
- 270
- Issue
- 17
- Pages
- 10017-10026
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2017214714
- Cited by
- 576
- References
- 28
- Citations by year
- 2026: 10 · 2025: 9 · 2024: 13 · 2023: 13 · 2022: 12 · 2021: 24 · 2020: 8 · 2019: 12 · 2018: 24 · 2017: 16 · 2016: 19 · 2015: 20 · 2014: 22 · 2013: 19 · 2012: 18
- FWCI
- 11.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ag005601-13)
- National Institute on Aging (AG 05601)
- National Eye Institute (EY 07099, R01EY007099)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- Maillard reaction, glyoxal, glycolaldehyde, carboxymethyllysine, protein cross-linking, bovine serum albumin, Amadori products, Cannizzaro reaction, protein oxidation, boric acid, aminoguanidine
- MeSH terms
- Acetaldehyde, Chromatography, High Pressure Liquid, Chromatography, Thin Layer, Electrophoresis, Polyacrylamide Gel, Glyoxal, Lysine, Gas Chromatography-Mass Spectrometry, Oxidation-Reduction, Proteins, Maillard Reaction
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