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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]
In the citing paper
“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]
In the citing paper
“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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“…impairing insulin signaling, or the modification of the three arginine residues in the AMP binding site of AMP kinases, decreasing their activity (23); and (2) interference with activation of downstream proteins involved in cell insulin signaling, including IRS-1 and Akt, through RAGE-dependent…”
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“Although AGEs are produced physiologically in the human body, when present in high concentrations, they can cause a number of pathological states, including diabetic complications [5,6].”
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“90 This process is also known to contribute to the pathology of several metabolic diseases, including diabetes and atherosclerosis as well as conditions of oxidative stress and inflammation, which are frequently associated with neurodegenerative diseases.”
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The AGE-RAGE axis associates with chronic pulmonary diseases and smoking in the Rotterdam study
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“AGEs contribute to aging and age-related diseases [10–12] by forming cross-links between proteins [13], modifying protein structure and functions [14], and via their receptor (RAGE) to induce inflammation [9, 15].”
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“The Maillard theory of aging proposes that the slow and continuous accumulation of AGEs may be a factor in aging rates (10).”
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“Amino acids can form multifunctional proteins and nucleotides required for body growth, they also play a regulatory role in hormone regulation and metabolic pathways (Chaudhuri et al., 2018; Liu et al., 2021).”
BackgroundNew Chalcone-Derived Molecule for the Topical Regulation of Hyperpigmentation and Skin Aging
Martínez-Gutiérrez, A., Bertran, A., Noya, T., Pena-Rodríguez, E., Gómez-Escalante, S., Pascual, S., Luis, L., & González, M. C. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16111405 · Cited by 7
“Several molecular mechanisms have been described as protective against the aging process, such as autophagy [14], a reduction in advanced glycation end products (AGEs) [15], or antioxidation [16], as some examples.”
Early and advanced glycation end product analysis from women with PCOS on metformin
Ambekar, A. S., Naredi, N., Malakar, D., Vashum, Y., Misra, P., & Kulkarni, M. J. (2025) · Reproductive Biology · doi:10.1016/j.repbio.2024.100993 · Cited by 6
Zhou, J., Wang, S., Wang, Q., Zhao, R., Wang, D., Xie, H., Du, Y., Xu, Y., Deng, J., Huang, Y., et al. (2025) · Food & Function · doi:10.1039/d4fo05578k · Cited by 6
de Mello, N. P., Berger, M. T., Lagerborg, K. A., Yan, Y., Wettmarshausen, J., Keipert, S., Weidner, L., Tokarz, J., Möller, G., Ciciliot, S., et al. (2025) · Molecular Metabolism · doi:10.1016/j.molmet.2025.102163 · Cited by 6
“While systemic AGEs mostly arise from a combination of glucose exposure, defective glycolysis, and insuf fi cient detoxi fi cation, w 30 % are directly from dietary sources [7].”
InfluentialLin, H. R., Liu, S., Yang, Q., Li, J., Wang, J., Semyachkina-Glushkovskaya, O. V., Li, D., Yu, T., & Zhu, D. Y. (2025) · Aging Cell · doi:10.1111/acel.70261 · Cited by 7
“Advanced glycation end products (AGEs) are a complex and heterogeneous group that accumulate significantly in the aging brain via the nonenzymatic Maillard reaction, the polyol pathway, and lipid peroxidation (Chaudhuri et al. 2018; Ott et al. 2014).”
InfluentialBayarsaikhan, G., Bayarsaikhan, D., Oh, P. C., Kang, W. C., & Lee, B. (2021) · Antioxidants · doi:10.3390/antiox10030434 · Cited by 6
“In contrast, in the intracellular environment, AGE formation from glycation is driven by glucose metabolites such as glyoxal, methylglyoxal, and 3-deoxyglucosone [40].”
Backgroundde Araújo, R. L., de Pinho, C. L. C., Farias, F. O., Zanzarini, I. D. S., Moure, V. R., Valdameri, G., Igarashi‐Mafra, L., & Mafra, M. R. (2024) · Industrial Crops and Products · doi:10.1016/j.indcrop.2023.118012 · Cited by 6
A comprehensive model for the biochemistry of ageing, senescence and longevity
Keizer, H. G., Brands, R., Oosting, R. S., & Seinen, W. (2024) · Biogerontology · doi:10.1007/s10522-024-10097-8 · Cited by 6
“…of biochemistry has allowed us to develop a concise and comprehensive model of aging, that uses widely accepted biochemical principles to explain how spontaneously formed advanced glycation end products (AGEs) (Chaudhuri et al. 2018), ultimately lead to age-related phenotypic changes (Fig.”
Lee, H., Liu, K., Yang, Y.-H., Liao, J., Lin, B.-S., Wu, Z.-Z., Chang, A. C., Tseng, C., Wang, M., & Tsai, Y.-S. (2024) · The Analyst · doi:10.1039/d4an00057a · Cited by 6
Gurumayum, N., Devi, M. B., Khound, P., Bhattacharya, A., Sarma, H., Khan, M. R., & Devi, R. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.11.016 · Cited by 6
AGEs in cooked meat: Production, detection, and mechanisms of its inhibition by plant extracts
Han, X. F., Shi, Z., Wu, Z., Zeng, X., Sun, Y., Yao, K., Shen, Q. W., Fan, X., Luo, J., & Pan, D. (2025) · Food Research International · doi:10.1016/j.foodres.2025.116067 · Cited by 6
Oliveira, A. R., Chevalier, C., Wargny, M., Pakulska, V., Caradeuc, C., Cloteau, C., Letertre, M. P. M., Giraud, N., Bertho, G., Bigot‐Corbel, E., et al. (2025) · Clinical Chemistry · doi:10.1093/clinchem/hvaf035 · Cited by 6
PNS protects brain against ischemic injury by acting as an antagonist for AGE/RAGE signaling
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Zhu, J., Lian, S.-F., Zhong, H., Sun, R., Xiao, Z., & Li, H. (2023) · Biosensors · doi:10.3390/bios13020170 · Cited by 7
Topical Application of Deglycating Enzymes as an Alternative Non-Invasive Treatment for Presbyopia
Delanghe, J., Beeckman, J., Beerens, K., Himpe, J., Bostan, N., Speeckaert, M. M., Notebaert, M., Huizing, M. T., & Aken, E. V. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087343 · Cited by 6
Egawa, T., Ogawa, T., Yokokawa, T., Kido, K., Iyama, R., Zhao, H., Kurogi, E., Goto, K., & Hayashi, T. (2024) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13444 · Cited by 6
In vivo assay and modelling of protein and mitochondrial turnover during aging
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Photocaged dicarbonyl probe provides spatiotemporal control over protein glycation
Hurben, A. K., Ge, P., Bouchard, J. L., Doran, T. M., & Tretyakova, N. Y. (2021) · Chemical Communications · doi:10.1039/d1cc06651j · Cited by 6
Health-Promoting Potential of Mandarin Pomace Extracts Enriched with Phenolic Compounds
Fernández‐Fernández, A. M., Dellacassa, E. S., Curbelo, R., Nardin, T., Larcher, R., Medrano, A., & del Castillo, M. D. (2024) · Nutrients · doi:10.3390/nu16142370 · Cited by 6
“Furthermore, hyperglycemia promotes protein glycation, generating advanced glycation end products (AGEs) in tissues, which increase the release of free radicals and pro-inflammatory molecules [10,11].”
BackgroundZhang, C., Zhang, J., Huang, T., Jiang, P., Qie, X., Mo, L., Li, M., Lou, A., Shen, Q. W., Luo, J., et al. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.140763 · Cited by 5
Advanced glycation end-products accelerate amyloid deposits in adipocyte’s lipid droplets
Izgilov, R., Kislev, N., Omari, E., & Benayahu, D. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07211-6 · Cited by 5
“Chronic hyperglycemia accelerates this process and exposes the cells to high levels of carbonyl metabolites, which react with lipids and proteins to generate advanced glycation end products (AGEs) through the Maillard reaction [5 – 7].”
Cai, Y., Hu, S., Liu, J., Luo, J., Li, W., Tang, J., Liu, S., Dong, R., Yang, Y., Tu, L., et al. (2025) · Chinese Medical Journal · doi:10.1097/cm9.0000000000003792 · Cited by 5
“[9,10] Recent studies have suggested that the levels of advanced glycation end products (AGEs) induced by hyperglycemia, [11] oxidative stress, [12,13] protein glycosylation (O-linked β -N-acetylglucosamine), [14] and other pathways are associated with diabetic vascular calcification.”
Biomarkers for diabetic peripheral neuropathy: A narrative review of advanced glycation end products
Srivastava, S., Bisen, A. C., Srivastava, D., & Awasthi, H. (2025) · NeuroMarkers. · doi:10.1016/j.neumar.2025.100149 · Cited by 6
Vizuete, A. F. K., & Gonçalves, C. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04142-8 · Cited by 5
Chen, L., Mori, Y., Nishii, S., Sakamoto, M., Ohara, M., Yamagishi, S., & Sekizawa, A. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13237158 · Cited by 5
Ottone, O. K., Mundo, J. J., Kwakye, B. N., Slaweski, A., Collins, J. A., Wu, Q., Connelly, M. A., Niaziorimi, F., van de Wetering, K., & Risbud, M. V. (2025) · Aging Cell · doi:10.1111/acel.14504 · Cited by 5
Pu, C., Shi, D., Ingrassia, M., Gedeon, H., Chu, T., Zhang, J., & Wang, C. (2025) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.70067 · Cited by 5
Berardi, D., Farrell, G., Al-Sultan, A., McCulloch, A., Hall, N. M., Sousa, R. P. P., Jimenez, M., Selman, C., Bellantuono, I., Johnson, C. H., et al. (2025) · Aging Cell · doi:10.1111/acel.70127 · Cited by 5
“…et al. 2017), SASP-mediated lipid dysregulation (Zeng et al. 2024), alongside metabolic rewiring in glucose/glutamine metabolism (Wiley and Campesi 2021) leading to the accumulation of advanced glycation end-products (AGEs) (Chaudhuri et al. 2018) further complement these analyses.”
Shin, E. S., Park, Y. S., & Nam, S. H. (2019) · Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC) · doi:10.1109/embc.2019.8857867 · Cited by 5
“AGE accumulation in tissues is known to be related to the progression of aging, cardiovascular disease and diabetic complications [2].”
BackgroundMaasen, K., Hanssen, N. M. J., Kallen, C., Stehouwer, C. D. A., van Greevenbroek, M. M. J., & Schalkwijk, C. G. (2021) · Antioxidants · doi:10.3390/antiox10020219 · Cited by 5
Kamari, V. E., Rodríguez, K. M. G., Moser, C., Currier, J. S., Kelesidis, T., Stein, J. H., Brown, T. T., Howell, S. K., Beisswenger, P. J., & McComsey, G. A. (2021) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofab423 · Cited by 5
“Previous data have shown that the accumulation of AGEs has many consequences that can lead to a wide variety of pathological effects [26, 33].”
BackgroundMethodChen, X., Wang, C., Zhou, D., Zhao, G., Li, Z., & Duan, N. (2023) · Experimental Cell Research · doi:10.1016/j.yexcr.2023.113765 · Cited by 5
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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