The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Proteins containing reductively aminated disaccharides
Schwartz, B. A., & Gray, G. R. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90261-2 · Cited by 230
The interaction of aldehydes with collagen
Bowes, J. H., & Cater, C. W. (1968) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(68)90156-6 · Cited by 219
Miyata, S., & Monnier, V. M. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115690 · Cited by 218
Self-citationPentosidine: A molecular marker for the cumulative damage to proteins in diabetes, aging, and uremia
Sell, D. R., Nagaraj, R. H., Grandhee, S. K., Odetti, P. R., Lapolla, A., Fogarty, J. F., & Monnier, V. M. (1991) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610070404 · Cited by 187
Self-citationDunn, J. A., Ahmed, M. U., Murtiashaw, M. H., Richardson, J. M., Walla, M. D., Thorpe, S. R., & Baynes, J. (1990) · Biochemistry · doi:10.1021/bi00501a014 · Cited by 170
Role of Oxygen in Cross-Linking and Chemical Modification of Collagen by Glucose
Fu, M.-X., Wells‐Knecht, K. J., Thorpe, S. R., & Baynes, J. (1992) · Diabetes · doi:10.2337/diab.41.2.s42 · Cited by 149
Reaction of glycolaldehyde with proteins: latent crosslinking potential of alpha-hydroxyaldehydes.
Acharya, A. S., & Manning, J. M. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.12.3590 · Cited by 89
Brownlee, M., Vlassara, H., & Cerami, A. (1980) · Diabetes · doi:10.2337/diab.29.12.1044 · Cited by 79
Nedvidek, W., Ledl, F., & Fischer, P. (1992) · European Food Research and Technology · doi:10.1007/bf01198411 · Cited by 64
Hayashi, T., Ohta, Y., & Namiki, M. (1977) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60214a047 · Cited by 50
Darstellung aliphatischer Amadori‐Produkte
Micheel, F., & Hagemann, G. (1959) · Chemische Berichte · doi:10.1002/cber.19590921127 · Cited by 37
2,3-Dihydroxy-1,4-dioxane: A Stable Synthetic Equivalent of Anhydrous Glyoxal
Venuti, M. C. (1982) · Synthesis · doi:10.1055/s-1982-29701 · Cited by 34
New Imidazoles Formed in Nonenzymatic Browning Reactions
Velı́šek, J., Davídek, T., DAVÍEK, J., Trška, P., Kvasnička, F., & VELCOVÁ, K. (1989) · Journal of Food Science · doi:10.1111/j.1365-2621.1989.tb05155.x · Cited by 32
Erickson, J. G. (1952) · Journal of the American Chemical Society · doi:10.1021/ja01138a506 · Cited by 30
Smith, P. R., Somani, H. H., Thornalley, P. J., Benn, J. J., & Sönksen, P. H. (1993) · Clinical Science · doi:10.1042/cs0840087 · Cited by 23
Marion, M. S., & Carlson, E. C. (1994) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(94)90230-5 · Cited by 20
Slight, S. H., Prabhakaram, M., Shin, D. B., Feather, M. S., & ORTWERTH, B. J. (1992) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(92)90080-e · Cited by 17
Reversible modification of arginine residues with glyoxal
Glass, J. D., & Pelzig, M. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91566-8 · Cited by 16
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
Cited by
Sorted by citations
Role of advanced glycation end products in cellular signaling
Ott, C., Jacobs, K., Haucke, E., Navarrete Santos, A., Grune, T., & Simm, A. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.016 · Cited by 1,150
Basta, G. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.05.001 · Cited by 1,018
Advanced glycation endproducts in food and their effects on health
Poulsen, M. W., Hedegaard, R. V., Andersen, J. M., de Courten, B., Bügel, S., Nielsen, J., Skibsted, L. H., & Dragsted, L. O. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.06.052 · Cited by 751
Oxidative Stress and Diabetic Retinopathy
Kowluru, R. A., & Chan, P.-S. (2007) · Journal of Diabetes Research · doi:10.1155/2007/43603 · Cited by 772
Aldehyde Sources, Metabolism, Molecular Toxicity Mechanisms, and Possible Effects on Human Health
O'Brien, P. J., Siraki, A. G., & Shangari, N. (2005) · Critical Reviews in Toxicology · doi:10.1080/10408440591002183 · Cited by 738
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
