The Maillard reaction in the human body. The main discoveries and factors that affect glycation;La réaction de Maillard dans le corps humain. Découvertes majeures et facteurs qui affectent la glycation

Pathologie Biologie

Volumn 58, Issue 3, 2010, Pages 214-219

  Tessier, F J ^a  

^a INSTITUT POLYTECHNIQUE LASALLE BEAUVAIS   (France)

Author keywords

Advanced glycation end products (AGE); Aging; Diabetes; Glycation; Maillard reaction

Indexed keywords

ADVANCED GLYCATION END PRODUCT; CARBONYL DERIVATIVE; CELL PROTEIN;

AGING; ARTICLE; EXTRACELLULAR MATRIX; GLYCATION; HUMAN; IN VIVO STUDY; MEMBRANE PERMEABILITY; PROTEIN METABOLISM;

AGING; AMINO ACIDS; ANTIGENS, NEOPLASM; DIABETES MELLITUS; EXTRACELLULAR MATRIX; FOOD; FREE RADICALS; GLUCOSE; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMANS; LYSINE; MAILLARD REACTION; MITOGEN-ACTIVATED PROTEIN KINASES; MONOSACCHARIDES; OXIDATION-REDUCTION; PROTEIN CARBONYLATION; PROTEINS;

EID: 77953621114     PISSN: 03698114     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.patbio.2009.09.014     Document Type: Article

References (83)

1. Medvedev Z.A. An attempt at a rational classification of theories of ageing. Biol Rev 1990, 65:375-398.
2. Yin D., Chen K. The essential mechanisms of aging: Irreparable damage accumulation of biochemical side-reactions. Exp Gerontol 2005, 40:455-465.
3. Soskić V., Groebe K., Schrattenholz A. Nonenzymatic posttranslational protein modifications in ageing. Exp Gerontol 2008, 43:247-257.
4. Harman D. The free radical theory of aging. Antioxid Redox Signal 2003, 5:557-561.
5. Baynes J.W. From life to death--the struggle between chemistry and biology during aging: the Maillard reaction as an amplifier of genomic damage. Biogerontology 2000, 1:235-246.
6. Maillard L.C. Action des acides aminés sur les sucres: formation des mélanoïdines par voie méthodique. C R Acad Sci 1912, 154:66-68.
7. Maillard L.C. Genèse des matières protéiques et des matières humiques - Action de la glycérine et des sucres sur les acides aminés 1913, 1 volume in 8:XI. Masson & Cie.
8. Hodge J.E. Chemistry of browning reactions in model systems. J Agric Food Chem 1953, 1:928-943.
9. Yatscoff R.W., Tevaarwerk G.J.M., MacDonald J.C. Quantification of nonenzymically glycated albumin and total serum protein by affinity chromatography. Clin Chem 1984, 30:446-449.
10. Monnier V.M., Cerami A. Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. Science 1981, 211:491-493.
11. Monnier V.M. Intervention against the Maillard reaction in vivo. Arch Biochem Biophys 2003, 419:1-15.
12. Baynes J.W., Thorpe S.R. Glycoxidation and lipoxidation in atherogenesis. Free Radic Biol Med 2000, 28:1708-1716.
13. Brownlee M., Vlassara H., Cerami A. Nonenzymatic glycosylation and the pathogenesis of diabetic complications. Ann Intern Med 1984, 101:527-537.
14. Kunkel H.G., Wallenius G. New hemoglobin in normal adult blood. Science 1955, 122:288.
15. Rahbar S. An abnormal hemoglobin in red cells of diabetics. Clin Chim Acta 1968, 22:296-298.
16. Roth M. Glycated hemoglobin", not "glycosylated" or "glucosylated" Clin Chem 1983, 29:1991.
17. Cerami A. Hypothesis: glucose as a mediatoir of aging. J Am Geriatr Soc 1985, 33:626-634.
18. Ahmed M.U., Thorpe S.R., Baynes J.W. Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J Biol Chem 1986, 261:4889-4894.
19. Dunn J.A., Patrick J.S., Thorpe S.R., Baynes J.W. Oxidation of glycated proteins: age-dependent accumulation of N epsilon-(carboxymethyl)lysine in lens proteins. Biochemistry 1989, 28:9464-9468.
20. Dunn J.A., McCance D.R., Thorpe S.R., Lyons T.J., Baynes J.W. Age-dependent accumulation of N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)hydroxylysine in human skin collagen. Biochemistry 1991, 30:1205-1210.
21. Wadman S.K., De Bree P.K., Van Sprang F.J., Kamerling J.P., Haverkamp J., Vliegenthart J.F.G. N-(Carboxymethyl)lysine, a constituent of human urine. Clin Chim Acta 1975, 59:313-320.
22. Thorpe S.R., Baynes J.W. CML: a brief history. Int Congress Series 2002, 1245:91-99.
23. Sell D.R., Monnier V.M. Structure elucidation of a senescence cross-link from human extracellular matrix: implication of pentoses in the aging process. J Biol Chem 1989, 264:21597-21602.
24. Monnier V.M., Vishwanath V., Frank K.E., Elmets C.A., Dauchot P., Kohn R.R. Relation between complications of type I diabetes mellitus and collagen-linked fluorescence. N Engl J Med 1986, 314:403-408.
25. Matiacevich S.B., Santagapita P.R., Buera M.P. Fluorescence from the Maillard Reaction and its potential applications in food science. Crit Rev Food Sci Nutr 2005, 45:483-495.
26. Hartog J.W.L., DeVries A.P.J., Lutgers H.L., Meerwaldt R., Huisman R.M., Van Son W.J., et al. Accumulation of advanced glycation end products, measured as skin autofluorescence, in renal disease. Ann NY Acad Sci 2005, 1043:299-307.
27. Biemel K.M., Reihl O., Conrad J., Lederer M.O. Formation pathways for lysine-arginine cross-links derived from hexoses and pentoses by Maillard processes: unraveling the structure of a pentosidine precursor. J Biol Chem 2001, 276:23405-23412.
28. Sell D.R., Biemel K.M., Reihl O., Lederer M.O., Strauch C.M., Monnier V.M. Glucosepane is a major protein cross-link of the senescent human extracellular matrix. Relationship with diabetes. J Biol Chem 2005, 280:12310-12315.
29. Dyer D.G., Blackledge J.A., Katz B.M., Hull C.J., Adkisson H.D., Thorpe S.R., et al. The Maillard reaction in vivo. Z Ernahrungswiss 1991, 30:29-45.
30. Namiki M., Hayashi T. A new mechanism of the Maillard reaction involving sugar fragmentation and free radical formation. ACS Symposium 1983, Series 215. American Chemical Society, Washington DC. G.R. Waller, M.S. Feather (Eds.).
31. Wolff S.P., Jiang Z.Y., Hunt J.V. Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Radic Biol Med 1991, 10:339-352.
32. Buettner G.R. The pecking order of free radicals and antioxidants: lipid peroxidation, alpha-tocopherol and ascorbate. Arch Biochem Biophys 1993, 300:535-543.
33. Requena J.R., Fu M.X., Ahmed M.U., Jenkins A.J., Lyons T.J., Thorpe S.R. Lipoxidation products as biomarkers of oxidative damage to proteins during lipid peroxidation reactions. Nephrol Dial Transplant 1996, 11:48-53.
34. Brownlee M., Vlassara H., Kooney A., Ulrich P., Cerami A. Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 1986, 232:1629-1632.
35. Intervention against the Maillard reaction in diabetes and aging. Special issue of the Archives of Biochemistry and biophysics, 2003;419(1):1-97, Edited by V.M. Monnier.
36. Vlassara H., Brownlee M., Cerami A. High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: A potential mechanism for the removal of senescent macromolecules. Proc Natl Acad Sci U S A 1985, 82:5588-5592.
37. Ramasamy R., Yan S.F., Herold K., Clynes R., Schmidt A.M. Receptor for advanced glycation end products: fundamental roles in the inflammatory response: winding the way to the pathogenesis of endothelial dysfunction and atherosclerosis. Ann N Y Acad Sci 2008, 1126:7-13.
38. Cerami C., Founds H., Nicholl I., Mitsuhashi T., Giordana D., Vanpatten S., et al. Tobacco smoke is a source of toxic reactive glycation products. Proc Natl Acad Sci U S A 1997, 94:13915-13920.
39. Koschinsky T., He C.J., Mitsuhashi T., Bucala R., Liu C., Buenting C., et al. Orally absorbed reactive glycation products (glycotoxins): An environmental risk factor in diabetic nephropathy. Proc Natl Acad Sci U S A 1997, 94:6474-6479.
40. Cai W., He J.C., Zhu L., Chen X., Zheng F., Striker G.E., et al. Oral glycotoxins determine the effects of calorie restriction on oxidant stress. age-related diseases, and lifespan. Am J Pathol 2008, 173:327-336.
41. Olufemi S., Talwar D., Robb D.A. The relative extent of glycation of haemoglobin and albumin. Clin Chim Acta 1987, 163:125-136.
42. Tessier F., Obrenovich M., Monnier V.M. Structure and mechanism of formation of human lens fluorophore LM-1. Relationship to vesperlysine A and the advanced Maillard reaction in aging, diabetes, and cataractogenesis. J Biol Chem 1999, 274:20796-20804.
43. Dyer D.G., Dunn J.A., Thorpe S.R., Bailie K.E., Lyons T.J., McCance D.R., et al. Accumulation of Maillard reaction products in skin collagen in diabetes and aging. J Clin Invest 1993, 91:2463-2469.
44. Sell D.R., Lane M.A., Johnson W.A., Masoro E.J., Mock O.B., Reiser K.M., et al. Longevity and the genetic determination of collagen glycoxidation kinetics in mammalian senescence. Proc Natl Acad Sci U S A 1996, 93:485-490.
45. Verzijl N., DeGroot J., Thorpe S.R., Bank R.A., Shaw J.N., Lyons T.J., et al. Effect of collagen turnover on the accumulation of advanced glycation end products. J Biol Chem 2000, 275:39027-39031.
46. Bunn H.F., Haney D.N., Kamin S., Gabbay K.H., Gallop P.M. The biosynthesis of human hemoglobin A1c. Slow glycosylation of hemoglobin in vivo. J Clin Invest 1976, 57:1652.
47. Youssef D., El Abbassi A., Jordan R.M., Peiris A.N. Fructosamine - an underutilized tool in diabetes management: case report and literature review. Tenn Med 2008, 101:31-33.
48. Murtiashaw M.H., Baynes J.W., Thorpe S.R. Albumin catabolism in diabetic rats. Arch Biochem Biophys 1983, 225:256-262.
49. Brownlee M. Negative consequences of glycation. Metabolism 2000, 49:9-13.
50. Brown S.M., Smith D.M., Alt N., Thorpe S.R., Baynes J.W. Tissue-specific variation in glycation of proteins in diabetes: evidence for a functional role of amadoriase enzymes. Ann N Y Acad Sci 2005, 1043:817-823.
51. Alt N., Carson J.A., Alderson N.L., Wang Y., Nagai R., Henle T., et al. Chemical modification of muscle protein in diabetes. Arch Biochem Biophys 2004, 425:200-206.
52. Wada R., Yagihashi S. Role of advanced glycation end products and their receptors in development of diabetic neuropathy. Ann N Y Acad Sci 2005, 1043:598-604.
53. Cohen G., Riahi Y., Alpert E., Gruzman A., Sasson S. The roles of hyperglycaemia and oxidative stress in the rise and collapse of the natural protective mechanism against vascular endothelial cell dysfunction in diabetes. Arch Physiol Biochem 2007, 113:259-267.
54. Stevens A. The contribution of glycation to cataract formation in diabetes. J Am Optom Assoc 1998, 69:519-530.
55. Fukami K., Yamagishi S., Ueda S., Okuda S. Role of AGEs in diabetic nephropathy. Curr Pharm Des 2008, 14:946-952.
56. Smith C., Marks A., Lieberman M. Marks' basic medical biochemistry: a clinical approach 2004, Lippincott Williams and Wilkins, Philadelphia.
57. Ashoor S.H., Zent J.B. Maillard browning of common amino acids and sugars. J Food Sci 1984, 49:1206-1207.
58. Kwak E.J., Lim S.I. The effect of sugar, amino acid, metal ion, and NaCl on model Maillard reaction under pH control. Amino Acids 2004, 27:85-90.
59. Swamy M.S., Tsai C., Abraham A., Abraham E.C. Glycation mediated lens crystallin aggregation and cross-linking by various sugars and sugar phosphates in vitro. Exp Eye Res 1993, 56:177-185.
60. Bunn H.F., Higgins P.J. Reaction of monosaccharides with proteins: possible evolutionary significance. Science 1981, 213:222-224.
61. Beisswenger P.J., Szwergold B.S., Yeo K.T. Glycated proteins in diabetes. Clin Lab Med 2001, 21:53-78.
62. Shinohara M., Thornalley P.J., Giardino I., Beisswenger P., Thorpe S.R., Onorato J., et al. Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis. J Clin Invest 1998, 101:1142-1147.
63. Wells-Knecht K.J., Lyons T.J., McCance D.R., Thorpe S.R., Feather M.S., Baynes J.W. 3-Deoxyfructose concentrations are increased in human plasma and urine in diabetes. Diabetes 1994, 43:1152-1156.
64. Odani H., Shinzato T., Matsumoto Y., Usami J., Maeda K. Increase in three alpha,beta-dicarbonyl compound levels in human uremic plasma: specific in vivo determination of intermediates in advanced Maillard. Biochem Biophys Res Commun 1999, 256:89-93.
65. Hayashi T., Shibamoto T. Analysis of methylglyoxal in foods and beverages. J Agric Food Chem 1985, 33:1090-1093.
66. Reiser K.M., Amigable M.A., Last J.A. Nonenzymatic glycation of type I collagen. The effects of aging on preferential glycation sites. J Biol Chem 1992, 267:24207-24216.
67. Casey E.B., Zhao H.R., Abraham E.C. Role of glycine 1 and lysine 2 in the glycation of bovine γB-crystallin. J Biol Chem 1995, 270:20781-20786.
68. Shapiro R., McManus M.J., Zalut C., Bunn H.F. Sites of nonenzymatic glycosylation of human hemoglobin A. J Biol Chem 1980, 255:3120-3127.
69. Ames J.M. Mass spectrometry to detect the site specificity of advanced glycation/lipoxidation end-product formation on protein: some challenges and solutions. Biochem Soc Trans 2008, 36:1051-1054.
70. Watkins N.G., Thorpe S.R., Baynes J.W. Glycation of amino groups in protein. Studies on the specificity of modification of RNase by glucose. J Biol Chem 1985, 260:10629-10636.
71. Iberg N., Fluckinger R. Nonenzymatic glycosylation of albumin in vivo: Identification of multiple glycosylation sites. J Biol Chem 1986, 261:13542-13545.
72. Ahmed N., Thornalley P.J. Peptide mapping of human serum albumin modified minimally by methylglyoxal in vitro and in vivo. Ann N Y Acad Sci 2005, 1043:260-266.
73. Day J.F., Ingebretsen C.G., Ingebretsen W.R., Baynes J.W., Thorpe S.R. Nonenzymatic glucosylation of serum proteins and hemoglobin: response to changes in blood glucose levels in diabetic rats. Diabetes 1980, 29:524-527.
74. Delpierre G., Rider M.H., Collard F., Stroobant V., Vanstapel F., Santos H., et al. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes 2000, 49:1627-1634.
75. Szwergold B.S., Howell S., Beisswenger P.J. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. Diabetes 2001, 50:2139-2147.
76. Szwergold B.S., Beisswenger P.J. Enzymatic deglycation--a new paradigm or an epiphenomenon?. Biochem Soc Trans 2003, 31:1428-1432.
77. Morgan P.E., Dean R.T., Davies M.J. Inactivation of cellular enzymes by carbonyls and protein-bound glycation/glycoxidation products. Arch Biochem Biophys 2002, 403:259-269.
78. Zeng J., Dunlop R.A., Rodgers K.J., Davies M.J. Evidence for inactivation of cysteine proteases by reactive carbonyls via glycation of active site thiols. Biochem J 2006, 398:197-206.
79. Kent M.J.C., Light N.B., Bailey A.J. Evidence for glucose-mediated covalent cross-linking of collagen after glycosylation in vitro. Biochem J 1985, 225:745-752.
80. Brock J.W., Hinton D.J., Cotham W.E., Metz T.O., Thorpe S.R., Baynes J.W., et al. Proteomic analysis of the site specificity of glycation and carboxymethylation of ribonuclease. J Proteome Res 2003, 2:506-513.
81. Vlassara H., Palace M.R. Glycoxidation: the menace of diabetes and aging. Mt Sinai J Med 2003, 70:232-241.
82. Baynes J.W. The role of AGEs in aging: causation or correlation. Exp Gerontol 2001, 36:1527-1537.
83. Kristal B.S., Yu B.P. An emerging hypothesis: synergistic induction of aging by free radicals and Maillard reactions. Gerontology 1992, 47:B107-B114.