Journal Home > Volume 13 , Issue 3
Food Science and Human Wellness 2024, 13(3): 1118-1134 https://doi.org/10.26599/FSHW.2022.9250094
Review Article | Open Access | Issue | Published: 08 February 2024

Effects of Maillard reaction and its product AGEs on aging and age-related diseases

Show Author's Information Huan Peng,,  Yuqi Gao,  Chenye Zeng,  Rui Hua,  Yannan Guo,  Yida Wang,  Zhao Wang( )
Protein Science Key Laboratory of the Ministry of Education, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China

Peer review under responsibility of Tsinghua University Press.

Keywords:
Maillard reaction, Advanced glycation end products, Physiologic aging, Pathological aging, Drug intervention
Cite this article:
Peng H, Gao Y, Zeng C, et al. Effects of Maillard reaction and its product AGEs on aging and age-related diseases. Food Science and Human Wellness, 2024, 13(3): 1118-1134. https://doi.org/10.26599/FSHW.2022.9250094
Download citation
EndNote(RIS)
BibTeX

2188

Views

640

Downloads

Citations

2

Crossref

1

WoS

1

Scopus

0

CSCD

Abstract Full text About this article

Maillard reaction (MR) is a non-enzymatic browning reaction commonly seen in food processing, which occurs between reducing sugars and compounds with amino groups. Despite certain advantages based on Maillard reaction products (MRPs) found in some food for health and storage application have appeared, however, the MR occurring in human physiological environment can produce advanced glycation end products (AGEs) by non-enzymatic modif ication of macromolecules such as proteins, lipids and nucleic acid, which could change the structure and functional activity of the molecules themselves. In this review, we take AGEs as our main object, on the one hand, discuss physiologic aging, that is, age-dependent covalent cross-linking and modif ication of proteins such as collagen that occur in eyes and skin containing connective tissue. On the other hand, pathological aging associated with autoimmune and inflammatory diseases, neurodegenerative diseases, diabetes and diabetic nephropathy, cardiovascular diseases and bone degenerative diseases have been mainly proposed. Based on the series of adverse effects of accelerated aging and disease pathologies caused by MRPs, the possible harm caused by some MR can be slowed down or inhibited by artif icial drug intervention,dietary pattern and lifestyle control. It also stimulates people’s curiosity to continue to explore the potential link between the MR and human aging and health, which should be paid more attention to for the development of life sciences.


menu
Abstract
Full text
Outline
About this article

Effects of Maillard reaction and its product AGEs on aging and age-related diseases

Show Author's information Huan Peng,, Yuqi Gao, Chenye Zeng, Rui Hua, Yannan Guo, Yida Wang, Zhao Wang( )
Protein Science Key Laboratory of the Ministry of Education, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China

Peer review under responsibility of Tsinghua University Press.

Abstract

Maillard reaction (MR) is a non-enzymatic browning reaction commonly seen in food processing, which occurs between reducing sugars and compounds with amino groups. Despite certain advantages based on Maillard reaction products (MRPs) found in some food for health and storage application have appeared, however, the MR occurring in human physiological environment can produce advanced glycation end products (AGEs) by non-enzymatic modif ication of macromolecules such as proteins, lipids and nucleic acid, which could change the structure and functional activity of the molecules themselves. In this review, we take AGEs as our main object, on the one hand, discuss physiologic aging, that is, age-dependent covalent cross-linking and modif ication of proteins such as collagen that occur in eyes and skin containing connective tissue. On the other hand, pathological aging associated with autoimmune and inflammatory diseases, neurodegenerative diseases, diabetes and diabetic nephropathy, cardiovascular diseases and bone degenerative diseases have been mainly proposed. Based on the series of adverse effects of accelerated aging and disease pathologies caused by MRPs, the possible harm caused by some MR can be slowed down or inhibited by artif icial drug intervention,dietary pattern and lifestyle control. It also stimulates people’s curiosity to continue to explore the potential link between the MR and human aging and health, which should be paid more attention to for the development of life sciences.

Keywords: Maillard reaction, Advanced glycation end products, Physiologic aging, Pathological aging, Drug intervention

References(230)

[1]

L.C. Maillard, Condensation des acides amines en presence de la glycerine; Cycloglycylglycine et polypeptides, CR Hebd. Seances Acad. Sci 153 (1911) 1078-1080.
Google Scholar
[2]

L.C. Maillard, Synthèse des matières humiques par action des acides aminés sur les sucres réducteurs, Ann. Chim. 6 (1916) 258-317.
Google Scholar
[3]

L.C. Maillard, Action des acids amines sur les sucres: Formation des melanoidines par voie methodique, CR Acad. Sci. 154 (1912) 66-68.
Google Scholar
[4]

C.J. Lintner, Color and aroma formation in dry malt, Z. ges. Brauw 35 (1912) 545-548.
Google Scholar
[5]

W. Ruckdeschel, Melanoidins and their occurrence in kiln malt, Z. ges. Brauw 37 (1914) 430-432.
Google Scholar
[6]

A. Schonberg, R. Moubacher, The Strecker degradation of α-amino acids, Chem. Rev. 50 (1952) 261-277. https://doi.org/10.1021/cr60156a002.
DOI Google Scholar
[7]

M. Amadori, Products of condensation between glucose and p-phenetidine, Atti Accad. Lincei 2 (1925) 337-342.
Google Scholar
[8]

K. Heyns, W. Koch, Formation of an amino sugar from D-fructose and ammonia, Z. Naturforsch 7 (1952) 486-488.
DOI Google Scholar
[9]

T.M. Wrodnigg, B. Eder, The Amadori and Heyns rearrangements: landmarks in the history of carbohydrate chemistry or unrecognized synthetic opportunities? Glycoscience 215 (2001) 115-152. https://doi.org/10.1007/3-540-44422-X_6.
DOI Google Scholar
[10]

F. Ledl, R. Schleicher, New aspects of the Maillard reaction in foods and in the human body, Angew. Chem. Int. Ed. Engl. 29 (2010) 565-594. https://doi.org/10.1002/anie.199005653.
DOI Google Scholar
[11]

F.D. Mills, B.G. Baker, J.E. Hodge, Amadori compounds as nonvolatile flavor precursors in processed food, J. Agric. Food Chem. 17 (1969) 723-727. https://doi.org/10.1021/jf60164a027.
DOI Google Scholar
[12]

V.V. Mossine, T.P. Mawhinney, 1-Amino-1-deoxy-D-fructose(“Fructosamine”) and its derivatives, Adv. Carbohydr. Chem. Biochem. 64 (2010) 291-402. https://doi.org/10.1016/S0065-2318(10)64006-1.
DOI Google Scholar
[13]

M. Namiki, Chemistry of Maillard reactions: recent studies on the browning reaction mechanism and the development of antioxidants and mutagens, Adv. Food Res. 32 (1988) 115-184. https://doi.org/10.1016/S0065-2628(08)60287-6.
DOI Google Scholar
[14]

Y. Luo, S. Li, C.T. Ho, Key aspects of Amadori rearrangement products as future food additives, Molecules 26 (2021) 4314. https://doi.org/10.3390/molecules26144314.
DOI Google Scholar
[15]

H. Cui, J. Yu, Y. Zhai, et al., Formation and fate of Amadori rearrangement products in Maillard reaction, Trends Food Sci. Technol. 115 (2021) 391-408. https://doi.org/10.1016/j.tifs.2021.06.055.
DOI Google Scholar
[16]

M.A.J.S. Van Boekel, Effect of heating on Maillard reactions in milk, Food Chem. 62 (1998) 403-414. https://doi.org/10.1016/S0308-8146(98)00075-2.
DOI Google Scholar
[17]

Z. Zhou, T. Langrish, A review of Maillard reactions in spray dryers, J. Food Eng. 305 (2021) 110615. https://doi.org/10.1016/j.jfoodeng.2021.110615.
DOI Google Scholar
[18]

M. Hellwig, T. Henle, Baking, ageing, diabetes: a short history of the Maillard reaction, Angew. Chem., Int. Ed. 53 (2014) 10316-10329. https://doi.org/10.1002/anie.201308808.
DOI Google Scholar
[19]

J.M. Ames, The Maillard reaction, Biochem. Food Proteins (1992) 99-153. https://doi.org/10.1007/978-1-4684-9895-0_4.
DOI Google Scholar
[20]

J.A. Gerrard, New aspects of an AGEing chemistry–recent developments concerning the Maillard reaction, Aust. J. Chem. 55 (2002) 299-310. https://doi.org/10.1071/CH02076.
DOI Google Scholar
[21]

W. Wang, Y.H. Bao, Y. Chen, Characteristics and antioxidant activity of water-soluble Maillard reaction products from interactions in a whey protein isolate and sugars system, Food Chem. 139 (2013) 355-361. https://doi.org/10.1016/j.foodchem.2013.01.072.
DOI Google Scholar
[22]

M.M Hashemi, M. Aminlari, M. Moosavinasab, Preparation of and studies on the functional properties and bactericidal activity of the lysozyme-xanthan gum conjugate, LWT-Food Sci. Technol. 57 (2014) 594-602. https://doi.org/10.1016/j.lwt.2014.01.040.
DOI Google Scholar
[23]

A.M. Hamdani, I.A. Wani, N.A. Bhat, et al., Effect of guar gum conjugation on functional, antioxidant and antimicrobial activity of egg white lysozyme, Food Chem. 240 (2018) 1201-1209. https://doi.org/10.1016/j.foodchem.2017.08.060.
DOI Google Scholar
[24]

L. Khadidja, C. Asma, B. Mahmoud, et al., Alginate/gelatin crosslinked system through Maillard reaction: preparation, characterization and biological properties, Polym. Bull. 74 (2017) 4899-4919. https://doi.org/10.1007/s00289-017-1997-z.
DOI Google Scholar
[25]

H.Y. Wang, H. Qian, W.R. Yao, Melanoidins produced by the Maillard reaction: structure and biological activity, Food Chem. 128 (2011) 573-584. https://doi.org/10.1016/j.foodchem.2011.03.075.
DOI Google Scholar
[26]

M. Daglia, A. Papetti, C. Aceti, et al., Isolation of high molecular weight components and contribution to the protective activity of coffee against lipid peroxidation in a rat liver microsome system, J. Agric. Food Chem. 56 (2008) 11653-11660. https://doi.org/10.1021/jf802018c.
DOI Google Scholar
[27]

A. Michalskaparda, M. Benavent, H. Zieliński, et al., Effect of bread making on formation of Maillard reaction products contributing to the overall antioxidant activity of rye bread, J. Cereal Sci. 48 (2008) 123-132. https://doi.org/10.1016/j.jcs.2007.08.012.
DOI Google Scholar
[28]

M.A. Martin, S. Ramos, R. Mateos, et al., Biscuit melanoidins of different molecular masses protect human HepG2 cells against oxidative stress, J. Agric. Food Chem. 57 (2009) 7250-7258. https://doi.org/10.1021/jf9006032.
DOI Google Scholar
[29]

D. Tagliazucchi, E. Verzelloni, A. Conte, Contribution of melanoidins to the antioxidant activity of traditional balsamic vinegar during aging, J. Food Biochem. 34 (2010) 1061-1078. https://doi.org/10.1111/j.1745-4514.2010.00349.x.
DOI Google Scholar
[30]

K. Brudzynski, D. Miotto, The recognition of high molecular weight melanoidins as the main components responsible for radical-scavenging capacity of unheated and heat-treated Canadian honeys, Food Chem. 125 (2011) 570-575. https://doi.org/10.1016/j.foodchem.2010.09.049.
DOI Google Scholar
[31]

F. Yan, X. Yu, Y. Jing, Optimized preparation, characterization, and antioxidant activity of chitooligosaccharide-glycine Maillard reaction products, J. Food Sci. Technol. 55 (2018) 712-720. https://doi.org/10.1007/s13197-017-2982-0.
DOI Google Scholar
[32]

C.L. Fernández, R.A. Fogar, M.M. Doval, et al., Antioxidant effect of bovine plasma proteins modified via maillard reaction on n-3 fortified beef patties, Food Nutr. Sci. 7 (2016) 671-681. https://doi.org/10.4236/fns.2016.78068.
DOI Google Scholar
[33]

K.X. Zhu, J. Li, M. Li, et al., Functional properties of chitosan-xylose Maillard reaction products and their application to semi-dried noodle, Carbohydr. Polym. 92 (2013) 1972-1977. https://doi.org/10.1016/j.carbpol.2012.11.078.
DOI Google Scholar
[34]

S. González-Mateo, M. González-SanJosé, P. Muñiz, Presence of Maillard products in Spanish muffins and evaluation of colour and antioxidant potential, Food Chem. Toxicol. 47 (2009) 2798-2805. https://doi.org/10.1016/j.fct.2009.08.015.
DOI Google Scholar
[35]

A. Serpen, V. Gokmen, Evaluation of the Maillard reaction in potato crisps by acrylamide, antioxidant capacity and color, J. Food Compos. Anal. 22 (2009) 589-595. https://doi.org/10.1016/j.jfca.2008.11.003.
DOI Google Scholar
[36]

H.J. Giroux, J. Houde, M. Britten, Use of heated milk protein-sugar blends as antioxidant in dairy beverages enriched with linseed oil, LWT-Food Sci. Technol. 43 (2010) 1373-1378. https://doi.org/10.1016/j.lwt.2010.05.001.
DOI Google Scholar
[37]

D. Tagliazucchi, E. Verzelloni, A. Conte, Effect of dietary melanoidins on lipid peroxidation during simulated gastric digestion: their possible role in the prevention of oxidative damage, J. Agric. Food Chem. 58 (2010) 2513-2519. https://doi.org/10.1021/jf903701h.
DOI Google Scholar
[38]

E. Verzelloni, D. Tagliazucchi, A. Conte, From balsamic to healthy:traditional balsamic vinegar melanoidins inhibit lipid peroxidation during simulated gastric digestion of meat, Food Chem. Toxicol. 48 (2010) 2097-2102. https://doi.org/10.1016/j.fct.2010.05.010.
DOI Google Scholar
[39]

M. Lindenmeier, V, Faist, T. Hofmann, Structural and functional characterization of pronyl-lysine, a novel protein modification in bread crust melanoidins showing in vitro antioxidative and phase Ⅰ/Ⅱ enzyme modulating activity, J. Agric. Food Chem. 50 (2002) 6997-7006. https://doi.org/10.1021/jf020618n.
DOI Google Scholar
[40]

V. Valls-Bellés, M.C. Torres, P. Muñiz, et al., The protective effects of melanoidins in adriamycin-induced oxidative stress in isolated rat hepatocytes, J. Sci. Food Agric. 84 (2004) 1701-1707. https://doi.org/10.1002/jsfa.1859.
DOI Google Scholar
[41]

H.Y. Wang, X. Yu, H. Qian, et al., Separation of antioxidant components from meat flavor and their antioxidant capacities, Food Sci. 31 (2010) 59-62.
Google Scholar
[42]

M. Patrignani, G.J. Rinaldi, C.E. Lupano, In vivo effects of Maillard reaction products derived from biscuits, Food Chem. 196 (2016) 204-210. https://doi.org/10.1016/j.foodchem.2015.09.038.
DOI Google Scholar
[43]

R. Dittrich, C. Dragonas, D. Kannenkeril, et al., A diet rich in Maillard reaction products protects LDL against copper induced oxidation ex vivo, a human intervention trial, Food Res. Int. 42 (2009) 1315-1322. https://doi.org/10.1016/j.foodres.2009.04.007.
DOI Google Scholar
[44]

I. Seiquer, B. Ruiz-Roca, M. Mesías, et al., The antioxidant effect of a diet rich in Maillard reaction products is attenuated after consumption by healthy male adolescents. In vitro and in vivo comparative study, J. Sci. Food Agric.88 (2008) 1245-1252. https://doi.org/10.1002/jsfa.3213.
DOI Google Scholar
[45]

J.A. Rufián-Henares, S.P. de la Cueva, Antimicrobial activity of coffee melanoidins–a study of their metal-chelating properties, J. Agric. Food Chem. 57 (2009) 432-438. https://doi.org/10.1021/jf8027842.
DOI Google Scholar
[46]

J. Wang, R. Wei, R. Song, Novel antibacterial peptides isolated from the maillard reaction products of half-fin anchovy (Setipinna taty) hydrolysates/glucose and their mode of action in Escherichia coli, Mar. Drugs 17 (2019) 47. https://doi.org/10.3390/md17010047.
DOI Google Scholar
[47]

J.A. Rufián-Henares, F.J. Morales, Microtiter plate-based assay for screening antimicrobial activity of melanoidins against E. coli and S. aureus, Food Chem. 111 (2008) 1069-1074. https://doi.org/10.1016/j.foodchem.2008.05.027.
DOI Google Scholar
[48]

J.A. Rurián-Henares, F.J. Morales, Antimicrobial activity of melanoidins against Escherichia coli is mediated by a membrane-damage mechanism, J. Agric. Food Chem. 56 (2008) 2357-2362. https://doi.org/10.1021/jf073300+.
DOI Google Scholar
[49]

U. Mueller, T. Sauer, I. Weigel, et al., Identification of H2O2 as a major antimicrobial component in coffee, Food Funct. 2 (2011) 265-272. https://doi.org/10.1039/C0FO00180E.
DOI Google Scholar
[50]

H. Einarsson, B.G. Snygg, C. Eriksson, Inhibition of bacterial growth by Maillard reaction products, J. Agric. Food Chem. 31 (1983) 1043-1047. https://doi.org/10.1021/jf00119a031.
DOI Google Scholar
[51]

K. Hiramoto, T. Kida, K. Kikugawa, Increased urinary hydrogen peroxide levels caused by coffee drinking, Biol. Pharm. Bull. 25 (2002) 1467-1471. https://doi.org/10.1248/bpb.25.1467.
DOI Google Scholar
[52]

A. Tauer, S. Elss, M. Frischmann, et al., Influence of thermally processed carbohydrate/amino acid mixtures on the fermentation by Saccharomyces cerevisiae, J. Agric. Food Chem. 52 (2004) 2042-2046. https://doi.org/10.1021/jf034995r.
DOI Google Scholar
[53]

V.T. Trang, H. Takeuchi, H. Kudo, et al., Antimicrobial activity of aminoreductone against Helicobacter pylori, J. Agric. Food Chem. 57 (2009) 11343-11348. https://doi.org/10.1021/jf9026876.
DOI Google Scholar
[54]

C. Hauser, U. Müller, T. Sauer, et al., Maillard reaction products as antimicrobial components for packaging films, Food Chem. 145 (2014) 608-613. https://doi.org/10.1016/j.foodchem.2013.08.083.
DOI Google Scholar
[55]

H.L. Chang, Y.C. Chen, F.J. Tan, Antioxidative properties of a chitosan-glucose Maillard reaction product and its effect on pork qualities during refrigerated storage, Food Chem. 124 (2011) 589-595. https://doi.org/10.1016/j.foodchem.2010.06.080.
DOI Google Scholar
[56]

T. Sun, Y. Qin, H. Xu, et al., Antibacterial activities and preservative effect of chitosan oligosaccharide Maillard reaction products on Penaeus vannamei, Int. J. Biol. Macromol. 105 (2017) 764-768. https://doi.org/10.1016/j.ijbiomac.2017.07.100.
DOI Google Scholar
[57]

T. Sun, Y. Qin, H. Xu, et al., Inhibitory effect of a tyrosine-fructose Maillard reaction product, 2,4-bis(p-hydroxyphenyl)-2-butenal on amyloid-β generation and inflammatory reactions via inhibition of NF-κB and STAT3 activation in cultured astrocytes and microglial BV-2 cells, J. Neuroinflamm.8 (2011) 1-15. https://doi.org/10.1186/1742-2094-8-132.
DOI Google Scholar
[58]

D. Qin, L. Li, J. Li, et al., A new compound isolated from the reduced ribose-tryptophan maillard reaction products exhibits distinct anti-inflammatory activity, J. Agric. Food Chem. 66 (2018) 6752-6761. https://doi.org/10.1021/acs.jafc.8b01561.
DOI Google Scholar
[59]

D. Kitts, X. Chen, H. Jing, Demonstration of antioxidant and anti-inflammatory bioactivities from sugar-amino acid Maillard reaction products, J. Agric. Food Chem. 60 (2012) 6718-6727. https://doi.org/10.1021/jf2044636.
DOI Google Scholar
[60]

C. Hong, C. Rhee, M. Pyo, et al., Anti-inflammatory effect of glucoselysine Maillard reaction products on intestinal inflammation model in vivo, Int. Immunopharmacol. 52 (2017) 324-332. https://doi.org/10.1016/j.intimp.2017.09.009.
DOI Google Scholar
[61]

Q. Yang, T. Li, S. Lyu, et al., Ovalbumin and its Maillard reaction products ameliorate dextran sulfate sodium-induced colitis by mitigating the imbalance of gut microbiota and metabolites, Int. J. Biol. Macromol. 222(2017) 715-724. https://doi.org/10.1016/j.ijbiomac.2022.09.224.
DOI Google Scholar
[62]

M. Smach, A. Zarrouk, J. Hafsa, et al., Maillard reaction products and phenolic compounds from roasted peanut flour extracts prevent scopolamine-induced amnesia via cholinergic modulation and antioxidative effects in mice, Int. J. Med. Food 24 (2021) 645-652. https://doi.org/10.1089/jmf.2020.0028.
DOI Google Scholar
[63]

G. Su, T. Zhao, Y. Zhao, et al., Effect of anchovy (Coilia mystus) protein hydrolysate and its Maillard reaction product on combating memory-impairment in mice, Food Res. Int. 82 (2016) 112-120. https://doi.org/10.1016/j.foodres.2016.01.022.
DOI Google Scholar
[64]

K. Ikeda, T. Higashi, H. Sano, et al., Nε-(Carboxymethyl) lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction, Biochemistry 35 (1996)8075-8083. https://doi.org/10.1021/bi9530550.
DOI Google Scholar
[65]

C. Sharma, A. Kaur, S. Thind, et al., Advanced glycation end-products(AGEs): an emerging concern for processed food industries, J. Food Sci. Technol. 52 (2015) 7561-7576. https://doi.org/10.1007/s13197-015-1851-y.
DOI Google Scholar
[66]

C. Luevano-Contreras, K. Chapman-Novakofski, Dietary advanced glycation end products and aging, Nutrients 2 (2010) 1247-1265. https://doi.org/10.3390/nu2121247.
DOI Google Scholar
[67]

M.W. Poulsen, R.V. Hedegaard, J.M. Andersen, et al., Advanced glycation endproducts in food and their effects on health, Food Chem. Toxicol. 60 (2013) 10-37. https://doi.org/10.1016/j.fct.2013.06.052.
DOI Google Scholar
[68]

N. Araki, T. Higashi, T. Mori, et al., Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end products of the Maillard reaction, Eur. J. Biochem. 230 (1995) 408-415. https://doi.org/10.1111/j.1432-1033.1995.0408h.x.
DOI Google Scholar
[69]

H. Suzuki, Y. Kurihara, M. Takeya, et al., A role for macrophage scavenger receptors in atherosclerosis and susceptibility to infection, Nature 386 (1997) 292-296. https://doi.org/10.1038/386292a0.
DOI Google Scholar
[70]

K. Waqas, J. Chen, B.C. van der Eerden, et al., Dietary advanced glycation end-products (dAGEs) intake and bone health: a cross-sectional analysis in the Rotterdam Study, Nutrients 12 (2020) 2377. https://doi.org/10.3390/nu12082377.
DOI Google Scholar
[71]

H. Vlassara, J. Uribarri, W. Cai, et al., Advanced glycation end product homeostasis: exogenous oxidants and innate defenses, Ann. N. Y. Acad. Sci. 1126 (2008) 46-52. https://doi.org/10.1196/annals.1433.055.
DOI Google Scholar
[72]

T. Goldberg, W. Cai, M. Peppa, et al., Advanced glycoxidation end products in commonly consumed foods, J. Am. Diet. Assoc. 104 (2004) 1287-1291. https://doi.org/10.1016/j.jada.2004.05.214.
DOI Google Scholar
[73]

S. Palimeri, E. Palioura, E. Diamanti-Kandarakis, Current perspectives on the health risks associated with the consumption of advanced glycation end products: recommendations for dietary management, iabetes, Metab. Syndr. Obes. 8 (2015) 415-426. https://doi.org/10.2147/DMSO.S63089.
DOI Google Scholar
[74]

K. Prasad, I. Dhar, G. Caspar-Bell, Role of advanced glycation end products and its receptors in the pathogenesis of cigarette smoke-induced cardiovascular disease, Int. J. Angiol. 24 (2015) 75-80. https://doi.org/10.1055/s-0034-1396413.
DOI Google Scholar
[75]

K. Nowotny, T. Jung, T. Grune, et al., Accumulation of modified proteins and aggregate formation in aging, Exp. Gerontol. 57 (2014) 122-131. https://doi.org/10.1016/j.exger.2014.05.016.
DOI Google Scholar
[76]

C.G. Schalkwijk, Vascular AGE-ing by methylglyoxal: the past, the present and the future, Diabetologia 58 (2015) 1715-1719. https://doi.org/10.1007/s00125-015-3597-5.
DOI Google Scholar
[77]

D.E. Maessen, C.D. Stehouwer, C.G. Schalkwijk, The role of methylglyoxal and the glyoxalase system in diabetes and other age-related diseases, Clin Sci 128 (2015) 839-861. https://doi.org/10.1042/CS20140683.
DOI Google Scholar
[78]

P. Thornalley, Glyoxalase Ⅰ–structure, function and a critical role in the enzymatic defence against glycation, Biochem. Soc. Trans. 31 (2003) 1343-1348. https://doi.org/10.1042/bst0311343.
DOI Google Scholar
[79]

N. Rabbani, M. Xue, P.J. Thornalley, Activity, regulation, copy number and function in the glyoxalase system, Biochem. Soc. Trans. 42 (2014) 419-424. https://doi.org/10.1042/BST20140008.
DOI Google Scholar
[80]

C. Ott, K. Jacobs, E. Haucke, et al., Role of advanced glycation end products in cellular signaling, Redox Biol. 2 (2014) 411-429. https://doi.org/10.1016/j.redox.2013.12.016.
DOI Google Scholar
[81]

X.J. Zhou, D. Rakheja, X. Yu, et al., The aging kidney, Kidney Int. 74 (2008) 710-720. https://doi.org/10.1038/ki.2008.319.
DOI Google Scholar
[82]

V.M. Monnier, D.R. Sell, Prevention and repair of protein damage by the maillard reaction in vivo, Rejuvenation Res. 9 (2006) 264-273. https://doi.org/10.1089/rej.2006.9.264.
DOI Google Scholar
[83]

C. Sady, C.L. Jiang, P. Chellan, et al., Maillard reactions by α-oxoaldehydes: detection of glyoxal-modified proteins, Biochim. Biophys. Acta 1481 (2000) 255-264. https://doi.org/10.1016/S0167-4838(00)00133-3.
DOI Google Scholar
[84]

Y. Kaji, T. Usui, T. Oshika, et al., Advanced glycation end products in diabetic corneas, Invest. Ophthalmol. Visual Sci. 41 (2000) 362-368. https://doi.org/10.1007/s004170050033.
DOI Google Scholar
[85]

N.S. Malik, S. Moss, N. Ahmed, et al., Ageing of the human corneal stroma:structural and biochemical changes, Biochim. Biophys. Acta 1138 (1992) 222-228. https://doi.org/10.1016/0925-4439(92)90041-K.
DOI Google Scholar
[86]

N.S. Malik, K.M. Meek, The inhibition of sugar-induced structural alterations in collagen by aspirin and other compounds, Biochem. Biophys. Res. Commun. 199 (1994) 683-686. https://doi.org/10.1006/bbrc.1994.1282.
DOI Google Scholar
[87]

D.R. Sell, N.R. Kleinman, V.M. Monnier, Longitudinal determination of skin collagen glycation and glycoxidation rates predicts early death in C57BL/6NNIA mice, FASEB J. 14 (2000) 145-146. https://doi.org/10.1096/fasebj.14.1.145.
DOI Google Scholar
[88]

L. Kessel, J.L. Hougaard, K.O. Kyvik, et al., Corneal fluorescence in relation to genetic and environmental factors: a twin study, Acta Ophthalmol. Scand. 81 (2009) 508-513. https://doi.org/10.1034/j.1600-0420.2003.00089.x.
DOI Google Scholar
[89]

N.S. Malik, K.M. Meek, Vitamins and analgesics in the prevention of collagen ageing, Age Ageing 25 (1996) 279-284. https://doi.org/10.1093/ageing/25.4.279.
DOI Google Scholar
[90]

A.M. Mcdermott, L.X. Tian, T.S. Kern, et al., Non-enzymatic glycation in corneas from normal and diabetic donors and its effects on epithelial cell attachment in vitro, Optometry 74 (2003) 443-452.
Google Scholar
[91]

Y. Kaji, S Amano, T Usui, et al., Advanced glycation end products in Descemet’s membrane and their effect on corneal endothelial cell, Curr. Eye Res. 23 (2001) 469-477. https://doi.org/10.1076/ceyr.23.6.469.6968.
DOI Google Scholar
[92]

Y. Kaji, S. Amano, T. Usui, et al., Expression and function of receptors for advanced glycation end products in bovine corneal endothelial cells, Invest. Ophthalmol. Visual Sci. 44 (2003) 521-528. https://doi.org/10.1167/iovs.02-0268.
DOI Google Scholar
[93]

R.H. Nagaraj, T. Oya-Ito, P.S. Padayatti, et al., Enhancement of chaperone function of α-crystallin by methylglyoxal modification, Biochemistry 42 (2003) 10746-10755. https://doi.org/10.1021/bi034541n.
DOI Google Scholar
[94]

B.K. Derham, J.C. Ellory, A.J. Bron, et al., The molecular chaperone α-crystallin incorporated into red cell ghosts protects membrane Na/K-ATPase against glycation and oxidative stress, Eur. J. Biochem. 270 (2003)2605-2611. https://doi.org/10.1046/j.1432-1033.2003.03631.x.
DOI Google Scholar
[95]

J. Sebag, B. Buckingham, M.A. Charles, et al., Biochemical abnormalities in vitreous of humans with proliferative diabetic retinopathy, Arch. Ophthalmol. 110 (1992) 1472-1476. https://doi.org/10.1001/archopht.1992.01080220134035.
DOI Google Scholar
[96]

H.P. Hammes, H. Hoerauf, A. Alt, et al., Nε-(Carboxymethyl) lysin and the AGE receptor RAGE colocalize in age-related macular degeneration, Invest. Ophthalmol. Visual Sci. 40 (1999) 1855-1859. https://doi.org/10.1007/s004170050286.
DOI Google Scholar
[97]

J.T. Handa, K.M. Reiser, H. Matsunaga, et al., The advanced glycation endproduct pentosidine induces the expression of PDGF-B in human retinal pigment epithelial cells, Exp. Eye Res. 66 (1998) 411-419. https://doi.org/10.1006/exer.1997.0442.
DOI Google Scholar
[98]

J.T. Handa, N. Verzijl, H. Matsunaga, et al., Increase in the advanced glycation end product pentosidine in Bruch’s membrane with age, Invest. Ophthalmol. Visual Sci. 40 (1999) 775-779.
Google Scholar
[99]

B. Farboud, A. Aotaki-Keen, T. Miyata, et al., Development of a polyclonal antibody with broad epitope specificity for advanced glycation endproducts and localization of these epitopes in Bruch’s membrane of the aging eye, Mol. Vis. 5 (1999) 11.
Google Scholar
[100]

J.G. Hollyfield, R.G. Salomon, J.W. Crabb, Proteomic approaches to understanding age-related macular degeneration, Retinal Degenerations 533 (2003) 83-89. https://doi.org/10.1007/978-1-4615-0067-4_11.
DOI Google Scholar
[101]

R.F. Mullins, S.R. Russell, D.H. Anderson, et al., Drusen associated with aging and age-related macular degeneration contain proteins common to extracellular deposits associated with atherosclerosis, elastosis, amyloidosis, and dense deposit disease, FASEB J. 14 (2000) 835-846. https://doi.org/10.1096/fasebj.14.7.835.
DOI Google Scholar
[102]

H.K. Pokharna, L.A. Pottenger, Nonenzymatic glycation of cartilage proteoglycans: an in vivo and in vitro study, Glycoconjugate J. 14 (1997) 917-923. https://doi.org/10.1023/A:1018514727213.
DOI Google Scholar
[103]

N. Verzijl, J. DeGroot, E. Oldehinkel, et al., Age-related accumulation of Maillard reaction products in human articular cartilage collagen, Biochem. J. 350 (2000) 381-387. https://doi.org/10.1042/bj3500381.
DOI Google Scholar
[104]

J. DeGroot, N. Verzijl, K. Jacobs, et al., Accumulation of advanced glycation endproducts reduces chondrocyte-mediated extracellular matrix turnover in human articular cartilage, Osteoarthr Cartilage 9 (2001) 720-726. https://doi.org/10.1053/joca.2001.0469.
DOI Google Scholar
[105]

M.M. Steenvoorden, T.W. Huizinga, N. Verzijl, et al., Activation of receptor for advanced glycation end products in osteoarthritis leads to increased stimulation of chondrocytes and synoviocytes, Arthritis Rheum. 54 (2006) 253-263. https://doi.org/10.1002/art.21523.
DOI Google Scholar
[106]

J. Xie, J.D. Méndez, V. Méndez-Valenzuela, et al., Cellular signalling of the receptor for advanced glycation end products (RAGE), Cell Signalling 25 (2013) 2185-2197. https://doi.org/10.1016/j.cellsig.2013.06.013.
DOI Google Scholar
[107]

Y. Arai, C.M. Martin-Ruiz, M. Takayama, et al., Inflammation, but not telomere length, predicts successful ageing at extreme old age: a longitudinal study of semi-supercentenarians, EBioMedicine 2 (2015) 1549-1558. https://doi.org/10.1016/j.ebiom.2015.07.029.
DOI Google Scholar
[108]

C. Franceschi, M. Bonafè, S. Valensin, et al., Inflamm-aging: an evolutionary perspective on immunosenescence, Ann. N. Y. Acad. Sci. 908 (2000) 244-254. https://doi.org/10.1111/j.1749-6632.2000.tb06651.x.
DOI Google Scholar
[109]

B.K. Kennedy, S.L. Berger, A. Brunet, et al. Aging: a common driver of chronic diseases and a target for novel interventions, Cell 159 (2014) 709-713. https://doi.org/10.1016/j.cell.2014.10.039.
DOI Google Scholar
[110]

A. Nowak, B. Przywara-Chowaniec, K. Tyrpień-Golder, et al., Systemic lupus erythematosus and glycation proces, Cent. Eur. J. Immunol. 45 (2020) 93-98. https://doi.org/10.5114/ceji.2018.77875.
DOI Google Scholar
[111]

K. De Leeuw, R. Graaff, R. De Vries, et al., Accumulation of advanced glycation endproducts in patients with systemic lupus erythematosus, Rheumatology 46 (2007) 1551-1556. https://doi.org/10.1093/rheumatology/kem215.
DOI Google Scholar
[112]

R. Vytášek, L. Šedová, V. Vilím, Increased concentration of two different advanced glycation end-products detected by enzyme immunoassays with new monoclonal antibodies in sera of patients with rheumatoid arthritis, BMC Musculoskel Dis. 11 (2010) 1-11. https://doi.org/10.1186/1471-2474-11-83.
DOI Google Scholar
[113]

I. Knani, H. Bouzidi, S. Zrour, et al. Increased serum concentrations of Nɛ-carboxymethyllysine are related to the presence and the severity of rheumatoid arthritis, Ann. Clin. Biochem. 55 (2018) 430-436. https://doi.org/10.1177/00045632177335.
DOI Google Scholar
[114]

O. Kaloudi, G. Basta, F. Perfetto, et al., Circulating levels of Nɛ-(carboxymethyl) lysine are increased in systemic sclerosis, Rheumatol. 46 (2007) 412-416. https://doi.org/10.1093/rheumatology/kel076.
DOI Google Scholar
[115]

J. Dadoniene, A. Cypiene, L. Ryliskyte, et al., Skin autofluorescence in systemic sclerosis is related to the disease and vascular damage: a cross-sectional analytic study of comparative groups, Dis. Markers 2015 (2015). https://doi.org/10.1155/2015/837470.
DOI Google Scholar
[116]

D.Y. Chen, Y.M. Chen, C.C Lin, et al., The potential role of advanced glycation end products (AGEs) and soluble receptors for AGEs (sRAGE) in the pathogenesis of adult-onset Still’s disease, BMC Musculoskeletal Disord. 16 (2015) 1-9. https://doi.org/10.1186/s12891-015-0569-3.
DOI Google Scholar
[117]

K. Kopeć-Pyciarz, I. Makulska, D. Zwolińska, et al., Skin autofluorescence, as a measure of AGE accumulation in individuals suffering from chronic plaque psoriasis, Mediators Inflamm. 2018 (2018) 4016939. https://doi.org/10.1155/2018/4016939.
DOI Google Scholar
[118]

A. Papagrigoraki, M. Del Giglio, C. Cosma, et al., Advanced glycation end products are increased in the skin and blood of patients with severe psoriasis, Acta Derm. Venereol. 97 (2017) 782-787. https://doi.org/10.2340/00015555-2661.
DOI Google Scholar
[119]

R.M. Ruggeri, T.M. Vicchio, M. Cristani, et al., Oxidative stress and advanced glycation end products in Hashimoto’s thyroiditis, Thyroid 26(2016) 504-511. https://doi.org/10.1089/thy.2015.0592.
DOI Google Scholar
[120]

A. Tarannum, A. Zarina, A. Khursheed, et al., Nitroxidized-albumin advanced glycation end product and rheumatoid arthritis, Arch. Rheumatol. 34 (2019) 461-475. https://doi.org/10.5606/ArchRheumatol.2019.7285.
DOI Google Scholar
[121]

L.M. Senatus, A.M. Schmidt, The AGE-RAGE axis: implications for age-associated arterial diseases, Front. Genet. 8 (2017) 187. https://doi.org/10.3389/fgene.2017.00187.
DOI Google Scholar
[122]

V.P. Reddy, P. Aryal, E.K. Darkwah, Advanced glycation end products in health and disease, Microorganisms 10 (2022) 1848. https://doi.org/10.3390/microorganisms10091848.
DOI Google Scholar
[123]

G. Sorci, F. Riuzzi, I. Giambanco, et al., RAGE in tissue homeostasis, repair and regeneration, Biochim. Biophys. Acta 1833 (2013) 101-109. https://doi.org/10.1016/j.bbamcr.2012.10.021.
DOI Google Scholar
[124]

D. Sanajou, A.G. Haghjo, H. Argani, et al., AGE-RAGE axis blockade in diabetic nephropathy: current status and future directions, Eur. J. Pharmacol. 833 (2018) 158-164. https://doi.org/10.1016/j.ejphar.2018.06.001.
DOI Google Scholar
[125]

M. MacLean, J. Derk, H.H. Ruiz, et al., The receptor for advanced glycation end products (RAGE) and DIAPH1: Implications for vascular and neuroinflammatory dysfunction in disorders of the central nervous system, Neurochem. Int. 126 (2019) 154-164. https://doi.org/10.1016/j.neuint.2019.03.012.
DOI Google Scholar
[126]
U.R. Addi, S. Jakhotia, S.S. Reddy, et al., Age-related neuronal damage by advanced glycation end products through altered proteostasis, Chem. Biol. Interact. 355 (2022) 109840. https://doi.org/10.1016/j.cbi.2022.109840Get rights and content.
DOI
[127]

K. Sathe, W. Maetzler, J.D. Lang, et al., S100B is increased in Parkinson’s disease and ablation protects against MPTP-induced toxicity through the RAGE and TNF-α pathway, Brain 135 (2012) 3336-3347. https://doi.org/10.1093/brain/aws250.
DOI Google Scholar
[128]

P. Teismann, K. Sathe, A. Bierhaus, et al., Receptor for advanced glycation endproducts (RAGE) deficiency protects against MPTP toxicity, Neurobiol. Aging 33 (2012) 2478-2490. https://doi.org/10.1016/j.neurobiolaging.2011.12.006.
DOI Google Scholar
[129]

S.D. Viana, J. Valero, P. Rodrigues-Santos, et al., Regulation of striatal astrocytic receptor for advanced glycation end-products variants in an early stage of experimental Parkinson’s disease, J. Neurochem. 138 (2016) 598-609. https://doi.org/10.1111/jnc.13682.
DOI Google Scholar
[130]

M. Santoro, W. Maetzler, P. Stathakos, et al., In-vivo evidence that high mobility group box 1 exerts deleterious effects in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine model and Parkinson’s disease which can be attenuated by glycyrrhizin, Neurobiol. Dis. 91(2016) 59-68. https://doi.org/10.1016/j.nbd.2016.02.018.
DOI Google Scholar
[131]

A. Sharma, D. Weber, J. Raupbach, et al., Advanced glycation end products and protein carbonyl levels in plasma reveal sex-specific differences in Parkinson’s and Alzheimer’s disease, Redox Biol. 34 (2020) 101546. https://doi.org/10.1016/j.redox.2020.101546.
DOI Google Scholar
[132]

N.T. Moldogazieva, I.M. Mokhosoev, T.I. Mel’nikova, et al., Oxidative stress and advanced lipoxidation and glycation end products (ALEs and AGEs) in aging and age-related diseases, Oxid. Med. Cell. Longevity 2019 (2019). https://doi.org/10.1155/2019/3085756.
DOI Google Scholar
[133]

S. Ko, H. Ko, K. Chu, et al., The possible mechanism of advanced glycation end products (AGEs) for Alzheimer’s disease, PLoS ONE 10 (2015) e0143345. https://doi.org/10.1371/journal.pone.0143345.
DOI Google Scholar
[134]

S.Y. Ko, Y.P. Lin, Y.S. Lin, et al., Advanced glycation end products enhance amyloid precursor protein expression by inducing reactive oxygen species, Free Radical Biol. Med. 49 (2010) 474-480. https://doi.org/10.1016/j.freeradbiomed.2010.05.005.
DOI Google Scholar
[135]

X.H. Li, B.L. Lv, J.Z. Xie, et al., AGEs induce Alzheimer-like tau pathology and memory deficit via RAGE-mediated GSK-3 activation, Neurobiol. Aging 33 (2012) 1400-1410. https://doi.org/10.1016/j.neurobiolaging.2011.02.003.
DOI Google Scholar
[136]

T.F. Outeiro, E. Kontopoulos, S.M. Altmann, et al., Sirtuin 2 inhibitors rescue α-synuclein-mediated toxicity in models of Parkinson’s disease, Science 317 (2007) 516-519. https://doi.org/10.1126/science.114378.
DOI Google Scholar
[137]

V. Padmaraju, J.J. Bhaskar, U.J. Prasada Rao, et al., Role of advanced glycation on aggregation and DNA binding properties of α-synuclein, J.Alzheimer’s Dis. 24 (2011) 211-221. https://doi.org/10.3233/JAD-2011-101965.
DOI Google Scholar
[138]

L. Chen, Y. Wei, X. Wang, et al., Ribosylation rapidly induces α-synuclein to form highly cytotoxic molten globules of advanced glycation end products, PLoS ONE 5 (2010) e9052. https://doi.org/10.1371/journal.pone.0009052.
DOI Google Scholar
[139]

G. Münch, H. Lüth, A.Wong, et al., Crosslinking of α-synuclein by advanced glycation endproducts–an early pathophysiological step in Lewy body formation? J. Chem. Neuroanat. 20 (2000) 253-257. https://doi.org/10.1016/S0891-0618(00)00096-X.
DOI Google Scholar
[140]

E. Dalfó, M. Portero-Otín, V. Ayala, et al., Evidence of oxidative stress in the neocortex in incidental Lewy body disease, J. Neuropathol. Exp. Neurol. 64 (2005) 816-830. https://doi.org/10.1097/01.jnen.0000179050.54522.5a.
DOI Google Scholar
[141]

E. Bayarsaikhan, D. Bayarsaikhan, J. Lee, et al., Microglial AGE-albumin is critical for neuronal death in Parkinson’s disease: a possible implication for theranostics, Int. J. Nanomed. 10 (2016) 281-292. https://doi.org/10.2147/IJN.S95077.
DOI Google Scholar
[142]

K.A. Adeshara, N. Bangar, A.G. Diwan, et al., Plasma glycation adducts and various RAGE isoforms are intricately associated with oxidative stress and inflammatory markers in type 2 diabetes patients with vascular complications, Diabetes Metab. Syndr. 16 (2022) 102441. https://doi.org/10.1016/j.dsx.2022.102441.
DOI Google Scholar
[143]

S. Yang, J.E. Litchfield, J.W. Baynes, AGE-breakers cleave model compounds, but do not break Maillard crosslinks in skin and tail collagen from diabetic rats, Arch. Biochem. Biophys. 412 (2003) 42-46. https://doi.org/10.1016/S0003-9861(03)00015-8.
DOI Google Scholar
[144]

S.J. Hunter, A.C. Boyd, F.P. O’Harte, et al., Demonstration of glycated insulin in human diabetic plasma and decreased biological activity assessed by euglycemic-hyperinsulinemic clamp technique in humans, Diabetes 52 (2003) 492-498. https://doi.org/10.2337/diabetes.52.2.492.
DOI Google Scholar
[145]

J.P. Sutherland, B. McKinley, R.H. Eckel, The metabolic syndrome and inflammation, Metab. Syndr. Relat. Disord. 2 (2004) 82-104. https://doi.org/10.1089/met.2004.2.82.
DOI Google Scholar
[146]

K.C. Nandipati, S. Subramanian, D.K. Agrawal, Protein kinases: mechanisms and downstream targets in inflammation-mediated obesity and insulin resistance, Mol. Cell. Biochem. 426 (2017) 27-45. https://doi.org/10.1007/s11010-016-2878-8.
DOI Google Scholar
[147]

V. Sidarala, A. Kowluru, The regulatory roles of mitogen-activated protein kinase (MAPK) pathways in health and diabetes: lessons learned from the pancreatic β-cell, Recent Pat. Endocr. Metab. Immune. Drug Discov. 10 (2016) 76-84. https://doi.org/10.2174/1872214810666161020154905.
DOI Google Scholar
[148]

A. Gabryelska, F.F. Karuga, B. Szmyd, et al., HIF-1α as a mediator of insulin resistance, T2DM, and its complications: potential links with obstructive sleep apnea, Front. Physiol. 11 (2020) 1035. https://doi.org/10.3389/fphys.2020.01035.
DOI Google Scholar
[149]

Y. Kihira, M. Miyake, M. Hirata, et al., Deletion of hypoxia-inducible factor-1α in adipocytes enhances glucagon-like peptide-1 secretion and reduces adipose tissue inflammation, PLoS ONE 9 (2014) e93856. https://doi.org/10.1371/journal.pone.0093856.
DOI Google Scholar
[150]

S.S. Guan, M.L. Sheu, R.S. Yang, et al., The pathological role of advanced glycation end products-downregulated heat shock protein 60 in islet β-cell hypertrophy and dysfunction, Oncotarget 7 (2016) 23072-23087. https://doi.org/10.18632/oncotarget.8604.
DOI Google Scholar
[151]

J. Bo, S. Xie, Y. Guo, et al., Methylglyoxal impairs insulin secretion of pancreatic β-cells through increased production of ROS and mitochondrial dysfunction mediated by upregulation of UCP2 and MAPKs, J. Diabetes Res. 2016 (2016). https://doi.org/10.1155/2016/2029854.
DOI Google Scholar
[152]

A. Abedini, P. Cao, A. Plesner, et al., RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity, J. Clin. Invest. 128 (2018) 682-698. https://doi.org/10.1172/JCI85210.
DOI Google Scholar
[153]

A. Abedini, J. Derk, A.M. Schmidt, The receptor for advanced glycation endproducts is a mediator of toxicity by IAPP and other proteotoxic aggregates: establishing and exploiting common ground for novel amyloidosis therapies, Protein Sci. 27 (2018) 1166-1180. https://doi.org/10.1002/pro.3425.
DOI Google Scholar
[154]

Y. Yuan, H. Sun, Z. Sun, Advanced glycation end products (AGEs) increase renal lipid accumulation: a pathogenic factor of diabetic nephropathy (DN), Lipids Health Dis. 16 (2017) 1-9. https://doi.org/10.1186/s12944-017-0522-6.
DOI Google Scholar
[155]

C.S. Haitoglou, E. Tsilibary, M. Brownlee, et al., Altered cellular interactions between endothelial cells and nonenzymatically glucosylated laminin/type Ⅳ collagen, J. Biol. Chem. 267 (1992) 12404-12407. https://doi.org/10.1016/S0021-9258(18)42287-9.
DOI Google Scholar
[156]

S. Yamagishi, T. Matsui, Advanced glycation end products, oxidative stress and diabetic nephropathy, Oxid. Med. Cell. Longevity 3 (2010) 101-108. https://doi.org/10.4161/oxim.3.2.11148.
DOI Google Scholar
[157]

M.D. Oldfield, L.A. Bach, J.M. Forbes, et al., Advanced glycation end products cause epithelial-myofibroblast transdifferentiation via the receptor for advanced glycation end products (RAGE), J. Clin. Invest. 108 (2001) 1853-1863. https://doi.org/10.1172/JCI11951.
DOI Google Scholar
[158]

A.G. Nerlich, E.D. Schleicher, Nε-(Carboxymethyl) lysine in atherosclerotic vascular lesions as a marker for local oxidative stress, Atheroscler 144 (1999) 41-47. https://doi.org/10.1016/S0021-9150(99)00038-6.
DOI Google Scholar
[159]

S.Y. Li, M. Du, E.K. Dolence, et al., Aging induces cardiac diastolic dysfunction, oxidative stress, accumulation of advanced glycation endproducts and protein modification, Aging Cell 4 (2005) 57-64. https://doi.org/10.1111/j.1474-9728.2005.00146.x.
DOI Google Scholar
[160]

C.P. Hodgkinson, R.C. Laxton, K. Patel, et al., Advanced glycation end-product of low density lipoprotein activates the toll-like 4 receptor pathway implications for diabetic atherosclerosis, Arterioscler. Thromb. Vasc. Biol.28 (2008) 2275-2281. https://doi.org/10.1161/ATVBAHA.108.175992.
DOI Google Scholar
[161]

L. Godfrey, N. Yamada-Fowler, J. Smith, et al., Arginine-directed glycation and decreased HDL plasma concentration and functionality, Nutr. Diabetes 4 (2014) e134. https://doi.org/10.1038/nutd.2014.31.
DOI Google Scholar
[162]

A. Baidoshvili, P. Krijnen, K. Kupreishvili, et al., Nε-(Carboxymethyl)lysine depositions in intramyocardial blood vessels in human and rat acute myocardial infarction: a predictor or reflection of infarction? Arterioscler. Thromb. Vasc. Biol. 26 (2006) 2497-2503. https://doi.org/10.1161/01.ATV.0000245794.45804.ab.
DOI Google Scholar
[163]

M.P. Begieneman, L. Rijvers, B. Kubat, et al., Atrial fibrillation coincides with the advanced glycation end product Nε-(carboxymethyl) lysine in the atrium, Am. J. Pathol. 185 (2015) 2096-2104. https://doi.org/10.1016/j.ajpath.2015.04.018.
DOI Google Scholar
[164]

C. Prasad, K.E. Davis, V. Imrhan, et al., Advanced glycation end products and risks for chronic diseases: intervening through lifestyle modification, Am. J. Lifestyle Med. 13 (2019) 384-404. https://doi.org/10.1177/1559827617708.
DOI Google Scholar
[165]

J.W. Baynes, V.M. Monnier, J.M. Ames, et al., The Maillard reaction: chemistry at the interface of nutrition, aging, and disease, New York Academy of Sciences, 2005.
DOI Google Scholar
[166]

L. Robert, A.M. Robert, T. Fülöp, Rapid increase in human life expectancy: will it soon be limited by the aging of elastin? Biogerontology 9 (2008) 119-133. https://doi.org/10.1007/s10522-007-9122-6.
DOI Google Scholar
[167]

L. Robert, J. Labat-Robert, Role of the Maillard reaction in aging and age-related diseases. Studies at the cellular-molecular level, Clin. Chem. Lab.Med. 52 (2014) 5-10. https://doi.org/10.1515/cclm-2012-0763.
DOI Google Scholar
[168]

L. Robert, J. Molinari, V. Ravelojaona, et al., Age- and passage-dependent upregulation of fibroblast elastase-type endopeptidase activity. Role of advanced glycation endproducts, inhibition by fucose- and rhamnose-rich oligosaccharides, Arch. Gerontol. Geriatr. 50 (2010) 327-331. https://doi.org/10.1016/j.archger.2009.05.006.
DOI Google Scholar
[169]

L. Bizbiz, A. Alpérovitch, L. Robert, Aging of the vascular wall: serum concentration of elastin peptides and elastase inhibitors in relation to cardiovascular risk factors. The EVA study, Atheroscler. 131 (1997) 73-78. https://doi.org/10.1016/S0021-9150(97)06076-0.
DOI Google Scholar
[170]

N. Harvey, E. Dennison, C. Cooper, Osteoporosis: impact on health and economics, Nat. Rev. Rheumatol. 6 (2010) 99-105. https://doi.org/10.1038/nrrheum.2009.260.
DOI Google Scholar
[171]

P. Odetti, S. Rossi, F. Monacelli, et al., Advanced glycation end products and bone loss during aging, Ann. N. Y. Acad. Sci. 1043 (2005) 710-717. https://doi.org/10.1196/annals.1333.082.
DOI Google Scholar
[172]

D.H. Yang, T.I. Chiang, I.C. Chang, et al., Increased levels of circulating advanced glycation end-products in menopausal women with osteoporosis, Int. J. Med. Sci. 11 (2014) 453-460. https://doi.org/10.7150/ijms.8172.
DOI Google Scholar
[173]

N.L. Reynaert, P. Gopal, E.P. Rutten, et al., Advanced glycation end products and their receptor in age-related, non-communicable chronic inflammatory diseases; overview of clinical evidence and potential contributions to disease, Int. J. Biochem. Cell Biol. 81 (2016) 403-418. https://doi.org/10.1016/j.biocel.2016.06.016.
DOI Google Scholar
[174]

G.E. Hein, Glycation endproducts in osteoporosis–is there a pathophysiologic importance? Clin. Chim. Acta 371 (2006) 32-36. https://doi.org/10.1016/j.cca.2006.03.017.
DOI Google Scholar
[175]

M. Saito, K. Fujii, K. Marumo, Degree of mineralization-related collagen crosslinking in the femoral neck cancellous bone in cases of hip fracture and controls, Calcif. Tissue Int. 79 (2006) 160-168. https://doi.org/10.1007/s00223-006-0035-1.
DOI Google Scholar
[176]

X.N. Dong, A. Qin, J. Xu, et al., In situ accumulation of advanced glycation endproducts (AGEs) in bone matrix and its correlation with osteoclastic bone resorption, Bone 49 (2011) 174-183. https://doi.org/10.1016/j.bone.2011.04.009.
DOI Google Scholar
[177]

R. Sanguineti, D. Storace, F. Monacelli, et al., Pentosidine effects on human osteoblasts in vitro, Ann. N. Y. Acad. Sci. 1126 (2008) 166-172. https://doi.org/10.1196/annals.1433.044.
DOI Google Scholar
[178]

S. Yamagishi, Role of advanced glycation end products (AGEs) in osteoporosis in diabetes, Curr. Drug Targets 12 (2011) 2096-2102. https://doi.org/10.2174/138945011798829456.
DOI Google Scholar
[179]

R. Sanguineti, A. Puddu, F. Mach, et al., Advanced glycation end products play adverse proinflammatory activities in osteoporosis, Mediators Inflamm.2014 (2014). https://doi.org/10.1155/2014/975872.
DOI Google Scholar
[180]

F. Azizian-Farsani, N. Abedpoor, M. Hasan Sheikhha, et al., Receptor for advanced glycation end products acts as a fuel to colorectal cancer development, Front. Oncol. 10 (2020) 552283. https://doi.org/10.3389/fonc.2020.552283.
DOI Google Scholar
[181]

P. Swami, S. Thiyagarajan, A. Vidger, et al., Rage up-regulation differently affects cell proliferation and migration in pancreatic cancer cells, Int. J. Mol. Sci. 21 (2020) 7723. https://doi.org/10.3390/ijms21207723.
DOI Google Scholar
[182]

G. Akkus, V. Izol, F. Ok, et al., Possible role of the receptor of advanced glycation end products (RAGE) in the clinical course of prostate neoplasia in patients with and without type 2 diabetes mellitus, Int. J. Clin. Pract. 75 (2021) e13723. https://doi.org/10.1111/ijcp.13723.
DOI Google Scholar
[183]

M.C. Chen, K.C. Chen, G.C. Chang, et al., RAGE acts as an oncogenic role and promotes the metastasis of human lung cancer, Cell Death Dis. 11 (2020) 1-13. https://doi.org/10.1038/s41419-020-2432-1.
DOI Google Scholar
[184]

W. Zhang, X. Deng, R. Tang, et al., Receptor for advanced glycation endproduct rs1800624 polymorphism contributes to increase breast cancer risk: evidence from a meta-analysis, Medicine 99 (2020) e22775. https://doi.org/10.1097/MD.0000000000022775.
DOI Google Scholar
[185]

K.C. Sourris, B.E. Harcourt, J.M. Forbes, A new perspective on therapeutic inhibition of advanced glycation in diabetic microvascular complications: common downstream endpoints achieved through disparate therapeutic approaches? Am. J. Nephrol. 30 (2009) 323-335. https://doi.org/10.1159/000226586.
DOI Google Scholar
[186]

H. Younus, S. Anwar, Prevention of non-enzymatic glycosylation (glycation): implication in the treatment of diabetic complication, Int. J. Health Sci. 10 (2016) 261-277. https://doi.org/0.12816/0048818.
DOI Google Scholar
[187]

G. Abbas, A.S. Al-Harrasi, H. Hussain, et al., Antiglycation therapy: discovery of promising antiglycation agents for the management of diabetic complications, Pharm. Biol. 4 (2016) 198-206. https://doi.org/10.3109/13880209.2015.1028080.
DOI Google Scholar
[188]

S. Rowan, E. Bejarano, A. Taylor, Mechanistic targeting of advanced glycation end-products in age-related diseases, Biochim. Biophys. Acta 1864 (2018) 3631-3643. https://doi.org/10.1016/j.bbadis.2018.08.036.
DOI Google Scholar
[189]

V.P. Reddy, A. Beyaz, Inhibitors of the Maillard reaction and AGE breakers as therapeutics for multiple diseases, Drug Discov. Today 11 (2006) 646-654. https://doi.org/10.1016/j.drudis.2006.05.016.
DOI Google Scholar
[190]

P.J. Thornalley, Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts, Arch. Biochem. Biophys. 419 (2003) 31-40. https://doi.org/10.1016/j.abb.2003.08.013.
DOI Google Scholar
[191]

H. Chilukuri, M. Kulkarni, M. Fernandes, Revisiting amino acids and peptides as anti-glycation agents, Med. Chem. Comm. 9 (2018) 614-624. https://doi.org/10.1039/C7MD00514H.
DOI Google Scholar
[192]

D.Y. Kim, M.K. Kang, E.J. Lee, et al., Eucalyptol inhibits advanced glycation end products-induced disruption of podocyte Slit junctions by suppressing Rage-Erk-C-Myc signaling pathway, Mol. Nutr. Food Res. 62 (2018) 1800302. https://doi.org/10.1002/mnfr.201800302.
DOI Google Scholar
[193]

Y.Y. Qiu, L.Q. Tang, W. Wei, Berberine exerts renoprotective effects by regulating the AGEs-RAGE signaling pathway in mesangial cells during diabetic nephropathy, Mol. Cell. Endocrinol. 443 (2017) 89-105. https://doi.org/10.1016/j.mce.2017.01.009.
DOI Google Scholar
[194]

B. Hou, G. Qiang, Y. Zhao, et al., Salvianolic acid A protects against diabetic nephropathy through ameliorating glomerular endothelial dysfunction via inhibiting AGE-RAGE signaling, Cell. Physiol. Biochem. 44 (2017) 2378-2394. https://doi.org/10.1159/000486154.
DOI Google Scholar
[195]

Y.J. Chen, L. Kong, Z.Z. Tang, et al., Hesperetin ameliorates diabetic nephropathy in rats by activating Nrf2/ARE/glyoxalase 1 pathway, Biomed. Pharmacother. 111 (2019) 1166-1175. https://doi.org/10.1016/j.biopha.2019.01.030.
DOI Google Scholar
[196]

K. Prasad, S. Tiwari, Therapeutic interventions for advanced glycation-end products and its receptor-mediated cardiovascular disease, Curr. Pharm. Des. 23 (2017) 937-943. https://doi.org/10.2174/1381612822666161006143032.
DOI Google Scholar
[197]

A. Dhar, I. Dhar, A. Bhat, et al., Alagebrium attenuates methylglyoxal induced oxidative stress and AGE formation in H9C2 cardiac myocytes, Life Sci. 146 (2016) 8-14. https://doi.org/10.1016/j.lfs.2016.01.006.
DOI Google Scholar
[198]

T. Matsui, N. Nakamura, A. Ojima, et al., Sulforaphane reduces advanced glycation end products (AGEs)-induced inflammation in endothelial cells and rat aorta, Nutr. Metab. Cardiovasc. Dis. 26 (2016) 797-807. https://doi.org/10.1016/j.numecd.2016.04.008.
DOI Google Scholar
[199]

P. Sanchis, R. Rivera, F. Berga, et al., Phytate decreases formation of advanced glycation end-products in patients with type Ⅱ diabetes: randomized crossover trial, Sci. Rep. 8 (2018) 1-13. https://doi.org/10.1038/s41598-018-27853-9.
DOI Google Scholar
[200]

Y.M. Lee, J. Kim, C.S. Kim, et al., Anti-glycation and anti-angiogenic activities of 5’-methoxybiphenyl-3,4,3’-triol, a novel phytochemical component of Osteomeles schwerinae, Eur. J. Pharmacol. 760 (2015) 172-178. https://doi.org/10.1016/j.ejphar.2015.04.022.
DOI Google Scholar
[201]

J. Kim, C.S. Kim, M.K. Moon, et al., Epicatechin breaks preformed glycated serum albumin and reverses the retinal accumulation of advanced glycation end products, Eur. J. Pharmacol. 748 (2015) 108-114. https://doi.org/10.1016/j.ejphar.2014.12.010.
DOI Google Scholar
[202]

A. Parveen, J.H. Kim, B.G. Oh, et al., Phytochemicals: target-based therapeutic strategies for diabetic retinopathy, Molecules 23 (2018) 1519. https://doi.org/10.3390/molecules23071519.
DOI Google Scholar
[203]

Y. Liu, W. Shen, Q. Chen, et al., Inhibition of RAGE by FPS-ZM1 alleviates renal injury in spontaneously hypertensive rats, Eur. J. Pharmacol. 882 (2020) 173228. https://doi.org/10.1016/j.ejphar.2020.173228.
DOI Google Scholar
[204]

C. Shen, Y. Ma, Z. Zeng, et al., RAGE-specific inhibitor FPS-ZM1 attenuates AGEs-induced neuroinflammation and oxidative stress in rat primary microglia, Neurochem. Res. 42 (2017) 2902-2911. https://doi.org/10.1007/s11064-017-2321-x.
DOI Google Scholar
[205]

L.K. Huang, S.P. Chao, C.J. Hu, Clinical trials of new drugs for Alzheimer disease, J. Biomed. Sci. 27 (2020) 1-13. https://doi.org/10.1186/s12929-019-0609-7.
DOI Google Scholar
[206]

A. Pinkas, M. Aschner, Advanced glycation end-products and their receptors: related pathologies, recent therapeutic strategies, and a potential model for future neurodegeneration studies, Chem. Res. Toxicol. 29 (2016) 707-714. https://doi.org/10.1021/acs.chemrestox.6b00034.
DOI Google Scholar
[207]

R. Babaei-Jadidi, N. Karachalias, N. Ahmed, et al., Prevention of incipient diabetic nephropathy by high-dose thiamine and benfotiamine, Diabetes 52 (2003) 2110-2120. https://doi.org/10.2337/diabetes.52.8.2110.
DOI Google Scholar
[208]

K.C. Sourris, A. Watson, K. Jandeleit-Dahm, Inhibitors of advanced glycation end product (AGE) formation and accumulation, Mol. Nutr. Food Res. 264 (2020) 395-423. https://doi.org/10.1007/164_2020_391.
DOI Google Scholar
[209]

V. Maleki, E. Foroumandi, F. Hajizadeh-Sharafabad, et al., The effect of resveratrol on advanced glycation end products in diabetes mellitus: a systematic review, Arch. Physiol. Biochem. 128 (2022) 253-260. https://doi.org/10.1080/13813455.2019.1673434.
DOI Google Scholar
[210]

C. Toprak, S. Yigitaslan, Alagebrium and complications of diabetes mellitus, Eurasian J. Med. 51 (2019) 285-292. https://doi.org/10.5152/eurasianjmed.2019.18434.
DOI Google Scholar
[211]

P.C. Chang, S.C. Tsai, L.Y. Chong, et al., N-Phenacylthiazolium bromide inhibits the advanced glycation end product (AGE)-AGE receptor axis to modulate experimental periodontitis in rats, J. Periodontol. 85 (2014) e268-e276. https://doi.org/10.1902/jop.2014.130554.
DOI Google Scholar
[212]

H. Singh, D.K. Agrawal., Therapeutic potential of targeting the receptor for advanced glycation end products (RAGE) by small molecule inhibitors, Drug Dev. Res. 83 (2022) 1257-1269. https://doi.org/10.1002/ddr.21971.
DOI Google Scholar
[213]

A.H.A.M. El-Far, S. Munesue, A. Harashima, et al., In vitro anticancer effects of a RAGE inhibitor discovered using a structure-based drug design system, Oncol. Lett. 15 (2018) 4627-4634. https://doi.org/10.3892/ol.2018.7902.
DOI Google Scholar
[214]

M.P. Billacura, K. Hanna, D.J. Boocock, et al., Carnosine protects stimulus-secretion coupling through prevention of protein carbonyl adduction events in cells under metabolic stress, Free Radicals Biol. Med. 175 (2021) 65-79. https://doi.org/10.1016/j.freeradbiomed.2021.08.233.
DOI Google Scholar
[215]

J.H. Chen, X. Lin, C. Bu, et al., Role of advanced glycation end products in mobility and considerations in possible dietary and nutritional intervention strategies, Nutr. Metab. 15 (2018) 1-18. https://doi.org/10.1186/s12986-018-0306-7.
DOI Google Scholar
[216]

F. Zheng, W. Cai, T. Mitsuhashi, et al., Lysozyme enhances renal excretion of advanced glycation endproducts in vivo and suppresses adverse age-mediated cellular effects in vitro: a potential AGE sequestration therapy for diabetic nephropathy? Mol. Med. 7 (2001) 737-747. https://doi.org/10.1007/BF03401963.
DOI Google Scholar
[217]

M.H. Do, J. Hur, J. Choi, et al., Eucommia ulmoides ameliorates glucotoxicity by suppressing advanced glycation end-products in diabetic mice kidney, Nutrients 10 (2018) 265. https://doi.org/10.3390/nu10030265.
DOI Google Scholar
[218]

M.H. Do, J. Hur, J. Choi, et al., Spatholobus suberectus ameliorates diabetes-induced renal damage by suppressing advanced glycation end products in db/db mice, Int. J. Mol. Sci. 19 (2018) 2774. https://doi.org/10.3390/ijms19092774.
DOI Google Scholar
[219]

S. Yamagishi, K. Fukami, T. Matsui, Crosstalk between advanced glycation end products (AGEs)-receptor RAGE axis and dipeptidyl peptidase-4-incretin system in diabetic vascular complications, Cardiovasc. Diabetol. 14(2015) 1-12. https://doi.org/10.1186/s12933-015-0176-5.
DOI Google Scholar
[220]

S. Yamagishi, N. Nakamura, M. Suematsu, et al., Advanced glycation end products: a molecular target for vascular complications in diabetes, Mol. Med. 21 (2015) S32-S40. https://doi.org/10.2119/molmed.2015.00067.
DOI Google Scholar
[221]

B. Guan, X. Zhang, Aptamers as versatile ligands for biomedical and pharmaceutical applications, Int. J. Nanomed. 15 (2020) 1059-1071. https://doi.org/10.2147/IJN.S237544.
DOI Google Scholar
[222]

S. Yamagishi, K.Taguchi, K. Fukami, DNA-aptamers raised against AGEs as a blocker of various aging-related disorders, Glycoconjugate J. 33 (2016) 683-690. https://doi.org/10.1007/s10719-016-9682-2.
DOI Google Scholar
[223]

A. Chhabra, A. Bhatia, A.K. Ram, et al., Increased advanced glycation end product specific fluorescence in repeatedly heated used cooking oil, J. Food Sci. Technol. 54 (2017) 2602-2606. https://doi.org/10.1007/s13197-017-2682-9.
DOI Google Scholar
[224]

Y. Kim, J.B. Keogh, P. Deo, et al., Differential effects of dietary patterns on advanced glycation end products: a randomized crossover study, Nutrients 12 (2020) 1767. https://doi.org/10.3390/nu12061767.
DOI Google Scholar
[225]

H. Vlassara, W. Cai, J. Crandall, et al., Inflammatory mediators are induced by dietary glycotoxins, a major risk factor for diabetic angiopathy, Proc. Natl. Acad. Sci. 99 (2002) 15596-15601. https://doi.org/10.1073/pnas.242407999.
DOI Google Scholar
[226]

K. Šebeková, M. Krajčovičová-Kudláčková, R. Schinzel, et al., Plasma levels of advanced glycation end products in healthy, long-term vegetarians and subjects on a western mixed diet, Eur. J. Nutr. 40 (2001) 275-281. https://doi.org/10.1007/s394-001-8356-3.
DOI Google Scholar
[227]

J. Lopez-Moreno, G.M. Quintana-Navarro, J. Delgado-Lista, et al., Mediterranean diet supplemented with coenzyme Q10 modulates the postprandial metabolism of advanced glycation end products in elderly men and women, J. Gerontol. A 73 (2018) 340-346. https://doi.org/10.1093/gerona/glw214.
DOI Google Scholar
[228]

C. Cerami, H. Founds, I. Nicholl, et al., Tobacco smoke is a source of toxic reactive glycation products, Proc. Natl. Acad. Sci. 94 (1997) 13915-13920. https://doi.org/10.1073/pnas.94.25.13915.
DOI Google Scholar
[229]

I.D. Nicholl, A.W. Stitt, J.E. Moore, et al., Increased levels of advanced glycation endproducts in the lenses and blood vessels of cigarette smokers, Mol. Med. 4 (1998) 594-601. https://doi.org/10.1007/BF03401759.
DOI Google Scholar
[230]

G. Federico, M. Gori, E. Randazzo, et al., Skin advanced glycation end-products evaluation in infants according to the type of feeding and mother’s smoking habits, SAGE Open Med. 4 (2016). https://doi.org/10.1177/2050312116682126.
DOI Google Scholar
Publication history
Copyright
Acknowledgements
Rights and permissions

Publication history

Received: 30 December 2022
Revised: 28 February 2023
Accepted: 30 March 2023
Published: 08 February 2024
Issue date: May 2024

Copyright

© 2024 Beijing Academy of Food Sciences. Publishing services by Tsinghua University Press.

Acknowledgements

Acknowledgment

This review was financially supported by grants from the National Natural Science Foundation of China (82170873; 81871095), the National Natural Science Foundation of China (81974503), and the Tsinghua University Spring Breeze Fund (20211080005).

Rights and permissions

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Return