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MeSH Review

Maillard Reaction

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Disease relevance of Maillard Reaction


Psychiatry related information on Maillard Reaction


High impact information on Maillard Reaction


Chemical compound and disease context of Maillard Reaction


Biological context of Maillard Reaction


Anatomical context of Maillard Reaction


Associations of Maillard Reaction with chemical compounds

  • High dietary intake of ascorbic acid did not affect the fluorescence spectrum of murine lenses; thus, we assume that the speed and extent of the lenticular browning reactions must depend on a deterioration of other factors of the multicomponent antioxidant system of the eye [26].
  • Pentosidine is a recently discovered protein crosslink, involving lysine and arginine residues linked together in an imidazo [4,5,6] pyridinium ring formed by a 5-carbon sugar during nonenzymatic browning (Maillard reaction) [27].
  • The detection of a time-related increase in the amount of FFI or a closely related structure in enzymatically digested proteins implicates it as an in situ product on proteins which have undergone the Maillard reaction with glucose [28].
  • The chemistry of Maillard or browning reactions of glycated proteins was studied using the model compound, N alpha-formyl-N epsilon-fructoselysine (fFL), an analog of glycated lysine residues in protein [29].
  • Increase in 3-deoxyglucosone levels in diabetic rat plasma. Specific in vivo determination of intermediate in advanced Maillard reaction [2].

Gene context of Maillard Reaction

  • This suggests that sufficient ALR is present to detoxify 3-DG when it is formed through the Maillard reaction in vivo [30].
  • We have reported that the enzyme which reduces 3-deoxyglucosone (3-DG), a major intermediate and a potent cross-linker in the Maillard reaction, is identical with aldehyde reductase [Takahashi, M., Fujii, J., Teshima, T., Suzuki, K., Shiba, T., & Taniguchi, N. (1993) Gene 127, 249-253] [31].
  • DESIGN: Test proteins (bovine serum albumin/type I collagen) were incubated continuously for 16 weeks in glucose solutions (200 mmol/L) with or without NAC (2 mmol/L), and the generation time courses (8 and 16 weeks) of CML and furosine (the biomarker of the glycation products of the early Maillard reaction) were determined [32].
  • We propose that of the two pathways, the FN3K-independent mechanism is more important due to the fact that it breaks down the very first intermediate of the Maillard reaction, the Schiff base (a.k.a aldosamine) [33].
  • Immunochemical studies showed that acidic beta 2M reacted with anti-AGE antibody and also with an antibody against an Amadori product, an early product of the Maillard reaction, but normal beta 2M did not react with either antibody [34].

Analytical, diagnostic and therapeutic context of Maillard Reaction


  1. The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyloidosis. Miyata, T., Hori, O., Zhang, J., Yan, S.D., Ferran, L., Iida, Y., Schmidt, A.M. J. Clin. Invest. (1996) [Pubmed]
  2. Increase in 3-deoxyglucosone levels in diabetic rat plasma. Specific in vivo determination of intermediate in advanced Maillard reaction. Yamada, H., Miyata, S., Igaki, N., Yatabe, H., Miyauchi, Y., Ohara, T., Sakai, M., Shoda, H., Oimomi, M., Kasuga, M. J. Biol. Chem. (1994) [Pubmed]
  3. Is glucose the sole source of tissue browning in diabetes mellitus? Hunt, J.V., Wolff, S.P. FEBS Lett. (1990) [Pubmed]
  4. Mutagenicity of Maillard reaction products from D-glucose-amino acid mixtures and possible roles of active oxygens in the mutagenicity. Kim, S.B., Kim, I.S., Yeum, D.M., Park, Y.H. Mutat. Res. (1991) [Pubmed]
  5. Protein glycation and in vivo distribution of human lens fluorescence. Mota, M.C., Carvalho, P., Ramalho, J.S., Cardoso, E., Gaspar, A.M., Abreu, G. International ophthalmology. (1994) [Pubmed]
  6. Inhibitory effects of tenilsetam on the Maillard reaction. Shoda, H., Miyata, S., Liu, B.F., Yamada, H., Ohara, T., Suzuki, K., Oimomi, M., Kasuga, M. Endocrinology (1997) [Pubmed]
  7. Micellization of casein-graft-dextran copolymer prepared through Maillard reaction. Pan, X., Mu, M., Hu, B., Yao, P., Jiang, M. Biopolymers (2006) [Pubmed]
  8. Acrylamide from Maillard reaction products. Stadler, R.H., Blank, I., Varga, N., Robert, F., Hau, J., Guy, P.A., Robert, M.C., Riediker, S. Nature (2002) [Pubmed]
  9. Involvement of beta 2-microglobulin modified with advanced glycation end products in the pathogenesis of hemodialysis-associated amyloidosis. Induction of human monocyte chemotaxis and macrophage secretion of tumor necrosis factor-alpha and interleukin-1. Miyata, T., Inagi, R., Iida, Y., Sato, M., Yamada, N., Oda, O., Maeda, K., Seo, H. J. Clin. Invest. (1994) [Pubmed]
  10. Accumulation of Maillard reaction products in skin collagen in diabetes and aging. Dyer, D.G., Dunn, J.A., Thorpe, S.R., Bailie, K.E., Lyons, T.J., McCance, D.R., Baynes, J.W. J. Clin. Invest. (1993) [Pubmed]
  11. Advanced Maillard reaction end products are associated with Alzheimer disease pathology. Smith, M.A., Taneda, S., Richey, P.L., Miyata, S., Yan, S.D., Stern, D., Sayre, L.M., Monnier, V.M., Perry, G. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  12. Long-term fructose consumption accelerates glycation and several age-related variables in male rats. Levi, B., Werman, M.J. J. Nutr. (1998) [Pubmed]
  13. Protein modification by methylglyoxal: chemical nature and synthetic mechanism of a major fluorescent adduct. Shipanova, I.N., Glomb, M.A., Nagaraj, R.H. Arch. Biochem. Biophys. (1997) [Pubmed]
  14. Antimutagenic activity of browning reaction products. Chan, R.I., Stich, H.F., Rosin, M.P., Powrie, W.D. Cancer Lett. (1982) [Pubmed]
  15. The cognition-enhancing drug tenilsetam is an inhibitor of protein crosslinking by advanced glycosylation. Münch, G., Taneli, Y., Schraven, E., Schindler, U., Schinzel, R., Palm, D., Riederer, P. Journal of neural transmission. Parkinson's disease and dementia section. (1994) [Pubmed]
  16. Inhibitory activity of Maillard reaction products against Trp-P1-induced mutagenicity to the Salmonella typhimurium TA 98 streptomycin-dependent strain assayed in the absence of S-9 mix. Hosono, A., Usman, n.u.l.l., Ohba, R. Biosci. Biotechnol. Biochem. (1997) [Pubmed]
  17. Pentosidine formation in skin correlates with severity of complications in individuals with long-standing IDDM. Sell, D.R., Lapolla, A., Odetti, P., Fogarty, J., Monnier, V.M. Diabetes (1992) [Pubmed]
  18. Formation of vinylogous compounds in model Maillard reaction systems. Stadler, R.H., Verzegnassi, L., Varga, N., Grigorov, M., Studer, A., Riediker, S., Schilter, B. Chem. Res. Toxicol. (2003) [Pubmed]
  19. Oxidative deamination of lysine residue in plasma protein of diabetic rats. Novel mechanism via the Maillard reaction. Akagawa, M., Sasaki, T., Suyama, K. Eur. J. Biochem. (2002) [Pubmed]
  20. Accelerated glycation of the aorta in diabetic rats. Oimomi, M., Masuda, S., Nakamichi, T., Maeda, Y., Hata, F., Kitamura, Y., Matsumoto, S., Hatanaka, H., Baba, S. Diabetes Res. Clin. Pract. (1987) [Pubmed]
  21. Lipid peroxidation of liposome induced by glucosone. Nakayama, T., Yamada, M., Osawa, T., Kawakishi, S. J. Nutr. Sci. Vitaminol. (1992) [Pubmed]
  22. Lysyl oxidase and Maillard reaction-mediated crosslinks in aging and osteoarthritic rabbit cartilage. Pokharna, H.K., Monnier, V., Boja, B., Moskowitz, R.W. J. Orthop. Res. (1995) [Pubmed]
  23. Identification and quantification of phosphatidylethanolamine-derived glucosylamines and aminoketoses from human erythrocytes--influence of glycation products on lipid peroxidation. Breitling-Utzmann, C.M., Unger, A., Friedl, D.A., Lederer, M.O. Arch. Biochem. Biophys. (2001) [Pubmed]
  24. Non-clastogenicity in mouse bone marrow of fructose/lysine and other sugar/amino acid browning products with in vitro genotoxicity. MacGregor, J.T., Tucker, J.D., Ziderman, I.I., Wehr, C.M., Wilson, R.E., Friedman, M. Food Chem. Toxicol. (1989) [Pubmed]
  25. Bacterial enzymes that can deglycate glucose- and fructose-modified lysine. Monnier, V.M. Biochem. J. (2005) [Pubmed]
  26. The role of ascorbic acid in senile cataract. Bensch, K.G., Fleming, J.E., Lohmann, W. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  27. High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis. Nagaraj, R.H., Sell, D.R., Prabhakaram, M., Ortwerth, B.J., Monnier, V.M. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  28. Detection of an advanced glycosylation product bound to protein in situ. Chang, J.C., Ulrich, P.C., Bucala, R., Cerami, A. J. Biol. Chem. (1985) [Pubmed]
  29. Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. Ahmed, M.U., Thorpe, S.R., Baynes, J.W. J. Biol. Chem. (1986) [Pubmed]
  30. Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression. Takahashi, M., Fujii, J., Teshima, T., Suzuki, K., Shiba, T., Taniguchi, N. Gene (1993) [Pubmed]
  31. In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites. Takahashi, M., Lu, Y.B., Myint, T., Fujii, J., Wada, Y., Taniguchi, N. Biochemistry (1995) [Pubmed]
  32. Suppression of N(epsilon)-(carboxymethyl)lysine generation by the antioxidant N-acetylcysteine. Nakayama, M., Izumi, G., Nemoto, Y., Shibata, K., Hasegawa, T., Numata, M., Wang, K., Kawaguchi, Y., Hosoya, T. Peritoneal dialysis international : journal of the International Society for Peritoneal Dialysis. (1999) [Pubmed]
  33. Intrinsic toxicity of glucose, due to non-enzymatic glycation, is controlled in-vivo by deglycation systems including: FN3K-mediated deglycation of fructosamines and transglycation of aldosamines. Szwergold, B.S. Med. Hypotheses (2005) [Pubmed]
  34. beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. Miyata, T., Oda, O., Inagi, R., Iida, Y., Araki, N., Yamada, N., Horiuchi, S., Taniguchi, N., Maeda, K., Kinoshita, T. J. Clin. Invest. (1993) [Pubmed]
  35. Conversion of Amadori products of the Maillard reaction to N(epsilon)-(carboxymethyl)lysine by short-term heating: possible detection of artifacts by immunohistochemistry. Miki Hayashi, C., Nagai, R., Miyazaki, K., Hayase, F., Araki, T., Ono, T., Horiuchi, S. Lab. Invest. (2002) [Pubmed]
  36. Monitoring the formation of Maillard reaction products of glucosamine with fibrinogen and human serum albumin using capillary electrophoresis. Zhang, X., Ma, Y., Liu, H., de Sa, P.F., Brown, P.R., Dain, J.A. Anal. Biochem. (2004) [Pubmed]
  37. Silver staining of collagen type I after sodium dodecylsulphate polyacrylamide gel electrophoresis: effect of Maillard reaction. Hodny, Z., Struzinsky, R., Deyl, Z. J. Chromatogr. (1992) [Pubmed]
  38. Antioxidant activity of sugar-lysine Maillard reaction products in cell free and cell culture systems. Jing, H., Kitts, D.D. Arch. Biochem. Biophys. (2004) [Pubmed]
  39. Two types of radicals in whole milk powder. Effect of lactose crystallization, lipid oxidation, and browning reactions. Thomsen, M.K., Lauridsen, L., Skibsted, L.H., Risbo, J. J. Agric. Food Chem. (2005) [Pubmed]
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