Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification-A role in pathogenesis and antiproliferative chemotherapy
Abstract
1. Methylglyoxal is a reactive alpha-oxoaldehyde and physiological metabolite formed by the fragmentation of triose-phosphates, and by the metabolism of acetone and aminoacetone. 2. Methylglyoxal modifies guanylate residues to form 6,7-dihydro-6,7-dihydroxy-6-methyl-imidazo[2,3-b]purine-9(8)one and N2-(1-carboxyethyl)guanylate residues and induces apoptosis. 3. Methylglyoxal modifies arginine residues in proteins to form N(delta)-(4,5-dihydroxy-4-methylimidazolidin-2-yl) ornithine, N(delta)-(5-hydro-5-methylimidazol-4-on-2-yl)ornithine and N(delta)-(5)methylimidazol-4-on-2-yl)ornithine residues. 4. Methylglyoxal-modified proteins undergo receptor-mediated endocytosis and lysosomal degradation in monocytes and macrophages, and induce cytokine synthesis and secretion. 5. Methylglyoxal is detoxified by the glyoxalase system. Decreased detoxification of methylglyoxal may be induced pharmacologically by glyoxalase I inhibitors which have anti-tumor and anti-malarial activities. 6. The modification of nucleic acids and protein by methylglyoxal is a signal for their degradation and may have a role in the development of diabetic complications, atherosclerosis, the immune response in starvation, aging and oxidative stress.
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AGEs can be formed through the polyol pathway and lipid peroxidation in the presence and absence of hyperglycemia.
“In addition to nonenzymatic glycation, AGEs can be formed through the polyol pathway and lipid peroxidation in the presence and absence of hyperglycemia, depending on the substrate type, reactant concentration, exposure time, and host cellular context14–17.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [17]
Cites
Oxidative stress as a mediator of apoptosis
Buttke, T. M., & Sandstrom, P. A. (1994) · Immunology Today · doi:10.1016/0167-5699(94)90018-3 · Cited by 2,149 · see citing works
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 · see citing works
Rajavashisth, T. B., Andalibi, A., Territo, M., Berliner, J. A., Navab, M., Fogelman, A. M., & Lusis, A. J. (1990) · Nature · doi:10.1038/344254a0 · Cited by 775 · see citing works
Lo, T. W. C., Westwood, M. E., McLellan, A. C., Selwood, T., & Thornalley, P. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31635-1 · Cited by 695 · see citing works
Self-citationRelation between Complications of Type I Diabetes Mellitus and Collagen-Linked Fluorescence
Monnier, V. M., Vishwanath, V., Frank, K. E., Elmets, C. A., Dauchot, P. J., & Kohn, R. R. (1986) · New England Journal of Medicine · doi:10.1056/nejm198602133140702 · Cited by 585 · see citing works
Glomb, M. A., & Monnier, V. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.10017 · Cited by 576 · see citing works
The formation of methylglyoxal from triose phosphates
Phillips, S. A., & Thornalley, P. J. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17638.x · Cited by 565 · see citing works
Self-citationGlyoxalase System in Clinical Diabetes Mellitus and Correlation with Diabetic Complications
McLellan, A. C., Thornalley, P. J., Benn, J. J., & Sönksen, P. H. (1994) · Clinical Science · doi:10.1042/cs0870021 · Cited by 557 · see citing works
Self-citationThe glyoxalase system in health and disease
Thornalley, P. J. (1993) · Molecular Aspects of Medicine · doi:10.1016/0098-2997(93)90002-u · Cited by 535 · see citing works
Self-citationAminoguanidine treatment inhibits the development of experimental diabetic retinopathy.
Hammes, H., Martin, S., Federlin, K., Geisen, K., & Brownlee, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11555 · Cited by 523 · see citing works
Soulis, T., Cooper, M. E., Papazoglou, D., Clarke, B., & Jerums, G. (1991) · Diabetes · doi:10.2337/diabetes.40.10.1328 · Cited by 446 · see citing works
McCance, 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 · see citing works
The role of aldose reductase in the development of diabetic complications
Kador, P. F. (1988) · Medicinal Research Reviews · doi:10.1002/med.2610080302 · Cited by 298 · see citing works
Jagt, D. L. V., Robinson, B., Taylor, K. K., & Hunsaker, L. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42844-x · Cited by 280 · see citing works
Pompliano, D. L., Peyman, A., & Knowles, J. R. (1990) · Biochemistry · doi:10.1021/bi00465a005 · Cited by 272 · see citing works
Koop, D. R., & Casazza, J. P. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38768-9 · Cited by 260 · see citing works
Araki, N., Higashi, T., Mori, T., Shibayama, R., Kawabe, Y., Kodama, T., Takahashi, K., Shichiri, M., & Horiuchi, S. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0408h.x · Cited by 248 · see citing works
Modification of the glyoxalase system in human red blood cells by glucose in vitro
Thornalley, P. J. (1988) · Biochemical Journal · doi:10.1042/bj2540751 · Cited by 239 · see citing works
Self-citationMcLellan, A. C., Phillips, S. A., & Thornalley, P. J. (1992) · Analytical Biochemistry · doi:10.1016/s0003-2697(05)80005-3 · Cited by 220 · see citing works
Self-citationStimulation of rat mesangial cell proliferation by macrophage interleukin 1.
Lovett, D. H., Ryan, J. L., & Sterzel, R. B. (1983) · The Journal of Immunology · doi:10.4049/jimmunol.131.6.2830 · Cited by 218 · see citing works
Richard, J. P. (1991) · Biochemistry · doi:10.1021/bi00232a031 · Cited by 204 · see citing works
Lyles, G. A., & Chalmers, J. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90196-p · Cited by 197 · see citing works
Kang, Y., Edwards, L. G., & Thornalley, P. J. (1996) · Leukemia Research · doi:10.1016/0145-2126(95)00162-x · Cited by 182 · see citing works
Self-citationAcetone Metabolism in Humans During Diabetic Ketoacidosis
Reichard, G., Skutches, C. L., Hoeldtke, R. D., & Owen, O. E. (1986) · Diabetes · doi:10.2337/diab.35.6.668 · Cited by 177 · see citing works
Taylor, R., & Agius, L. (1988) · Biochemical Journal · doi:10.1042/bj2500625 · Cited by 166 · see citing works
Identification of N2-(1-Carboxyethyl)guanine (CEG) as a Guanine Advanced Glycosylation End Product
Papoulis, A. T., Al‐Abed, Y., & Bucala, R. (1995) · Biochemistry · doi:10.1021/bi00002a032 · Cited by 160 · see citing works
Plasma Acetone Metabolism in the Fasting Human
Reichard, G., Haff, A. C., Skutches, C. L., Paul, P., Holroyde, C. P., & Owen, O. E. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109344 · Cited by 156 · see citing works
Modification of the glyoxalase system in streptozotocin-induced diabetic rats
Phillips, S. A., Mirrlees, D. J., & Thornalley, P. J. (1993) · Biochemical Pharmacology · doi:10.1016/0006-2952(93)90488-i · Cited by 141 · see citing works
Self-citationCameron, N. E., Cotter, M. A., Dines, K. C., & Love, A. (1992) · Diabetologia · doi:10.1007/bf00401423 · Cited by 136 · see citing works
d-Lactate production in erythrocytes infected with Plasmodium falciparum
Jagt, D. L. V., Hunsaker, L. A., Campos, N. M., et al. (1990) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(90)90171-h · Cited by 131 · see citing works
Enzymology and Molecular Biology of Carbonyl Metabolism 7
Weiner, H., Maser, E., Crabb, D. W., & Lindahl, R. G. (1999) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4735-8 · Cited by 127 · see citing works
Schmidt, A. M., Mora, R., Cao, R. Y., Yan, S. D., Brett, J., Ramakrishnan, R., Tsang, T. C., Simionescu, M., & Stern, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36965-x · Cited by 123 · see citing works
Lo, T. W. C., Selwood, T., & Thornalley, P. J. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90584-3 · Cited by 103 · see citing works
Self-citationGlyoxalase inhibitors as potential anticancer agents
Vince, R., & Wadd, W. B. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90445-8 · Cited by 103 · see citing works
Methylglyoxal Concentration and Glyoxalase Activities in the Human Lens
HAIK, G. M., Lo, T. W. C., & Thornalley, P. J. (1994) · Experimental Eye Research · doi:10.1006/exer.1994.1135 · Cited by 96 · see citing works
Self-citationMotoko, T., Fujii, J., Teshima, T., Keiichiro, S., Shiba, T., & Taniguchi, N. (1993) · Gene · doi:10.1016/0378-1119(93)90728-l · Cited by 93 · see citing works
Mutagenicity of methylglyoxal in coffee.
Kasai, H., Kumeno, K., Yamaizumi, Z., Nishimura, S., Nagao, M., Fujita, Y., Sugimura, T., Nukaya, H., & Kosuge, T. (1982) · PubMed · Cited by 91 · see citing works
Tumour necrosis factor and cachexia: a current perspective
Espat, N. J., Copeland, E. M., & Moldawer, L. L. (1994) · Surgical Oncology · doi:10.1016/0960-7404(94)90027-2 · Cited by 90 · see citing works
Isolation of methylglyoxal synthase from goat liver.
Ray, S., & Ray, M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69151-9 · Cited by 89 · see citing works
Humoral Mediation of Changing Body Composition During Aging and Chronic Inflammation
Roubenoff, R., & Rall, L. C. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1993.tb03045.x · Cited by 89 · see citing works
Aldose reductase: model for a new paradigm of enzymic perfection in detoxification catalysts
Grimshaw, C. E. (1992) · Biochemistry · doi:10.1021/bi00157a001 · Cited by 87 · see citing works
Optimization of efficiency in the glyoxalase pathway
Creighton, D. J., Migliorini, M., Pourmotabbed, T., et al. (1988) · Biochemistry · doi:10.1021/bi00419a031 · Cited by 83 · see citing works
Kinetic analysis of the human erythrocyte glyoxalase system using 1H NMR and a computer model
Rae, C. D., Berners‐Price, S. J., Bulliman, B. T., & Kuchel, P. W. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19307.x · Cited by 74 · see citing works
Lo, T. W. C., & Thornalley, P. J. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90680-h · Cited by 67 · see citing works
Self-citationThornalley, P. J., Strath, M., & Wilson, R. J. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90035-3 · Cited by 66 · see citing works
Self-citationJagt, D. L. V., Daub, E., Krohn, J. A., et al. (1975) · Biochemistry · doi:10.1021/bi00687a024 · Cited by 66 · see citing works
Reactions of methylglyoxal with nucleic acids
Krymkiewicz, N. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80013-4 · Cited by 63 · see citing works
Vaca, C. E., Fang, J., Conradi, M., & Hou, S. (1994) · Carcinogenesis · doi:10.1093/carcin/15.9.1887 · Cited by 61 · see citing works
Palkama, T. (1991) · PubMed · Cited by 59 · see citing works
Formation of methylglyoxal and d -lactate in human red blood cells in vitro
Phillips, S. A., & Thornalley, P. J. (1993) · Biochemical Society Transactions · doi:10.1042/bst021163s · Cited by 54 · see citing works
Self-citationMenzel, E. J., & Reihsner, R. (1991) · Diabetologia · doi:10.1007/bf00404018 · Cited by 52 · see citing works
Diamond, J. R., Ding, G., Frye, J., et al. (1992) · PubMed · Cited by 49 · see citing works
Allen, R. E., Lo, T. W. C., & Thornalley, P. J. (1993) · Journal of Protein Chemistry · doi:10.1007/bf01026032 · Cited by 47 · see citing works
Self-citationInhibition of proliferation of human leukaemia 60 cells by methylglyoxal in vitro
AYOUB, F. M., Allen, R. E., & Thornalley, P. J. (1993) · Leukemia Research · doi:10.1016/0145-2126(93)90094-2 · Cited by 45 · see citing works
Self-citationMethylglyoxal-induced DNA-protein cross-links and cytotoxicity in Chinese hamster ovary cells
Brambilla, G., Sciabà, L., Faggin, P., et al. (1985) · Carcinogenesis · doi:10.1093/carcin/6.5.683 · Cited by 45 · see citing works
Acetone metabolism in humans during diabetic ketoacidosis
Reichard, G. A., Skutches, C. L., Hoeldtke, R. D., et al. (1986) · Diabetes · doi:10.2337/diabetes.35.6.668 · Cited by 39 · see citing works
Expression of mRNA coding for TNFα, IL-1β and IL-6 by cells infiltrating retinal membranes
Limb, G. A., Earley, O., Jones, S. E., et al. (1994) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/bf00171378 · Cited by 38 · see citing works
Quantitative determination of human aldose reductase by enzyme-linked immunosorbent assay
Nishimura, C., Furue, M., Ito, T., Omori, Y., & Tanimoto, T. (1993) · Biochemical Pharmacology · doi:10.1016/0006-2952(93)90343-u · Cited by 37 · see citing works
Biologic control of the tumor necrosis factor and interleukin-1 signaling cascade
Stewart, R. J., & Marsden, P. A. (1995) · American Journal of Kidney Diseases · doi:10.1016/0272-6386(95)90582-0 · Cited by 36 · see citing works
Biosynthesis and degradation of methylglyoxal in animals.
Ohmori, S., Mori, M., Shiraha, K., et al. (1989) · PubMed · Cited by 35 · see citing works
Formation of strand breaks and interstrand cross‐links in DNA by methylglyoxal
Rahman, A., Shahab Uddin, M. S., & Hadi, S. M. (1990) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.2570050305 · Cited by 34 · see citing works
Nutritional and physiological consequences of tumour glycolysis
Dills, W. L. (1993) · Parasitology · doi:10.1017/s0031182000075600 · Cited by 32 · see citing works
Larsen, K., Aronsson, A.-C., Marmstål, E., & Mannervik, B. (1985) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(85)90499-7 · Cited by 30 · see citing works
Monitoring the progress of non‐enzymatic glycation in vitro
Shaw, S. M., & Crabbe, M. J. C. (1994) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1994.tb01149.x · Cited by 28 · see citing works
Shaw, S. M., & Crabbe, M. J. C. (1994) · Biochemical Journal · doi:10.1042/bj3040121 · Cited by 25 · see citing works
Tucker, J. D., Taylor, R. T., Christensen, M. L., et al. (1989) · Mutation Research/Genetic Toxicology · doi:10.1016/0165-1218(89)90166-3 · Cited by 24 · see citing works
Subchronic oral toxicity of glyoxal via drinking water in rats
UENO, H. (1991) · Fundamental and Applied Toxicology · doi:10.1016/0272-0590(91)90162-w · Cited by 20 · see citing works
Faggin, P., Bassi, A. M., Finollo, R., et al. (1985) · Mutation Research Letters · doi:10.1016/0165-7992(85)90138-1 · Cited by 19 · see citing works
N-2 Acetylation of 2′-deoxyguanosine by coffee mutagens, methylglyoxal and hydrogen peroxide
Nukaya, H., Iwami, T., Ishida, H., et al. (1990) · Mutation Research Letters · doi:10.1016/0165-7992(90)90154-c · Cited by 17 · see citing works
Cook, P. N., Ward, W. H. J., Petrash, J. M., et al. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)98499-y · Cited by 15 · see citing works
Lübec, G., Vierhapper, H., Bailey, A. J., et al. (1991) · Amino Acids · doi:10.1007/bf00808093 · Cited by 12 · see citing works
Changes of certain pharmacological and biochemical indices in acute methylglyoxal poisoning.
Jerzykowski, T., Matuszewski, W., Tarnawski, R., et al. (1975) · PubMed · Cited by 12 · see citing works
Praloran, V., Meur, Y. L., Coupey, L., & Rince, M. (1995) · Cytokine · doi:10.1006/cyto.1995.1029 · Cited by 5 · see citing works
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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 · see citing works
Vistoli, G., De Maddis, D., Cipak, A., Zarkovic, N., Carini, M., & Aldini, G. (2013) · Free Radical Research · doi:10.3109/10715762.2013.815348 · Cited by 823 · see citing works
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Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411 · see citing works
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Schalkwijk, C. G., Stehouwer, C. D. A., & van Hinsbergh, V. W. M. (2004) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.488 · Cited by 206 · see citing works
Advanced glycation end products and mortality in hemodialysis patients
Schwedler, S. B., Metzger, T., Schinzel, R., & Wanner, C. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00423.x · Cited by 195 · see citing works
Kumar Pasupulati, A., Chitra, P. S., & Reddy, G. B. (2016) · Biomolecular Concepts · doi:10.1515/bmc-2016-0021 · Cited by 163 · see citing works
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Jump, D. B., Lytle, K. A., Depner, C. M., & Tripathy, S. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.07.007 · Cited by 142 · see citing works
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Kuhla, B., Boeck, K., Schmidt, A., Ogunlade, V., Arendt, T., Münch, G., & Lüth, H.-J. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.11.007 · Cited by 108 · see citing works
Identification of α-dicarbonyl scavengers for cellular protection against carbonyl stress
Wondrak, G. T., Cervantes-Laurean, D., Roberts, M. J., Qasem, J. G., Kim, M., Jacobson, E. L., & Jacobson, M. K. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00915-7 · Cited by 108 · see citing works
Gutierrez‐Mariscal, F. M., Cardelo, M. P., de la Cruz, S., Alcala‐Diaz, J. F., Roncero‐Ramos, I., Guler, I., Vals‐Delgado, C., López‐Moreno, A., Luque, R. M., Delgado‐Lista, J., et al. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201901290 · Cited by 60 · see citing works
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Bechara, E. J. H., Dutra, F., Cardoso, V. E. S., Sartori, A., Olympio, K. P. K., Penatti, C. A. A., Adhikari, A., & Assunção, N. A. (2007) · Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology · doi:10.1016/j.cbpc.2006.07.004 · Cited by 57 · see citing works
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Lopez‐Moreno, J., Quintana‐Navarro, G. M., Camargo, A., Jimenez‐Lucena, R., Delgado‐Lista, J., Marin, C., Tinahones, F. J., Striker, G. E., Roche, H. M., Perez‐Martinez, P., et al. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201601029 · Cited by 41 · see citing works
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- Authors
- Thornalley, P. J.
- Affiliations
- University of Essex (GB)
- Corresponding author
- Thornalley, Paul J.
- ORCID
- Thornalley, Paul J.
- Venue
- General Pharmacology: The Vascular System
- Publisher
- Elsevier BV
- Published
- 1996-06
- Volume
- 27
- Issue
- 4
- Pages
- 565-573
- ISSN
- 0306-3623 (ISSN-L)
- OpenAlex
- W1973924126
- Cited by
- 591
- References
- 73
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 16 · 2023: 13 · 2022: 24 · 2021: 13 · 2020: 23 · 2019: 19 · 2018: 26 · 2017: 30 · 2016: 22 · 2015: 33 · 2014: 26 · 2013: 21 · 2012: 29
- FWCI
- 2.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- General Pharmacology The Vascular System (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Keywords
- methylglyoxal, advanced glycation end products, protein modification, nucleic acid modification, apoptosis, arginine modification, lysosomal degradation, cytokine production, monocytes/macrophages, diabetes complications, oxidative stress, alpha-oxoaldehydes
- MeSH terms
- Animals, Antineoplastic Agents, Biotransformation, Humans, Neoplasms, Nucleic Acids, Proteins, Pyruvaldehyde
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