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Article / Publication Details
Metabolic transit data on food-borne advanced MRPs (Maillard reaction products) termed melanoidins are yet not completely elucidated and it is still an open question whether isolated melanoidin structures undergo metabolic biotransformation and subsequently cause physiological effects in vivo. Advanced MRPs, acting as premelanoidins, and melanoidins are formed under severe heat treatment of foods and are ingested with the habitual diet at considerable amounts. Metabolic transit data are known for Amadori compounds classified as early MRPs, like, e.g., fructose-lysine. For rats and humans, the percentages of ingested free versus protein-bound fructose-lysine excreted in the urine were found within ranges of 60–80% and 3–10%, respectively. Balance studies on free advanced MRPs are still lacking, but protein-bound low-molecular-weight premelanoidins and high-molecular-weight melanoidins have already been investigated in animal experiments using 14C-tracer isotopes. The amount of ingested radioactivity absorbed and excreted in the urine was found at levels ranging from 16 to 30% and from 1 to 5% for premelanoidins and melanoidins, respectively. These different metabolic transit data of premelanoidins and melanoidins can be explained by the following mechanisms involved: (i) intestinal degradation by digestive and microbial enzymes; (ii) absorption of these compounds or their degradates, and (iii) tissue retention. Structure specific in vivo effects have been identified for protein-bound premelanoidins on intestinal microbial activity, xenobiotic biotransformation enzymes and further glycation reactions. The latter are hypothesized to be involved in the aging process and in the course of different diseases. Further investigations are needed to clarify synergistic in vivo effects of dietary ingested melanoidins and endogenously formed glycation products.
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- Adrian J: Nutritional and physiological consequences of the Maillard reaction. World Rev Nutr Diet 1974;19:71–122.
- Alaiz M, Hidalgo FJ, Zamora R: Antioxidative activity of nonenzymatically browned proteins produced in oxidized lipid/protein reactions. J Agric Food Chem 1997;45:3250–3254.
- Ames JM, Wynne A, Hofmann A, Plos S, Gibson GR: The effect of a model melanoidin mixture on faecel bacterial populations in vitro. Br J Nutr 1999;82:489–495.
- Andrieux C, Sacquet E, Gueguen L: Interactions between Maillard’s reaction products, the microflora of the digestive tract and mineral metabolism. Reprod Nutr Dev 1980;20:1061–1069.
- Andrieux C, Sacquet E: Effects of Maillard’s reaction products on apparent mineral absorption in different parts of the digestive tract: The role of microflora. Reprod Nutr Dev 1984;24:379–386.
- Blot WJ, Li JY, Taylor PR, Guo W, Dawsey SM, Li B: The Linxian trials: Mortality rates by vitamin-mineral intervention group. Am J Clin Nutr 1995;62:1424–1426.
- Bogaards JJ, van Ommen B, Falke HE, Willems MI, van Bladeren PJ: Glutathione S-transferase subunit induction patterns of brussels sprouts, allyl isothiocyanate and goitrin in rat liver and small intestinal mucosa: A new approach for the identification of inducing xenobiotics. Food Chem Toxicol 1990;28:81–88.
- Brands CM, Alink GM, van Boekel MAJS, Jongen WMF: Mutagenicity of heated sugar-casein systems: Effect of the Maillard Reaction. J Agric Food Chem 2000; in press.
- Brownlee M: Advanced protein glycosylation in diabetes and aging. Annu Rev Med 1995;46:271–278.
- Brüggemann J, Erbersdobler HF: Untersuchungen zur analytischen und physiologischen Charakterisierung der Aminosä&;acute;urenschädigung bei Hitzebehandlung von Nahrungs- und Futtermitteln. Z Tierphysiol Tierernähr Futtermittelk 1968;24:55–67.
- De Bry L: Anthropological implications of the Maillard reaction: An insight; in Labuza TP, Reineccius GA, Monnier VM, O’Brien J, Baynes JW (eds): Maillard Reactions in Chemistry, Food and Health. Cambridge, The Royal Society of Chemistry 1994, pp 28–36.
- Drusch S, Faist V, Erbersdobler HF: Determination of carboxymethyllysine in milk products by a modified reversed-phase-HPLC method. Food Chem 1998;65:537–543.
- Erbersdobler HF, Dümmer H: Untersuchungen zur analytischen und physiologischen Charakterisierung der Aminosäurenschädigung bei Hitzebehandlung. Z Tierphysiol, Tierernähr Futtermittelk 1971;28:224–231.
- Erbersdobler HF, Gunsser I, Weber G: Abbau von Fruktoselysin durch die Darmflora, Zentralbl Vet Med 1970;A17:573–575.
- Erbersdobler HF: The biological significance of carbohydrate-lysine crosslinks during heat-treatment of food proteins; in Friedman M (ed): Protein Crosslinking: Nutritional and Medical Consequences. New York, Plenum Press, 1977, pp 367–378.
- Erbersdobler HF, Brandt A, Scharrer E, von Wangenheim B: Transport and metabolism studies with fructose amino acids. Prog Fd Nutr Sci 1981;5:257–263.
- Erbersdobler HF, Purwing U, Bossen M, Trautwein EA: Urinary excretion of fructoselysine in human volunteers and diabetic patients; in Fujimaki M, Namiki N, Kato H (eds): Amino-Carbonyl Reactions in Food and Biological Systems. Developments in Food Science 13. Tokyo Elsevier, 1986, pp 503–508.
- Erbersdobler HF, Gross A, Klusman U, Schlecht K: Absorption and metabolism of heated protein-carbohydrate mixtures in humans; in Friedman M (ed): Absorption and Utilisation of Amino Acids. Boca Raton, CRC Press, 1989, vol III. pp 91–95.
- Erbersdobler HF, Weber G, Gunsser I: Untersuchungen zur analytischen und physiologischen Charakterisierung der Aminosäurenschädigung. Z Tierphysiol Tierernähr Futtermittelk 1972;29:325–334.
- Faist V, Wenzel E, Tasto S, Müller C, Erbersdobler HF: Tissue specific induction of phase I and II xenobiotic enzymes and oxygen free radical metabolism in rats fed alkali-treated protein containing high levels of lysinolanine. FASEB J 1998;27:A1268.
- Finch C, Cohen D: Aging, metabolism and Alzheimer’s disease: Review and hypotheses. Exp Neurol 1997;143:82–102.
- Finot PA: Chemical modifications of the milk proteins during processing and storage. Nutritional, metabolic and physiological consequences. Kieler Milchwissenschaftl Forschungsber 1983;35:357–369.
- Finot PA: Metabolism and physiological effects of Maillard reaction products; in Finot PA, Aeschbacher HU, Hurrell RF, Liardon R (eds): The Maillard Reaction in Food Processing, Human Nutrition and Physiology. Basel Birkhäuser, 1990; pp 258–272.
- Finot PA, Furniss DE: Metabolic transit and toxicity of Maillard reaction products; in Baynes JW, Monnier VM (eds): The Maillard Reaction in Ageing, Diabetes and Nutrition. Proc NIH Conf Bethesda. New York, Liss, 1989, pp 343–358.
- Finot PA, Magnenat E: Metabolic transit of early and advanced Maillard products. Prog Fd Nutr Sci 1981;5:193–207.
- Furniss DE, Hurrell RF, Finot PA: Modification of urinary zinc excretion in the rat associated with the feeding of Maillard reaction products. Acta Pharmacol Toxicol 1986;59:188–190.
- Gerhardinger C, Marion MS, Rovner A, Glomb M, Monnier V: Novel degradation pathway of glycated amino acids into free fructosamine by a Pseudomonas sp. soil strain extract. J Biol Chem 1995;270:218–224.
- Germond JE, Philippossian G, Richli U, Bracco I, Arnaud MJ: Rapid and complete urinary elimination of [14C]-5-hydroxymethyl-2-furaldehyde administered orally or intravenously to rats. J Toxicol Environ Health 1987;22:79–89.
- Hayase F, Hirashima S, Okamoto G, Kato H: Scavenging of active oxygens by melanoidin; in Finot PA, Aeschbacher HU, Hurrell RF, Liardon R (eds): The Maillard Reaction in Food Processing, Human Nutrition and Physiology, Basel Birkhäuser, 1990, pp 361–366.
- He C, Sabol J, Mitsuhashi T, Vlassara H: Dietary glycotoxins. Inhibition of reactive products by aminoguanidine facilitates renal clearance and reduces tissue sequestration. Diabetes 1999;48:1308–1315.
- Hiramoto K, Nasuhara A, Michikoshi K, Kato T, Kikuguwa K: DNA strand-breaking activity and mutagenicity of 2,3-dihydro-3,5-dihydroxy-6-methyl-4H-pyran-4-one (DDMP), a Maillard reaction product of glucose and glycine. Mutat Res 1997;395:47–56.
- Hodge JE: Chemistry of browning reactions in model systems. J Agric Food Chem 1953;1:928–943.
- Homma S, Fujimaki M: Growth response of rats fed a diet containing nondialyzable melanoidin. Prog Fd Nutr Sci 1981;5:209–216.
- Horikoshi M, Ohmura M, Gomyo T, Kuwabara Y, Ueda A: Effects of browning products on the intestinal microflora of the rat. Prog Fd Nutr Sci 1981;5:223–228.
- Jägerstad M, Skog K, Arvidsson P, Solyakov A: Chemistry, formation and occurrence of genotoxic heterocyclic amines identified in model systems and cooked foods. Z Lebensm Untersuch Forsch 1998;A207:419–427.
- Kaanane A, Labuza TP: The Maillard reaction in foods. Prog Clin Biol Res 1989;304:301–327.
- Kato H, Shin HS, Liang ZQ, Nishimura T, Hayase F: 2-Oxoaldehyde metabolising enzymes in animal tissues; in Labuza TP, Reineccius GA, Monnier VM, O’Brien J, Baynes JW (eds): Maillard Reactions in Chemistry, Food and Health, Cambridge, Royal Society of Chemistry, 1994, pp 309–313.
- Kato H, van Chuyen N, Shinoda T, Sekiya F, Hayase F: Metabolism of 3-deoxyglucosone, an intermediate compound in the Maillard reaction, administered orally or intravenously to rats. Biochim Biophys Acta 1990;1035:71–76.
- Kim SB, Hayase F, Kato H: Desmutagenic effects of melanoidins against amino acid and protein pyrolysates; in Fujimaki M, Namiki N, Kato H (eds): Amino-Carbonyl-Reaction in Food and Biological Systems. Developments in Food Science 13. Tokyo, Elsevier, 1986 pp 383–392.
- Kimiagar M, Lee T-C, Chichester CO: Long-term feeding effects of browned egg albumin to rats. J Agric Food Chem 1980;28:150–155.
- Kitts DD, Wu CH, Powrie WD: Effect of glucose-lysine Maillard reaction products fractions on tissue xenobiotic enzyme systems. J Agric Food Chem 1993;41:2359–2363.
- Knecht KJ, Dunn JA, McFarland KF, McCance DR, Lyons TJ, Thorpe SR, Baynes W: Effect of diabetes and aging on carboxymethyllysine levels in human urine. Diabetes 1991;40:190–196.
- Kohlmeier L, Simonsen N, Mottus K: Dietary modifiers of carcinogenesis. Environ Hlth Perspect 1995;103:177–184.
- Koschinsky T, He C-J, Mitsuhashi T, Bucala R, Liu C, Buenting C, Heitmann K, Vlassara H: Orally absorbed reactive glycation products (glycotoxins): An environmental risk factor in diabetic retinopathy. Proc Natl Acad Sci USA 1997;94:6474–6479.
- Ledl F, Beck J, Sengl M, Osiander H, Estendorfer S, Severin T, Huber B: Chemical pathways of the Maillard reaction. Prog Clin Biol Res 1989;304:23–42.
- Lee TC, Kimiagar M, Pintauro SJ, Chichester CO: Physiological and safety aspects of Maillard browning of foods. Prog Fd Nutr Sci 1981;5:1–6.
- Lee K, Erbersdobler HF: Balance experiments on human volunteers with ε-fructoselysine (FL) and lysinoalanine (LAL); in Labuza TP, Reineccius GA, Monnier VM, O’Brien J, Baynes JW (eds): Maillard Reactions in Chemistry, Food and Health, Cambridge, Royal Society of Chemistry, 1994, pp 358–363.
- Liardon R, De Weck-Godard D, Philippossian G, Finot PA: Identification of Nε-carboxymethyllysine: A new Maillard reaction product in rat urine. J Agric Food Chem 1987;35:427–431.
- Lingnert H, Eriksson CE: Antioxidative effect of Maillard reaction products. Prog Fd Nutr Sci 1981;5:453–466.
- Mauron J: The Maillard reaction in food: A critical review from the nutritional standpoint. Prog Fd Nutr Sci 1981;5:5–35.
- McCance DR, Dyer DG, Dunn JA, Bailie KE, Thorpe SR, Baynes JW, Lyons TJ: Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J Clin Invest 1993;91:2470–2478.
- Monnier VM, Sell DR, Nagaraj RH, Miyata S, Grandhee S, Odetti P, Ibrahim SA: Maillard reaction-mediated molecular damage to extracellular matrix and other tissue proteins in diabetes, aging, and uremia. Diabetes 1992;41:S36–S41.
- Mori B, Nakatsuji H: Utilization in rats of 14C-L-lysine labeled casein browned by amino-carbonyl reaction. Agric Biol Chem 1977;41:345–350.
- Münch G, Schinzel R, Loske C, Wong A, Durany N, Li JJ, Vlassara H, Smith MA, Perry G, Riederer P: Alzheimer’s disease-synergistic effects of glucose deficit, oxidative stress and advanced glycation endproducts. J Neural Transm 1998;105:439–461.
- Nair BM, Öste R, Asp NG, Pernemalm PA: Absorption and distribution of a C14-glucose lysine reaction mixture in the rat. Prog Fd Nutr 1981;5:217–222.
- Neumann A, Schinzel R, Palm D, Riederer P, Münch G: High molecular weight hyaluronic acid inhibits advanced glycation endproduct-induced NF-kappaB activation and cytokine expression. FEBS Lett 1999;453:283–287.
- Niederweiser A, Giliberti P, Matasovic A: Nε-L-deoxyfructosyl-lysine in urine after ingestion of a lactose-free, glucose-containing milk formula. Pediatr Res 1975;9:867–872.
- O’Brien J, Morrissey PA: Nutritional and toxicological aspects of the Maillard browning reaction in foods. Crit Rev Fd Sci Nutr 1989;28:211–248.
- O’Brien J, Walker R: Toxicological effects of dietary Maillard reaction products in the rat. Fd Chem Toxic 1988;26:775–783.
- Öste RE, Dahlquist A, Sjöström H, Norén O, Miller R: Effect of Maillard reaction products on protein digestion: In vitro studies. J Agric Food Chem 1986;34:354–358.
- Öste RE, Miller R, Sjöström H, Norén O: Effect of Maillard reaction products on protein digestion. Studies on pure compounds. J Agric Food Chem 1987;35:938–942.
- Pintauro SJ, Lee TC, Chichester CO: Physiological, toxicological and nutritional aspects of various Maillard browned products; in Waller R, Feather MS (eds): The Maillard Reaction in Foods and Nutrition. New York, American Chemical Society, 1983; pp 379–407.
- Pintauro SJ, Lucchina LA: Effects of Maillard browned egg albumin on drug-metabolizing enzyme systems in the rat. Food Chem Toxicol 1987;25:369–372.
- Powrie WD, Wu CH, Molund VP: Browning reaction systems as sources of mutagens and antimutagens. Environ Hlth Perspect 1986;67:47–54.
- Powrie WD, Wu CH, Rosin MP, Stich HF: Clastrogenic and mutagenic activities of Maillard reaction model systems. J Fd Sci 1981;46:1433–1438.
- Prochaska HJ, Talalay P: Regulatory mechanisms of monofunctional and bifunctional anticarcinogenic enzyme inducers in murine liver. Cancer Res 1988;48:4776–4782.
- Ragot FIJ, Russell GF, Schneeman BO: Effect of Maillard reaction products on bile acid binding, plasma and hepatic lipids and weight of gastrointestinal organs. J Agric Food Chem 1992;40:1634–1640.
- Rahimtula AD, Zachariah PK, O’Brien PJ: The effects of antioxidants on the metabolism and mutagenicity of benzo[a]pyrene in vitro. Biochem J 1977;164:473–475.
- Reiser KM: Influence of age and long-term dietary restriction on enzymatically mediated crosslinks and nonenzymatic glycation of collagen in mice. J Gerontol 1994;49:B71–B79.
- Sgarbieri VC, Amaya J, Tanaka M, Chichester CO: Nutritional consequences of the Maillard reaction. Amino acid bioavailability from fructose-leucine and fructose-tryptophan in the rat. J Nutr 1973;103:657–663.
- Schmidt AM, Hori O, Brett J, Yan S-D, Wautier JL, Stern D: Cellular receptor for advanced glycation end products: Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions. Atheroscler Thromb 1994;14:1521–1528.
- Sinha R, Rothman N, Brown ED, Mark SD, Hoover RN, Caporaso NE, Levander OA, Knize MG, Lang NP, Kadlubar FF: Pan-fried meat containing high levels of heterocyclic aromatic amines but low levels of polycyclic aromatic hydrocarbons induces cytochrome P4501A2 activity in humans. Cancer Res 1994;54:6154–6159.
- Skog K, Johansson M, Jägerstad M: Carcinogenic heterocyclic amines in model systems and cooked foods: A review on formation, occurrence and intake. J Food Chem Toxicol 1998;36:879–896.
- Tanaka M, Lee TC, Chichester CO: Nutritional consequences on the Maillard reaction: The absorption of fructose-L-tryptophan in the large intestine of the rat. J Nutr 1975;105:989–994.
- Thornalley PJ: Cell activation by glycated proteins. AGE receptors, receptor recognition factors and functional classification of AGEs. Cell Mol Biol (Noisy-le-Grand) 1998;44:1013–1023.
- Valle-Riestra J, Barnes R: Digestion of heat-damaged egg albumen by the rat. J Nutr 1969;100:873–882.
- Vlassara H, Brownlee M, Cerami A: Accumulation of diabetic rat peripheral nerve myelin by macrophages increases with extent and duration of non-enzymatic glycosylation. J Med 1984;160:197–207.
- Vlassara H, Brownlee M, Cerami A: Recognition and uptake of human diabetic peripheral nerve myelin by macrophages. Diabetes 1985;34:553–557.
- Vlassara H, Brownlee M, Cerami A: Novel macrophage receptor for glucose-modified proteins is distinct from previously described scavenger receptors. J Exp Med 1986;164:1301–1309.
- Weisburger JH: Mechanisms of macronutrient carcinogenesis; in Micozzi MS, Moon TE (eds): Macronutrients: Investigating Their Role in Cancer. New York, Decker, 1992, pp 3–31.
- Wells-Knecht KJ, Zyzak DV, Litchfield JE, Thorpe SR, Baynes JW: Mechanism of autoxidative glycosylation – identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry 1995;34:3702–3709.
- Wenzel E, Faist V, Tasto S, Erbersdobler HF: Einfluss von freiem und proteingebundenem Nε-Carboxymethyllysine auf die NADPH-Cytochrom c-Reduktase und die Glutathion-S-Transferase in vitro und in vivo. Proc Germ Nutr Soc 2000; in press.
- Wadman SK, De Bree PK, Van Sprang FJ, Kamerling JP, Haverkamp J, Vliegenthart JFG: Nε-carboxymethyllysine, a constituent of human urine. Clin Chim Acta 1975;59:313–320.
- Yan SD, Schmidt AM, Anderson GM, Zhang J, Brett J, Zou YS, Pinsky D, Stern D: Enhanced cellular oxidant stress by the interaction of advanced glycation and products with their receptors/binding proteins. J Biol Chem 1994;269:9889–9897.
- Yoshimura Y, Iijima T, Watanabe T, Nakazawa H: Antioxidative effect of Maillard reaction products using glucose-glycine model system. J Agric Food Chem 1997;45:4106–4109.
- Zyzak DV, Richardson JM, Thorpe SR, Baynes JW: Formation of reactive intermediates from Amadori compounds and physiological conditions. Arch Biochem Biophys 1995;316:547–554.