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The Role of Advanced Glycation End Products in Aging and Metabolic Diseases: Bridging Association and Causality
Open accessAbstract
Accumulation of advanced glycation end products (AGEs) on nucleotides, lipids, and peptides/proteins are an inevitable component of the aging process in all eukaryotic organisms, including humans. To date, a substantial body of evidence shows that AGEs and their functionally compromised adducts are linked to and perhaps responsible for changes seen during aging and for the development of many age-related morbidities. However, much remains to be learned about the biology of AGE formation, causal nature of these associations, and whether new interventions might be developed that will prevent or reduce the negative impact of AGEs-related damage. To facilitate achieving these latter ends, we show how invertebrate models, notably Drosophila melanogaster and Caenorhabditis elegans, can be used to explore AGE-related pathways in depth and to identify and assess drugs that will mitigate against the detrimental effects of AGE-adduct development.
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“The fundamental role of AGEs, including glycoxidation products, in human aging, but also in aging of vertebrate and invertebrate model organism has been reviewed in 2018 by Chaudhuri and colleagues [153]”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [153]
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“a growing body of evidence reveals that levels of glycoxidation products increase as a function of age in several tissues, dependent on the dietary intake and the presence of hyperglycemic conditions [152,153]”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [153]
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“together indicating the relevance of AGEs as biomarkers of aging and age-related diseases”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [153]
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“However, under pathological conditions, RAGEs can be upregulated and participate in various aging-related pathophysiologies, such as adult-onset type 2 diabetes mellitus (DM), cardiovascular disorders, myocardial infarction, chronic kidney failure, pancreatitis, cancer, Alzheimer’s disease (AD), Parkinson’s disease (PD), hepatic fibrosis, and alcohol-mediated tissue injury37,38.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [37]
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“Generally, RAGEs are expressed widely in various cells, such as endothelial cells, macrophages/monocytes, neutrophils, lymphocytes, microglia, astrocytes, and neurons, and organs, such as the brain, heart, lung, kidney, and liver36,37.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [37]
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Ma, H., Li, S., Xu, P., Babcock, S. A., Dolence, E. K., Brownlee, M., Li, J., & Ren, J. T. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00547.x · Cited by 154
RetractedLópez-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107 · cited 1×
“…anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript Diabetic macroangiopathy The detoxification of α-DCs, a precursor of AGE, also underlies the prevention of diabetesmediated micro and macro vascular damage that may contribute to atherosclerosis and stroke (Brownlee, 2001, 2005).”
The Pathobiology of Diabetic Complications
Brownlee, M. (2005) · Diabetes · doi:10.2337/diabetes.54.6.1615 · Cited by 5,339 · cited 3×
“…anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript Diabetic macroangiopathy The detoxification of α-DCs, a precursor of AGE, also underlies the prevention of diabetesmediated micro and macro vascular damage that may contribute to atherosclerosis and stroke (Brownlee, 2001, 2005).”
BackgroundGupta, A., & Uribarri, J. (2016) · Hormone Research in Paediatrics · doi:10.1159/000444053 · Cited by 4,023
Chronic Inflammation (Inflammaging) and Its Potential Contribution to Age-Associated Diseases
Franceschi, C., & Campisi, J. (2014) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glu057 · Cited by 3,891
Advanced Glycation End Products and Diabetic Complications
Singh, V. P., Bali, A., Singh, N., & Jaggi, A. S. (2014) · The Korean Journal of Physiology & Pharmacology · doi:10.4196/kjpp.2014.18.1.1 · Cited by 1,518
The use of animal models in diabetes research
King, A. J. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.01911.x · Cited by 1,303 · cited 1×
“Vertebrate model organisms such as rodents are a natural first choice to model AGEmediated pathologies, due to the relatively close link to human disease biology and a track record as a model for studying disease pathology in diabetes (King, 2012).”
BackgroundAminoguanidine Prevents Diabetes-Induced Arterial Wall Protein Cross-Linking
Brownlee, M., Vlassara, H., Kooney, A., Ulrich, P. C., & Cerami, A. (1986) · Science · doi:10.1126/science.3487117 · Cited by 1,146
Structure Elucidation of a Senescence Cross-Link from Human Extracellular Matrix
Sell, D. R., & Monnier, V. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88225-8 · Cited by 1,082
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Items 101–200 of 668
Autophagic receptor p62 protects against glycation‐derived toxicity and enhances viability
Aragonès, G., Dasuri, K., Olukorede, O., Francisco, S. G., Renneburg, C., Kumsta, C., Hansen, M., Kageyama, S., Komatsu, M., Rowan, S., et al. (2020) · Aging Cell · doi:10.1111/acel.13257 · Cited by 41
“…diets, is etiologically associated with multiple age-related disorders including CVD, diabetes, and AMD, but the mechanisms underlying these associations have not been well explored (Bejarano & Taylor, 2019; Chaudhuri et al., 2018; Moldogazieva & Mokhosoev, 2019; Vicente Miranda et al., 2016).”
BackgroundHyperglycemic memory in diabetic cardiomyopathy
Zhan, J., Chen, C., Wang, D. W., & Li, H. (2021) · Frontiers of Medicine · doi:10.1007/s11684-021-0881-2 · Cited by 42
“The late stages of Maillard reaction to form AGEs are reportedly irreversible [40], whereas multiple AGEmodified proteins, such as glycated fibrinogen and collagen, are stiffer and less susceptible to biological degradation [41,42].”
BackgroundWang, S., Jiao, F., Border, J. J., Fang, X., Crumpler, R. F., Liu, Y., Zhang, H., Jefferson, J. R., Guo, Y., Elliott, P. S., et al. (2021) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00438.2021 · Cited by 40
Witham, M. D., Granic, A., Pearson, E. R., Robinson, S. M., & Sayer, A. A. (2023) · Drugs & Aging · doi:10.1007/s40266-023-01042-4 · Cited by 45
“However, it is now clear that glycation is also an important contributor to the ageing phenotype even in individuals who do not have T2DM [33].”
BackgroundGuo, P., Chu, X., Wu, C., Qiao, T., Guan, W., Zhou, C., Wang, T., Tian, C., He, G., & Chen, G. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202318893 · Cited by 39
GLP-1RA and the possible skin aging
Paschou, I. A., Sali, E., Paschou, S. Α., Tsamis, K. I., Peppa, Μ., Ψαλτοπούλου, Θ., Nicolaidou, E., & Stratigos, A. J. (2025) · Endocrine · doi:10.1007/s12020-025-04293-w · Cited by 39
Physical exercise: An inducer of positive oxidative stress in skeletal muscle aging
Thirupathi, A., Pinho, R. A., & Chang, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117630 · Cited by 40
The Human Glyoxalase Gene Family in Health and Disease
Farrera, D. O., & Galligan, J. J. (2022) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.2c00182 · Cited by 39
Li, G., Jian, Z., Wang, H., Xu, L., Zhang, T., & Song, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/3319056 · Cited by 39
“Advanced glycation end products (AGEs) are commonly formed under chronic hyperglycemia, leading to abnormal protein, nucleic acid, and lipid functions [7].”
BackgroundMultiscale and multidisciplinary analysis of aging processes in bone
Ravazzano, L., Colaianni, G., Tarakanova, A., Xiao, Y.-B., Grano, M., & Libonati, F. (2024) · npj Aging · doi:10.1038/s41514-024-00156-2 · Cited by 37
“Despite the well-established accumulationofAGEsinproteinscontainedintissueofindividualsaffectedbyage-relatedchronicdiseases,itisnotyetclearwhetherAGEsareacause oraconsequenceofaging 52,53 .”
Network-Based Analysis of Fatal Comorbidities of COVID-19 and Potential Therapeutics
Chakrabarty, B., Das, D., Bulusu, G., & Roy, A. (2021) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2021.3075299 · Cited by 38
“It can be observed that all the three pathways common to the fatal comorbidities are also related to aging [69], [70], [71], [72].”
Methylglyoxal in the Brain: From Glycolytic Metabolite to Signalling Molecule
Yang, Z., Zhang, W., Han, L., & Cai, S. (2022) · Molecules · doi:10.3390/molecules27227905 · Cited by 36
“Here, Drosophila melanogaster and Caenorhabditis elegans can be used to explore AGE-related pathways in depth, and to identify and assess the drugs that may mitigate the detrimental effects of the development of AGE adducts [97].”
Dunn, T. C., Xu, Y., Bergenstal, R. M., Ogawa, W., & Ajjan, R. (2023) · Diabetes Technology & Therapeutics · doi:10.1089/dia.2023.0146 · Cited by 43
“40,41 A key difficulty has always been the lack of robust evidence directlylinking elevated HbA1c and increased tissueglycation.”
Sarcopenia and type 2 diabetes: Pathophysiology and potential therapeutic lifestyle interventions
Marcotte‐Chénard, A., Oliveira, B., Little, J. P., & Candow, D. G. (2023) · Diabetes & Metabolic Syndrome Clinical Research & Reviews · doi:10.1016/j.dsx.2023.102835 · Cited by 42
Update in the molecular mechanism and biomarkers of diabetic retinopathy
Zhu, H., Li, B., Huang, T., Wang, B., Li, S., Yu, K., Cai, L., Ye, Y., Chen, S., Zhu, H., et al. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167758 · Cited by 40
Sharifi‐Zahabi, E., Hajizadeh‐Sharafabad, F., Abdollahzad, H., Malekahmadi, M., & Rad, N. B. (2021) · Advances in Nutrition · doi:10.1093/advances/nmab072 · Cited by 36
Mitochondrion: A bridge linking aging and degenerative diseases
Zhang, L., Wu, J., Zhu, Z., He, Y., & Fang, R. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121666 · Cited by 38
Shariff, R., Du, Y., Dutta, M., Kumar, S., Thimmaiah, S., Doraiswamy, C., Kumari, A., Kale, V., Nair, N., Zhang, S., et al. (2021) · International Journal of Cosmetic Science · doi:10.1111/ics.12759 · Cited by 36
“Glycation is another key driver of skin ageing and, together with oxidative stress and inflammation, can lead to loss of collagen structure in the dermis and modify fibroblast functions [19].”
BackgroundMao, L., Yin, R., Yang, L., & Zhao, D. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.983723 · Cited by 42
Shen, Z., Chang, C.-Y., Yeh, C., Lu, C.-K., Hung, H., Wang, T.-W., Wu, K.-S., Tung, C.-Y., & Tsai, T. (2024) · Journal of Biomedical Science · doi:10.1186/s12929-024-01005-w · Cited by 38
“In addition, we found that hesperetin influences advanced glycation end products (AGE) and the receptor for the AGE (RAGE) pathway, which have been reported to be abnormally increased in several tissues during aging [65, 66].”
BackgroundThe Potential Role of Advanced Glycation End Products in the Development of Kidney Disease
Ma, Y., Wang, X., Lin, S., King, L., & Liu, L. (2025) · Nutrients · doi:10.3390/nu17050758 · Cited by 41
“About one-third of the products are excreted from the body through urine, while the remaining two-thirds stay in the body [25].”
Carotid ultrasound investigation as a prognostic tool for patients with diabetes mellitus
Hoke, M., Schillinger, M., Minar, E., Goliasch, G., Binder, C. J., & Mayer, F. (2019) · Cardiovascular Diabetology · doi:10.1186/s12933-019-0895-0 · Cited by 35
Glycan Mimetics from Natural Products: New Therapeutic Opportunities for Neurodegenerative Disease
Wang, W., Gopal, S., Pocock, R., & Xiao, Z. (2019) · Molecules · doi:10.3390/molecules24244604 · Cited by 36
“Glycation is a spontaneous age-dependent posttranslational modification which leads to advanced glycation end-products (AGEs) [24].”
BackgroundTeissier, T., Temkin, V., Pollak, R. D., & Cox, L. S. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.812157 · Cited by 35
Unveiling the Role of Schwann Cell Plasticity in the Pathogenesis of Diabetic Peripheral Neuropathy
Razak, N. H. A., Idris, J., Hassan, N. H., Zaini, F., Muhamad, N., & Daud, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910785 · Cited by 37
“The accumulation of advanced glycation end products (AGEs) is another causal factor in the development of oxidative stress in diabetes [71].”
BackgroundMetabolic and Mitochondrial Dysregulations in Diabetic Cardiac Complications
Tashkandi, A. J. A., Gorman, A., Mathers, E. M., Carney, G., Yacoub, A., Setyaningsih, W. A. W., Kuburas, R., & Margariti, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073016 · Cited by 35
“AGEs provoke glucotoxicity by altering the function of intracellular and extracellular proteins and binding to cell surface AGE receptors (RAGEs) [61].”
Sánchez, E., Betriu, À., Salas‐Salvadó, J., Pamplona, R., Barbé, F., Purroy, F. F., Farràs, C., Fernández, E., López‐Cano, C., Mizab, C., et al. (2019) · European Journal of Nutrition · doi:10.1007/s00394-019-01983-w · Cited by 35
Majeed, M., Majeed, S., Nagabhushanam, K., Lawrence, L., Arumugam, S., & Mundkur, L. (2020) · Cosmetics · doi:10.3390/cosmetics7040076 · Cited by 34
“Glycation in skin due to the undesired cross-linking of collagen proteins with sugar molecules eventually impairs the function of collagen fibers, leading to skin hardening and aging [38].”
BackgroundRAGE silencing deters CML-AGE induced inflammation and TLR4 expression in endothelial cells
Ramya, R., Coral, K., & Rajesh, B. S. (2021) · Experimental Eye Research · doi:10.1016/j.exer.2021.108519 · Cited by 37
p21-Activated kinase 1 (PAK1) in aging and longevity: An overview
Mohankumar, A., Sundararaj, P., & Tawata, S. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101443 · Cited by 34
Searching for plant-derived antivirals against dengue virus and Zika virus
Barbosa, E. D. C., Alves, T. M. D. A., Kohlhoff, M., Gaze, S. T., Pires, D. E. V., Figueiredo, A. C. C., Alves, É. A. R., Calzavara-Silva, C. E., Sobral, M., Kroon, E. G., et al. (2022) · Virology Journal · doi:10.1186/s12985-022-01751-z · Cited by 34
RAGE plays key role in diabetic retinopathy: a review
Lu, Z., Fan, B., Li, Y., & Zhang, Y. (2023) · BioMedical Engineering OnLine · doi:10.1186/s12938-023-01194-9 · Cited by 33
“AGEs accumulate during normal metabolism and aging, and their formation are accelerated under the action of inflammation, oxidative stress and hyperglycemia [20, 21].”
BackgroundKim, Y., Keogh, J. B., Deo, P., & Clifton, P. M. (2020) · Nutrients · doi:10.3390/nu12061767 · Cited by 33
“, methylglyoxal) is an arginine adduct [12].”
Raman spectroscopy of human skin for kidney failure detection
Bratchenko, L. A., Bratchenko, I. А., Khristoforova, Y. А., Artemyev, D. N., Konovalova, D. Y., Lebedev, P. A., & Zakharov, V. P. (2020) · Journal of Biophotonics · doi:10.1002/jbio.202000360 · Cited by 33
Advanced glycation end products and their adverse effects: The role of autophagy
Sruthi, C. R., & Raghu, K. G. (2021) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22710 · Cited by 33
Huang, Q., Hong, T., Zheng, M., Yang, Y., Zhu, Y., Jiang, Z., Ni, H., & Li, Q. (2023) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2023.103369 · Cited by 33
Feng, N., Feng, Y., Tan, J., Zhou, C. Y., Xu, J., Chen, Y., Xiao, J., He, Y., Wang, C., Zhou, M., et al. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125814 · Cited by 32
The Nigral Coup in Parkinson’s Disease by α-Synuclein and Its Associated Rebels
Sian‐Hülsmann, J., & Riederer, P. F. (2021) · Cells · doi:10.3390/cells10030598 · Cited by 30
“In addition, the accumulation of advanced glycation products (AGE) on nucleotides, lipids, and peptides/proteins are important components on the aging process [38] as they are structural crosslinkers that cause the transformation of soluble neurofilament proteins to insoluble LB [39,40].”
BackgroundRevealing Advanced Glycation End Products Associated Structural Changes in Serum Albumin
Naftaly, A., Izgilov, R., Omari, E., & Benayahu, D. (2021) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.1c00387 · Cited by 31
Suttisansanee, U., Thiyajai, P., Chalermchaiwat, P., Wongwathanarat, K., Pruesapan, K., Charoenkiatkul, S., & Temviriyanukul, P. (2021) · Plants · doi:10.3390/plants10081563 · Cited by 36
“Advanced glycation end products (AGEs), a group of molecules generated by a non-enzymatic glycation reaction between proteins and carbonyl compounds or reducing sugars, contribute to the prevalence of diabetes, neurodegenerative diseases, and aging [14].”
BackgroundRecent omics advances in hair aging biology and hair biomarkers analysis
Adav, S. S., & Ng, K. W. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102041 · Cited by 31
Gu, M. J., Lee, Y. R., Kim, D., Kim, Y., & Ha, S. K. (2024) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13412 · Cited by 34
Erkin‐Cakmak, A., Bains, Y., Caccavello, R. J., Noworolski, S. M., Schwarz, J., Mulligan, K. M., Lustig, R. H., & Gugliucci, A. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-02772 · Cited by 30
Self-citationSanzo, S. D., Spengler, K., Leheis, A., Kirkpatrick, J. M., Rändler, T. L., Baldensperger, T., Dau, T., Henning, C., Parca, L., Marx, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26982-6 · Cited by 30
Lin, S., Zhang, Q., Li, S., Qin, X., Cai, X., & Wang, H. (2022) · Cell Proliferation · doi:10.1111/cpr.13279 · Cited by 29
“In addition, the abnormal elevation in proteolytic activity also leads to growth factor degradation and subsequently attenuates angiogenesis in wound healing.(4,7,8) Based on the complex and variable physiological environment in vivo, it is still a challenge to design a delivery system for the changes of metabolic sta…”
BackgroundInfluentialMarkers and Mechanisms of Deterioration Reactions in Dairy Products
Fan, X., Wang, C., Cheng, M., Wei, H., Gao, X., Ma, M., Wang, X., & Li, Z. (2023) · Food Engineering Reviews · doi:10.1007/s12393-023-09331-9 · Cited by 30
Intrinsic and environmental basis of aging: A narrative review
Navarro, C., Salazar, J. J., Diaz, M. P., Chacín, M., Santeliz, R., Vera, I., D’Marco, L., Parra, H., Bernal, M. C., Castro, A. V., et al. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e18239 · Cited by 34
Fan, H., Wang, K., Zhao, X., Song, B., Yao, T., Liu, T., Gao, G., Lu, W., & Liu, C. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1335122 · Cited by 33
Zahir, A., Khan, I. A., Nasim, M., Azizi, M. N., & Azi, F. (2024) · Food Additives & Contaminants Part A · doi:10.1080/19440049.2024.2381210 · Cited by 29
“These compounds are produced through the classical Maillard reaction and have certain common characteristics such as fluorescence, covalent cross-link formation (among proteins), and the effect of changing the color of foodstuffs into yellow-brown colors (Chaudhuri et al. 2018).”
Amadori rearrangement products as potential biomarkers for inborn errors of amino-acid metabolism
van Outersterp, R. E., Moons, S. J., Engelke, U. F. H., Bentlage, H., Peters, T. M. A., van Rooij, A., Huigen, M. C. D. G., de Boer, S., van der Heeft, E., Kluijtmans, L. A. J., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01909-5 · Cited by 30
Controlled Formation of Carboxymethyllysine in Bone Matrix through Designed Glycation Reaction
Sroga, G. E., & Vashishth, D. (2021) · JBMR Plus · doi:10.1002/jbm4.10548 · Cited by 28
Protein glycation in diabetes mellitus
Shin, A., Connolly, S. M., & Kabytaev, K. (2023) · Advances in clinical chemistry · doi:10.1016/bs.acc.2022.11.003 · Cited by 34
Sandalova, E., Goh, J., Lim, Z. X., Lim, Z. M., Barardo, D., Dorajoo, R., Kennedy, B. K., & Maier, A. B. (2023) · GeroScience · doi:10.1007/s11357-023-00813-6 · Cited by 36
Copper metabolism and its role in diabetic complications: A review
Jia, D., Liu, L., Liu, W., Li, J., Jiang, X. M., & Xin, Y. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107264 · Cited by 30
Tian, S., Feng, J., Cao, Y., Shen, S., Cai, Y., Yang, D., Yan, R., Wang, L., Zhang, H., Zhong, X., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900413 · Cited by 26
“Source data are available for this fi gure. can react with lipids, nucleic acids, or with lysine and arginine residues of proteins to form advanced glycation end (AGE) products (Chaudhuri et al, 2018).”
BackgroundPARK7/DJ-1 as a Therapeutic Target in Gut-Brain Axis Diseases
Pap, D., Veres-Székely, A., Szebeni, B., & Vannay, Á. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126626 · Cited by 30
Lamprea-Montealegre, J. A., Arnold, A. M., McClelland, R. L., Mukamal, K. J., Djoussé, L., Biggs, M. L., Siscovick, D. S., Tracy, R. P., Beisswenger, P. J., Psaty, B. M., et al. (2022) · Journal of the American Heart Association · doi:10.1161/jaha.121.024012 · Cited by 28
The expanding impact of methylglyoxal on behavior-related disorders
de Almeida, G. R. L., Szczepanik, J. C., Selhorst, I., Cunha, M. P., & Dafré, A. L. (2022) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2022.110635 · Cited by 29
Glycation in Huntington’s Disease: A Possible Modifier and Target for Intervention
Brás, I. C., König, A., & Outeiro, T. F. (2019) · Journal of Huntington s Disease · doi:10.3233/jhd-190366 · Cited by 29
“opment of age-associated disorders [1].”
Age-Related Maintenance of the Autophagy-Lysosomal System Is Dependent on Skeletal Muscle Type
Fernando, R., Castro, J. P., Flore, T., Deubel, S., Grune, T., & Ott, C. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/4908162 · Cited by 27
“Among other posttranslational oxidative modifications, we investigated a product of glycosylation, pentosidine, known as advanced glycation end product and known to favor protein aggregation [33, 34].”
BackgroundMaran, A., Morieri, M. L., Falaguasta, D., Avogaro, A., & Fadini, G. P. (2022) · Diabetes Care · doi:10.2337/dc22-0980 · Cited by 27
Sultana, R., Parveen, A., Kang, M., Hong, S., & Kim, S. Y. (2024) · Scientific Reports · doi:10.1038/s41598-024-52037-z · Cited by 30
Normal ageing of the brain: Histological and biological aspects
Teissier, T., Boulanger, É., & Deramecourt, V. (2020) · Revue Neurologique · doi:10.1016/j.neurol.2020.03.017 · Cited by 37
The structure and stability analysis of the pea seed legumin glycosylated by oligochitosan
Yang, R., Liu, M., Liu, Y., Meng, D., Ma, T., Wang, C., Liu, J., Wang, Q., & Zhou, Z. (2020) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.10715 · Cited by 26
Bednarska, K., & Fecka, I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810026 · Cited by 26
“AGE formation in vivo is mostly attributed to the reaction of carbonyl groups of 1,2-dicarbonyl compounds (reactive carbonyl species, RCS) such as methylglyoxal (MGO) or glyoxal (GO) with the free amino groups of proteins and other biomacromolecules, resulting in the formation of covalently cross-linked aggregates [5].”
BackgroundModification of extracellular matrix proteins by oxidants and electrophiles
Yang-Jensen, K. C., Jørgensen, S. M., Chuang, C. Y., & Davies, M. J. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230860 · Cited by 26
Madiraju, S. R. M., Possik, E., Al‐Mulla, F., Nolan, C. J., & Prentki, M. (2025) · Endocrine Reviews · doi:10.1210/endrev/bnaf033 · Cited by 26
AGE/Non-AGE Glycation: An Important Event in Rheumatoid Arthritis Pathophysiology
Monu, M., Agnihotri, P., & Biswas, S. (2021) · Inflammation · doi:10.1007/s10753-021-01589-7 · Cited by 27
“Previously, increased AGEs levels were found to be related with Alzheimer’s disease (AD); their harmful effects were also studied in other prominent diseases such as atherosclerosis and inflammatory renal disease [22, 23].”
BackgroundWu, Y., Zong, M., Wu, H., He, D., Li, L., Zhang, X., Zhao, D., & Li, B. (2022) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202200046 · Cited by 26
Dietary advanced glycation end products and cancer risk in Japan: From the Takayama study
Wada, K., Nakashima, Y., Yamakawa, M., Hori, A., Seishima, M., Tanabashi, S., Matsushita, S., Tokimitsu, N., & Nagata, C. (2022) · Cancer Science · doi:10.1111/cas.15455 · Cited by 24
Hassan, H., Rawlinson, C., Lan, Y., Jenkins, S. I., & Chen, R. (2025) · Biomolecules · doi:10.3390/biom15111629 · Cited by 30
“Advanced glycation end products (AGEs), which accumulate in aging and AD, bind to RAGE, triggering inflammation and oxidative stress [116].”
Chen, M., Lin, J., Lin, H.-T., Chen, S.-Y., & Yen, G. (2019) · Food & Function · doi:10.1039/c9fo00240e · Cited by 24
The cardiovascular complications of diabetes: a striking link through protein glycation
Ahmad, M. N., Farah, A. I., & Al‐Qirim, T. M. (2020) · Romanian Journal of Internal Medicine · doi:10.2478/rjim-2020-0021 · Cited by 24
“These products undergo numerous irreversible rearrangement and dehydration reactions that lead to the generation of advanced glycation end-products (AGEs) [8].”
BackgroundInfluentialSirangelo, I., Borriello, M., Liccardo, M., Scafuro, M., Russo, P., & Iannuzzi, C. (2021) · Antioxidants · doi:10.3390/antiox10071127 · Cited by 24
Jin, Q., Lau, E. S. H., Luk, A. O. Y., Ozaki, R., Chow, E., So, T., Yeung, T., Loo, K.-M., Lim, C. K. P., Kong, A. P. S., et al. (2021) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2021.10.007 · Cited by 24
Pharmacological thiamine levels as a therapeutic approach in Alzheimer's disease
Gibson, G. E., Feldman, H., Zhang, S., Flowers, S. A., & Luchsinger, J. A. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.1033272 · Cited by 24
Sibbersen, C., & Johannsen, M. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190057 · Cited by 26
Petriv, N., Neubert, L., Vatashchuk, M., Timrott, K., Suo, H., Hochnadel, I., Huber, R., Petzold, C., Hrushchenko, A. O., Yatsenko, A. S., et al. (2021) · OncoImmunology · doi:10.1080/2162402x.2021.1874159 · Cited by 24
Yi, X., Song, Y., Xu, J., Wang, L., Liu, L., Huang, D., & Zhang, L. (2023) · Odontology · doi:10.1007/s10266-023-00813-0 · Cited by 23
“AGEs, as a kind of DAMPs, bind to the receptor RAGE on the cell membrane and trigger intracellular inflammatory response [28].”
Targeting the redox system for cardiovascular regeneration in aging
Allemann, M., Lee, P., Beer, J. H., & Saravi, S. S. S. (2023) · Aging Cell · doi:10.1111/acel.14020 · Cited by 23
“2 •− ) when cells become senescent, leading to the accumulation of oxidant products such as glycation end products (AGE) (Chaudhuri et al., 2018).”
BackgroundZhang, X., Yang, Y., Su, J., Zhong, H., & Fang, L. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5c02168 · Cited by 25
A Potential Role for Fructosamine-3-Kinase in Cataract Treatment
Bruyne, S. D., van Schie, L., Himpe, J., Somer, F. M. J. J. D., Everaert, I., Derave, W., den Broecke, C. V., Huizing, M. T., Bostan, N., Speeckaert, M. M., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083841 · Cited by 23
The Less We Eat, the Longer We Live: Can Caloric Restriction Help Us Become Centenarians?
Dakic, T. B., Jevdjovic, T. V., Vujovic, P. Z., & Mladenović, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126546 · Cited by 25
“Therefore, it is assumed that these changes may help slow down aging by decreasing the rate of protein glycation [79].”
BackgroundThe RAGE/multiligand axis: a new actor in tumor biology
Armando Rojas, R., Schneider, I., Lindner, C., González, I., & Morales, M. A. (2022) · Bioscience Reports · doi:10.1042/bsr20220395 · Cited by 24
Patil, R. S., & Tupe, R. S. (2023) · Medicinal Research Reviews · doi:10.1002/med.21987 · Cited by 23
Diabetes- versus smoking-related thrombo-inflammation in peripheral artery disease
Alnima, T., Meijer, R. I., Spronk, H. M. H., Warlé, M. C., & Cate, H. T. (2023) · Cardiovascular Diabetology · doi:10.1186/s12933-023-01990-6 · Cited by 27
“Generation of AGEs and other glycated proteins during hyperglycemia, as well as ROS upregulate TF production through activation of the NF-kB inflammatory pathway [73, 74].”
BackgroundShu, F., Gao, H., Wu, W., Yu, S., Zhang, L., Liu, H., Xiao, S., Xia, Z., & Zheng, Y. (2022) · Cell Biology International · doi:10.1002/cbin.11771 · Cited by 22
Zhang, R., Jiang, L., Li, G., Wu, J., Tian, P., Zhang, D., Qin, Y., Shi, Z., Gao, Z., Zhang, N., et al. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215589 · Cited by 21
“In brain, AGEs can mediate the progressive changes of neurostructural and functional deficits through a variety of ways [15–17].”
Cho, K., Kim, J., Nam, H.-S., Kang, D.-J., & Na, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710130 · Cited by 20
“Although the precise mechanisms are unknown, AGE-mediated neurodegeneration was implicated with inflammation, decreased proteostasis, and glycation of neurotransmitters [38].”
BackgroundBangar, N. S., Gvalani, A., Ahmad, S., Khan, M. S., & Tupe, R. S. (2022) · Glycobiology · doi:10.1093/glycob/cwac060 · Cited by 22
The Potential Influence of Advanced Glycation End Products and (s)RAGE in Rheumatic Diseases
Delrue, C., Speeckaert, R., Delanghe, J., & Speeckaert, M. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032894 · Cited by 24
“AGEs alter the three-dimensional integrity of various plasma proteins, which can cause functional abnormalities and contribute to the pathogenesis of a variety of diseases [5].”
BackgroundRungsang, T., Srivilai, J., Rakasawapokin, P., Rakasawapokin, P., Mungmai, L., Saesue, K., Aoonboontum, P., Plukham, N., Siriwipanan, P., Chaichanathawikit, P., et al. (2023) · Cosmetics · doi:10.3390/cosmetics10020043 · Cited by 22
“…This process spontaneously and naturally generates advanced glycation end-products (AGEs), which can directly lead to cellular damage to both extracellular and intracellular proteins, resulting in skin exhibiting signs of aging [48]. proteins, resulting in skin exhibiting signs of aging [48].”
O-GlcNAcylation is essential for therapeutic mitochondrial transplantation
Park, J. H., Tanaka, M., Nakano, T., Licastro, E., Nakamura, Y., Li, W., Esposito, E., Mandeville, E. T., Chou, S., Ning, M., et al. (2023) · Communications Medicine · doi:10.1038/s43856-023-00402-w · Cited by 21
“To further test this idea, we used methylglyoxal (MGO) to increase AGE in isolated mitochondria 20 (Fig.”
Martinez, C. S., Zheng, A., & Xiao, Q. (2024) · Antioxidants · doi:10.3390/antiox13111330 · Cited by 26
Esposito, S., Gialluisi, A., Castelnuovo, A. F. D., Costanzo, S., Pepe, A., Ruggiero, E., Curtis, A. D., Persichillo, M., Cerletti, C., Donati, M. B., et al. (2024) · American Journal of Clinical Nutrition · doi:10.1016/j.ajcnut.2024.10.006 · Cited by 23
Gut microbial evidence chain in high-salt diet exacerbates intestinal aging process
Liu, T., Zhao, L., Zhang, C.-Y., Li, X., Wu, T.-L., Dai, Y., Sheng, Y.-Y., Ren, Y., & Xue, Y.-Z. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1046833 · Cited by 21
Targeting α-synuclein post-translational modifications in Parkinson’s disease
Canever, J. B., Soares, E. S., de Avelar, N. C. P., & Cimarosti, H. (2022) · Behavioural Brain Research · doi:10.1016/j.bbr.2022.114204 · Cited by 22
SIRT6 : A potential therapeutic target for diabetic cardiomyopathy
Wu, T., Qu, Y., Xu, S., Wang, Y., Liu, X., & Ma, D. (2023) · The FASEB Journal · doi:10.1096/fj.202301012r · Cited by 23
Methylglyoxal suppresses microglia inflammatory response through NRF2-IκBζ pathway
Wei, S.-L., Yang, Y., Si, W.-Y., Zhou, Y., Li, T., Du, T., Zhang, P., Li, X.-L., Duan, R.-N., Duan, R., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102843 · Cited by 21
Wang, J., Liu, H., Xie, G., Cai, W., & Xu, J. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10872 · Cited by 21
Metadata
- Authors
- Chaudhuri, J., Bains, Y., Guha, S., Kahn, A., Hall, D., Bose, N., Gugliucci, A., & Kapahi, P.
- Affiliations
- Buck Institute for Research on Aging (US)
- Touro University California (US)
- Corresponding author
- Chaudhuri, Jyotiska
- Gugliucci, Alejandro
- Kapahi, Pankaj
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2018-09
- Volume
- 28
- Issue
- 3
- Pages
- 337-352
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC6355252
- OpenAlex
- W2892213316
- Cited by
- 669
- References
- 179
- Citations by year
- 2026: 70 · 2025: 118 · 2024: 91 · 2023: 107 · 2022: 83 · 2021: 116 · 2020: 48 · 2019: 34 · 2018: 1
- FWCI
- 6.44
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Touro Scholar (Touro College) (submittedVersion)
- Funders
- American Federation for Aging Research
- Larry L. Hillblom Foundation
- impact circle award
- NIH (R21 AG053066, RO1 AG045835, RO1 5RO1HL113887)
- Touro University California
- NIH/NIA (T32 AG000266)
- Hillblom Foundation Postdoctoral Fellowship
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Keywords
- advanced glycation end products, aging, metabolic disorders, AGE formation, age-related diseases, Drosophila melanogaster, Caenorhabditis elegans, invertebrate models, drug screening
- MeSH terms
- Aging, Animals, Drosophila melanogaster, Humans, Metabolic Diseases, Yeasts, Signal Transduction, Glycation End Products, Advanced, Caenorhabditis elegans, Oxidative Stress, Neurodegenerative Diseases, Models, Animal, Mice, Rats
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