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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AGEs, including glycoxidation products, play a fundamental role in human aging and in aging of vertebrate and invertebrate model organisms.
“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]
The Abstract describes AGE accumulation as an inevitable component of aging in humans and other eukaryotes, and the model-organism section reviews vertebrate and invertebrate studies. But the Abstract says AGEs are linked to, and only perhaps responsible for, aging-related changes; the Conclusions say their causal effects remain poorly understood. Calling their role in aging “fundamental” states that role more firmly than the review does. (LLM, conf=0.84)
Experimental — accuracy not yet measuredLevels of glycoxidation products increase as a function of age in several tissues, dependent on dietary intake and hyperglycemic conditions.
“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]
AGEs are relevant as biomarkers of aging and age-related diseases.
“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]
Under pathological conditions, RAGEs can be upregulated and participate in various aging-related pathophysiologies.
“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]
RAGEs are expressed widely in various cells and organs.
“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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Extending the Spectrum of α-Dicarbonyl Compounds in Vivo
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Glyoxalase 1 Modulation in Obesity and Diabetes
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Advanced glycation end-products and bone fractures
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“Several studies have addressed the buildup of AGEs in long-lived proteins (Hammes et al., 1999; Sell et al., 1992; Vashishth, 2009).”
BackgroundGlyoxal Formation and Its Role in Endogenous Oxalate Synthesis
Lange, J. N., Wood, K. D., Knight, J. L., Assimos, D. G., & Holmes, R. P. (2012) · Advances in Urology · doi:10.1155/2012/819202 · Cited by 97 · see citing works
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Serum Advanced Glycosylation End Products: A New Class of Uremic Toxins?
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“Due to this fact, AGE adducts are one of the classical ‘middle toxins’ associated with renal failure (Vlassara, 1994).”
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Impairing L-Threonine Catabolism Promotes Healthspan through Methylglyoxal-Mediated Proteohormesis
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Identification of Fructosamine Residues Deglycated by Fructosamine-3-kinase in Human Hemoglobin
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Advanced Glycation End Products in Renal Failure
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“These pathways, which depend on glomerular filtration and tubular function, are severely compromised in chronic and end-stage renal failure (Thornalley, 2005a, 2006).”
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“…of sensitive LC-MS/MS techniques, a more comprehensive representation of the role of the kidney in AGE control emerged, including the fate of small peptides and free adducts (Agalou et al., 2005; Rabbani and Thornalley, 2009; Rabbani et al., 2007; Thornalley, 2005b; Thornalley and Rabbani, 2009).”
MethodEnhanced RAGE-mediated NFκB stimulation in inflamed hemodialysis patients
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Advanced Glycation End Products Induce Obesity and Hepatosteatosis in CD-1 Wild-Type Mice
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Measurement of Protein Glycation, Glycated Peptides, and Glycation Free Adducts
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“…of sensitive LC-MS/MS techniques, a more comprehensive representation of the role of the kidney in AGE control emerged, including the fate of small peptides and free adducts (Agalou et al., 2005; Rabbani and Thornalley, 2009; Rabbani et al., 2007; Thornalley, 2005b; Thornalley and Rabbani, 2009).”
BackgroundMethodEvidence Against a Role for the Parkinsonism-associated Protein DJ-1 in Methylglyoxal Detoxification
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Glycation free adduct accumulation in renal disease: the new AGE
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“…of sensitive LC-MS/MS techniques, a more comprehensive representation of the role of the kidney in AGE control emerged, including the fate of small peptides and free adducts (Agalou et al., 2005; Rabbani and Thornalley, 2009; Rabbani et al., 2007; Thornalley, 2005b; Thornalley and Rabbani, 2009).”
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Identification of glyoxalase 1 polymorphisms associated with enzyme activity
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Hormesis enables cells to handle accumulating toxic metabolites during increased energy flux
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A newly discovered neurotoxin ADTIQ associated with hyperglycemia and Parkinson's disease
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Parkinsonism-associated protein DJ-1 is a bona fide deglycase
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Renal Microvascular Injury in Diabetes: RAGE and Redox Signaling
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Fructosamine 3-kinase-related protein and deglycation in human erythrocytes
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Glycation potentiates neurodegeneration in models of Huntington’s disease
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“Inactivation of AMPK would favor lipogenesis, insulin resistance, and hyperglycemia, all hallmarks of MetS and diabetes (Gugliucci, 2009, 2016, 2017).”
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“Polymorphisms associated with the glyoxalase Glo1 gene have been associated with the development of nephropathy and retinopathy in Type 2 diabetics (Gale et al., 2004; Kalousová et al., 2008; Wu et al., 2011).”
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Measurement of Lens Autofluorescence Can Distinguish Subjects With Diabetes From Those Without
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Fructosamine 3-kinase and other enzymes involved in protein deglycation
SCHAFTINGEN, E. V., Delpierre, G., Collard, F., Fortpied, J., Gemayel, R., Wiame, E., & Veiga‐da‐Cunha, M. (2007) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.12.002 · Cited by 25 · see citing works
Common polymorphisms in the glyoxalase-1 gene and their association with pro-thrombotic factors
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Advanced glycation in diabetes, aging and age-related diseases: editorial and dedication
Monnier, V. M., & Taniguchi, N. (2016) · Glycoconjugate Journal · doi:10.1007/s10719-016-9704-0 · Cited by 24 · see citing works
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DJ‐1 is a Parkinson's disease susceptibility gene in southern Italy
Marco, E. D., Annesi, G., Tarantino, P., Nicoletti, G., Civitelli, D., Messina, D. N., Annesi, F., Arabia, G., Salsone, M., Condino, F., et al. (2009) · Clinical Genetics · doi:10.1111/j.1399-0004.2009.01310.x · Cited by 22 · see citing works
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“…of sensitive LC-MS/MS techniques, a more comprehensive representation of the role of the kidney in AGE control emerged, including the fate of small peptides and free adducts (Agalou et al., 2005; Rabbani and Thornalley, 2009; Rabbani et al., 2007; Thornalley, 2005b; Thornalley and Rabbani, 2009).”
MethodMechanisms Linking Aging, Diseases and Biological Age Estimation
Núñez Martínez, P. (2017) · CRC Press eBooks · doi:10.1201/9781315371382 · Cited by 18 · see citing works
Gugliucci, A. (2009) · Medical Hypotheses · doi:10.1016/j.mehy.2009.06.044 · Cited by 16 · cited 1× · see citing works
“Inactivation of AMPK would favor lipogenesis, insulin resistance, and hyperglycemia, all hallmarks of MetS and diabetes (Gugliucci, 2009, 2016, 2017).”
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“The latter are unstable and spontaneously decompose into inorganic phosphate and 3-deoxyglucosone, regenerating the unglycated amine (Gugliucci, 2005).”
BackgroundSelf-citationReprint of “Accumulation of modified proteins and aggregate formation in aging”
Nowotny, K., Jung, T., Grune, T., & Höhn, A. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.10.001 · Cited by 15 · see citing works
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DJR-1.2 of Caenorhabditis elegans is induced by DAF-16 in the dauer state
Lee, J., Kim, C., Kim, J., & Park, C. (2013) · Gene · doi:10.1016/j.gene.2013.04.032 · Cited by 10 · see citing works
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Methylglyoxal concentrations differ in standard and washed neonatal packed red blood cells
Kiefer, A. S., Fleming, T. H., Eckert, G. J., Poindexter, B. B., Nawroth, P. P., & Yöder, M. C. (2013) · Pediatric Research · doi:10.1038/pr.2013.243 · Cited by 8 · see citing works
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From discoveries in ageing research to therapeutics for healthy ageing
Campisi, J., Kapahi, P., Lithgow, G. J., Melov, S., Newman, J. C., & Verdin, E. (2019) · Nature · doi:10.1038/s41586-019-1365-2 · Cited by 1,389 · see citing works
Self-citationKang, Q., & Yang, C. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101799 · Cited by 1,075 · see citing works
“During the process, large amounts of free radicals are produced, which in turn promotes AGE formation [69].”
BackgroundAdvanced Glycation End Products and Diabetes Mellitus: Mechanisms and Perspectives
Khalid, M., Petroianu, G. A., & Adem, A. (2022) · Biomolecules · doi:10.3390/biom12040542 · Cited by 931 · see citing works
“Maillard reaction generates highly reactive numerous intermediate carbonyl precursors of AGEs [20,29].”
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Mechanisms of Oxidative Stress in Metabolic Syndrome
Masenga, S. K., Kabwe, L. S., Chakulya, M., & Kirabo, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097898 · Cited by 786 · see citing works
“(3) Triose phosphates produce methylglyoxal, the main precursor of advanced glycation end products (AGEs) [63].”
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Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411 · see citing works
Ultra-processed Foods and Cardiovascular Diseases: Potential Mechanisms of Action
Juul, F., Vaidean, G., & Parekh, N. (2021) · Advances in Nutrition · doi:10.1093/advances/nmab049 · Cited by 374 · see citing works
Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367 · see citing works
“Although the study of AGEs is an active area of investigation in the field of aging research (184), it is still unknown how proteins are selected to be glycated and the biological role of glycation in neurodegeneration is not well-understood (185).”
BackgroundProtein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
“In line with earlier findings on glycoxidation levels in aging [153], studies from 2019 suggest an age-related increase in skin AF, pentosidine levels and total amount of AGEs [141,170,171].”
BackgroundResultSong, J., He, Y., Luo, C., Feng, B., Ran, F., Xu, H., Ci, Z., Xu, R., Han, L., & Zhang, D. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105109 · Cited by 308 · see citing works
Sirt3-mediated mitophagy regulates AGEs-induced BMSCs senescence and senile osteoporosis
Guo, Y., Jia, X., Cui, Y., Song, Y., Wang, S., Geng, Y., Li, R., Gao, W., & Fu, D. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101915 · Cited by 300 · see citing works
“The formation of AGEs, typical resulting from Maillard reaction or non-enzymatic glycation process, has been known to be irreversible and its accumulation could lead to the dysfunction of macromolecules such as nucleic acids, lipids and proteins [5].”
BackgroundMetformin: Is it a drug for all reasons and diseases?
Triggle, C. R., Mohammed, I., Bshesh, K., Marei, I., Ye, K., Ding, H., MacDonald, R. S., Hollenberg, M. D., & Hill, M. A. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155223 · Cited by 282 · see citing works
Ma, J., Li, Y., Yang, X., Liu, K., Zhang, X., Zuo, X., Ye, R., Wang, Z., Shi, R., Meng, Q., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01430-7 · Cited by 257 · see citing works
Klotho, Aging, and the Failing Kidney
Buchanan, S. J., Combet, E., Stenvinkel, P., & Shiels, P. G. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00560 · Cited by 243 · see citing works
Inflammation and Premature Ageing in Chronic Kidney Disease
Ebert, T., Pawelzik, S., Witasp, A., Arefin, S., Hobson, S., Kublickiene, K. R., Shiels, P. G., Bäck, M., & Stenvinkel, P. (2020) · Toxins · doi:10.3390/toxins12040227 · Cited by 242 · see citing works
“Thus, the AGE–RAGE axis induces renal cytosolic oxidative stress and mitochondrial dysfunction, as well as inflammation [26,61].”
BackgroundRamasubbu, K., & Rajeswari, V. D. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04587-x · Cited by 249 · see citing works
Huo, S., Wang, Q., Shi, W., Peng, L., Jiang, Y., Zhu, M., Guo, J., Peng, D., Wang, M., Men, L., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021667 · Cited by 232 · see citing works
“Glucose, fructose or more reactive dicarbonyls react nonenzymatically with nucleophilic groups on proteins, preferentially with ε-amino groups of lysines and N-terminal-amino groups, following a succession of rearrangements of intermediate compounds and subsequently converting to stable AGEs [20,21].”
BackgroundInfluentialWHO working definition of vitality capacity for healthy longevity monitoring
Bautmans, I., Knoop, V., Thiyagarajan, J. A., Maier, A. B., Beard, J., Freiberger, E., Belsky, D. W., Aubertin‐Leheudre, M., Mikton, C. R., Cesari, M., et al. (2022) · The Lancet Healthy Longevity · doi:10.1016/s2666-7568(22)00200-8 · Cited by 240 · see citing works
Nanodelivery of Natural Antioxidants: An Anti-aging Perspective
Vaiserman, A. M., Koliada, A. K., Zayachkivska, A., & Lushchak, O. V. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00447 · Cited by 208 · see citing works
“Chronic oxidative stress condition also leads to an enhanced level of nonenzymatic, covalent attachment of glucose molecules to proteins, resulting in an elevated generation of advanced glycation end products (AGEs), known to be substantially contributed to aging and age-associated disorders (Kim C. S. et al., 2017; C…”
BackgroundEffects of Hyperglycemia and Diabetes Mellitus on Coagulation and Hemostasis
Li, X., Weber, N. C., Cohn, D. M., Hollmann, M. W., DeVries, J. H., Hermanides, J., & Preckel, B. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10112419 · Cited by 182 · see citing works
“Generation of advanced glycation end-products, glycated lipids or proteins formed during hyperglycemia [40], as well as reactive oxygen species enhance TF production through activation of the nuclear factor (NF)-κB inflammatory pathway [41].”
BackgroundLi, Y., Peng, Y., Shen, Y., Zhang, Y., Liu, L., & Yang, X. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2076064 · Cited by 156 · see citing works
“It mainly occurred in the process of oxidative stress and gradually accumulated in normal tissue with age (Chaudhuri et al. 2018).”
BackgroundOxidative stress, nutritional antioxidants and beyond
Guo, Q., Li, F., Duan, Y., Wen, C., Wang, W., Zhang, L., Huang, R., & Yin, Y. (2019) · Science China Life Sciences · doi:10.1007/s11427-019-9591-5 · Cited by 154 · see citing works
Lee, J., Yun, J., & Ko, S. (2022) · Nutrients · doi:10.3390/nu14153086 · Cited by 155 · see citing works
“α-DCs are inevitable in anaerobic glycolysis, the polyol pathway, and lipid peroxidation [31,32].”
BackgroundProteomics in aging research: A roadmap to clinical, translational research
Moaddel, R., Ubaida‐Mohien, C., Tanaka, T., Lyashkov, A., Basisty, N., Schilling, B., Semba, R. D., Franceschi, C., Gorospe, M., & Ferrucci, L. (2021) · Aging Cell · doi:10.1111/acel.13325 · Cited by 139 · see citing works
Elastic fibers: formation, function, and fate during aging and disease
Schmelzer, C. E. H., & Duca, L. (2021) · FEBS Journal · doi:10.1111/febs.15899 · Cited by 139 · see citing works
Methylglyoxal Metabolism and Aging-Related Disease: Moving from Correlation toward Causation
Kold-Christensen, R., & Johannsen, M. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.10.003 · Cited by 128 · see citing works
Microglial phagocytosis in aging and Alzheimer's disease
Gabandé‐Rodríguez, E., Keane, L., & Capasso, M. (2020) · Journal of Neuroscience Research · doi:10.1002/jnr.24419 · Cited by 127 · see citing works
“AGEs accumulate during normal aging and in AD, diabetes, atherosclerosis or chronic kidney disease; their binding to RAGE causes inflammation and oxidative damage (Chaudhuri et al., 2018).”
BackgroundXenobiotic metabolism and transport in Caenorhabditis elegans
Hartman, J. H., Widmayer, S. J., Bergemann, C. M., King, D. E., Morton, K. S., Romersi, R. F., Jameson, L. E., Leung, M. C. K., Andersen, E. C., Taubert, S., et al. (2021) · Journal of Toxicology and Environmental Health Part B · doi:10.1080/10937404.2021.1884921 · Cited by 124 · see citing works
“…as α-dicarbonyls, and/or various diets or dietary components were described elsewhere and are not covered in detail herein (Blackwell et al. 2015; Chaudhuri et al. 2018; Ferguson and Bridge 2019; Gonzalez-Moragas et al. 2017b; Hoffmann and Partridge 2015; Olsen and Gill 2017; Shore and Ruvkun…”
BackgroundMitochondrial ROS and mitochondria-targeted antioxidants in the aged heart
Bou‐Teen, D., Kaludercic, N., Weissman, D., Turan, B., Maack, C., Lisa, F. D., & Ruiz‐Meana, M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.043 · Cited by 119 · see citing works
Li, M., Shen, M., Lu, J., Yang, J., Huang, Y., Liu, L., Fan, H., Xie, J., & Xie, M. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110839 · Cited by 110 · see citing works
Inflammation in Metabolic Cardiomyopathy
Wenzl, F. A., Ambrosini, S., Mohammed, S. A., Kraler, S. C., Lüscher, T. F., Costantino, S., & Paneni, F. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.742178 · Cited by 109 · see citing works
Zhao, D., Sheng, B., Wu, Y., Li, H., Xu, D., Nian, Y., Mao, S., Li, C., Xu, X., & Zhou, G. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b05891 · Cited by 107 · see citing works
Clinical/Translational Aspects of Advanced Glycation End-Products
Zeng, C., Li, Y., Ma, J., Niu, L., & Tay, F. R. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.08.005 · Cited by 107 · see citing works
Effects of exercise on cellular and tissue aging
Carapeto, P. V., & Aguayo-Mazzucato, C. (2021) · Aging · doi:10.18632/aging.203051 · Cited by 107 · see citing works
“AGEs, major inflammatory mediators in macrophages, affect the progression of age-related atherosclerosis and diabetes and inhibit AMPK activity through allosteric competitive binding to its AMP-binding site in the γ subunit [142].”
BackgroundPolyphenols and AGEs/RAGE axis. Trends and challenges
González, I., Morales, M. A., & Armando Rojas, R. (2019) · Food Research International · doi:10.1016/j.foodres.2019.108843 · Cited by 101 · see citing works
Zhang, Z., Yang, Z., Wang, S., Wang, X., & Mao, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116413 · Cited by 101 · see citing works
Miyamoto, S. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0286-9 · Cited by 96 · see citing works
Targeting metabolic pathways for extension of lifespan and healthspan across multiple species
Parkhitko, A. A., Filine, E., Mohr, S. E., Moskalev, A., & Perrimon, N. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101188 · Cited by 90 · see citing works
“Methylglyoxal (MGO) is a highly reactive carbonyl species that is mainly produced from the glycolytic intermediates glyceraldehyde 3-phosphate (GA3P) and dihydroxyacetone phosphate (DHAP) but can be also generated during the catabolism of threonine and other metabolic processes (Fig.”
BackgroundInfluentialAging Biomarkers: From Functional Tests to Multi‐Omics Approaches
Kudryashova, K. S., Burka, K., Kulaga, A. Y., Vorobyeva, N. S., & Kennedy, B. K. (2020) · PROTEOMICS · doi:10.1002/pmic.201900408 · Cited by 86 · see citing works
Collagen crosslinking: effect on structure, mechanics and fibrosis progression
Kong, W., Lyu, C., Liao, H., & Du, Y. (2021) · Biomedical Materials · doi:10.1088/1748-605x/ac2b79 · Cited by 85 · see citing works
“In the process of many chronic diseases associated with aging and inflammatory pro-gressions, the majority of collagen fiber crosslinking is mediated by lysyl oxidases (LOX), transglutaminases (TGase) and the NEG products—advanced glycosylation end products (AGEs) [13–32] (figure 2).”
Bone health in diabetes and prediabetes
Costantini, S., & Conte, C. (2019) · World Journal of Diabetes · doi:10.4239/wjd.v10.i8.421 · Cited by 84 · see citing works
Spagnuolo, L., Posta, S. D., Fanali, C., Dugo, L., & Gara, L. D. (2021) · Antioxidants · doi:10.3390/antiox10030424 · Cited by 82 · see citing works
“It is worth noting that the accumulation of glycation adducts during aging is involved in several diseases such as diabetes, renal diseases, and Alzheimer’s [18].”
BackgroundDNA Damage-Induced Inflammatory Microenvironment and Adult Stem Cell Response
Cinat, D., Coppes, R. P., & Barazzuol, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.729136 · Cited by 78 · see citing works
The Effects of Dietary Advanced Glycation End-Products on Neurocognitive and Mental Disorders
D'Cunha, N. M., Sergi, D., Lane, M. M., Naumovski, N., Gamage, E., Rajendran, A., Kouvari, M., Gauci, S., Dissanayaka, T. D., Marx, W., et al. (2022) · Nutrients · doi:10.3390/nu14122421 · Cited by 80 · see citing works
“Over decades, AGEs accumulate at the cellular level in body tissue, where they have the potential to irreversibly increase the rate of cellular aging [10,11].”
BackgroundSchalkwijk, C. G., Micali, L. R., & Wouters, K. (2022) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2022.11.004 · Cited by 76 · see citing works
Scheen, M., Giraud, R., & Bendjelid, K. (2021) · Physiological Reports · doi:10.14814/phy2.14713 · Cited by 79 · see citing works
“Modifications in extracellular matrix proteins such as collagen have been observed as a consequence of AGE pathobiology (Jyotiska et al., 2018; Karina et al., 2014; Leor et al., 1993).”
BackgroundInfluentialAdvanced glycation end products in diabetic retinopathy and phytochemical therapy
Kang, Q., Dai, H., Jiang, S., & Yu, L. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1037186 · Cited by 72 · see citing works
Guha, S. K., Johnson, G. V. W., & Nehrke, K. W. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02084-0 · Cited by 71 · see citing works
Self-citationDiabetes and cardiovascular disease: inter-relation of risk factors and treatment
Sharma, A., Mittal, S., Aggarwal, R., & Chauhan, M. K. (2020) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-020-00151-w · Cited by 71 · see citing works
“signaling pathways activation as well as are also involved in the modification of intracellular protein function [82].”
BackgroundCurrent Approach to the Pathogenesis of Diabetic Cataracts
Mrugacz, M., Pony-Uram, M., Bryl, A., & Zorena, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076317 · Cited by 71 · see citing works
“Moreover, the binding of AGEs to a specific receptor for advanced glycation end-products (RAGEs) on the cell surface activating the NADPH oxidase (Nox) and NF-κB [61] becomes an additional signal for intracellular ROS formation [62].”
BackgroundPathological and Inflammatory Consequences of Aging
García‐Domínguez, M. (2025) · Biomolecules · doi:10.3390/biom15030404 · Cited by 75 · see citing works
“This process results in the formation of advanced glycation end-products (AGEs), a diverse group of molecular complexes that progressively accumulate with age [129].”
Ali, M. Y., Zaib, S., Rahman, M., Jannat, S., Iqbal, J., Park, S. K., & Chang, M. S. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.03.018 · Cited by 71 · see citing works
Xue, C., Deng, P., Quan, W., Li, Y., He, Z., Qin, F., Wang, Z., Chen, J., & Zeng, M. (2022) · Food Control · doi:10.1016/j.foodcont.2022.109038 · Cited by 70 · see citing works
Parfitt, G. M., Coccia, E., Goldman, C., Whitney, K. R., Reyes, R., Sarrafha, L., Nam, K. H., Sohail, S., Jones, D. R., Crary, J. F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-44732-2 · Cited by 70 · see citing works
“cell function and is a feature of normal aging 2 .”
Age-related changes in dermal collagen physical properties in human skin
He, T., Fisher, G. J., Kim, A. J., & Quan, T. (2023) · PLoS ONE · doi:10.1371/journal.pone.0292791 · Cited by 69 · see citing works
Aging of the Retina: Molecular and Metabolic Turbulences and Potential Interventions
Campello, L., Singh, N., Advani, J., Mondal, A. K., Corso‐Díaz, X., & Swaroop, A. (2021) · Annual Review of Vision Science · doi:10.1146/annurev-vision-100419-114940 · Cited by 67 · see citing works
Sellegounder, D., Zafari, P., Rajabinejad, M., Taghadosi, M., & Kapahi, P. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107806 · Cited by 68 · see citing works
Self-citationFrom obesity to Alzheimer's disease through insulin resistance
Terzo, S., Amato, A., & Mulè, F. (2021) · Journal of Diabetes and its Complications · doi:10.1016/j.jdiacomp.2021.108026 · Cited by 62 · see citing works
The Role of DJ-1 in Cellular Metabolism and Pathophysiological Implications for Parkinson’s Disease
Mencke, P., Boussaad, I., Romano, C., Kitami, T., Linster, C. L., & Krüger, R. (2021) · Cells · doi:10.3390/cells10020347 · Cited by 62 · see citing works
“An accumulation of AGEs can interfere with biological function and result in cellular damage [65].”
BackgroundLiu, L., Zheng, C., Zhao, N., Zhu, T., Hu, C.-B., Zhang, N., Chen, J., Zhang, K., Zhang, S., Liu, J.-X., et al. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202300019 · Cited by 61 · see citing works
The anti-aging mechanism of ginsenosides with medicine and food homology
Tian, T., Ko, C.-N., Luo, W., Li, D., & Yang, C. (2023) · Food & Function · doi:10.1039/d3fo02580b · Cited by 62 · see citing works
Shu, M., Cheng, W., Jia, X., Bai, X., Zhao, Y., Lu, Y., Zhu, L., Zhu, Y. S., Wang, L., Shu, Y., et al. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00715-5 · Cited by 58 · see citing works
“Upon the ligation with AGEs, RAGE can modulate intracellular signal transduction pathways, such as the NF-ĸB signaling pathways, activate pro-inflammatory responses and trigger a cascade of pro-atherogenic responses (Chaudhuri et al. 2018; Hudson and Lippman 2018).”
BackgroundAn updated review of functional ingredients of Manuka honey and their value-added innovations
Wang, S., Qiu, Y., & Zhu, F. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.138060 · Cited by 57 · see citing works
Tang, D., He, W.-J., Zhang, Z., Shi, J., Wang, X., Gu, W.-T., Chen, Z., Xu, Y., Chen, Y., & Wang, S. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153777 · Cited by 56 · see citing works
Oxidative stress and aging: synergies for age related diseases
Santos, D. F., Simão, S., Nóbrega, C., Bragança, J., Castelo‐Branco, P., & Araújo, I. M. (2024) · FEBS Letters · doi:10.1002/1873-3468.14995 · Cited by 63 · see citing works
“Aging is also implicated in the increase in the formation of advanced glycated end products (AGEs), which in turn are strong inducers of oxidative stress [162].”
Baldensperger, T., Eggen, M., Kappen, J., Winterhalter, P. R., Pfirrmann, T., & Glomb, M. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-64265-0 · Cited by 54 · see citing works
Copper, Iron, Selenium and Lipo-Glycemic Dysmetabolism in Alzheimer’s Disease
Aaseth, J., Skalny, A. V., Roos, P. M., Alexander, J., Aschner, M., & Tinkov, A. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179461 · Cited by 57 · see citing works
“Briefly, protein glycation is a series of non-enzymatic reactions collectively termed the Maillard reaction [58] (Figure 1).”
BackgroundYuan, X., Nie, C., Liu, H., Ma, Q., Peng, B., Zhang, M., Chen, Z., & Li, J. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1991265 · Cited by 51 · see citing works
“…pathogenesis of other chronic diseases, such as nonalcoholic fatty liver disease (Fernando et al. 2019), cancer (Ahmad et al. 2018), diabetes and diabetic complications (Parveen et al. 2021), Alzheimer’s disease (Prasad 2019), atherosclerosis (Wang et al. 2018) and obesity (Chaudhuri et al. 2018).”
BackgroundProteomic architecture of valvular extracellular matrix
Bouchareb, R., Guauque-Olarte, S., Snider, J., Zaminski, D., Anyanwu, A., Stelzer, P., & Lebeche, D. (2021) · JACC: Basic to Translational Science · doi:10.1016/j.jacbts.2020.11.008 · Cited by 52 · see citing works
“MetS may affect aortic valve ECM through the overaccumulation of advanced glycation end-products (11).”
BackgroundEndocrine Regulation of Lifespan in Insect Diapause
Hutfilz, C. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.825057 · Cited by 53 · see citing works
“…for hydrolyzation of advanced glycation end products (AGEs), which are associated with diseases of old age in various Frontiers in Physiology | www.frontiersin.org 8 February 2022 | Volume 13 | Article 825057 model organisms (Oudes et al., 1998; Semba et al., 2010; Chaudhuri et al., 2018).”
BackgroundGranic, A., Hurst, C., Dismore, L. L., Dodds, R. M., Witham, M. D., Robinson, S. M., & Sayer, A. A. (2022) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2022.111744 · Cited by 52 · see citing works
“…inconclusive (Ebert et al., 2019; Dalal et al., 2009; Kim et al., 2018; Moriwaki eta l, 2021), these may act as scavengers of circulating AGEs, thus inhibiting the AGE-RAGE binding and the activation of pro-inflammatory pathway (Chaudhuri et al., 2018; Daussin et al., 2021; Riuzzi et al., 2018).”
BackgroundInfluentialHuang, W., Zhang, Z., Colucci, M., Deng, L., Yang, M., Huang, X., Zhou, X. J., Jin, Y., Lazzarini, E., Balbi, C., et al. (2024) · Environment International · doi:10.1016/j.envint.2024.108447 · Cited by 52 · see citing works
Xue, C., Quan, W., Li, Y., He, Z., Qin, F., Wang, Z., Chen, J., & Zeng, M. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.132660 · Cited by 51 · see citing works
Polyphenols: A Comprehensive Review of their Nutritional Properties
Ebrahimi, P., & Lante, A. (2021) · The Open Biotechnology Journal · doi:10.2174/1874070702115010164 · Cited by 50 · see citing works
Luo, Y., Zhang, J., Ho, C., & Li, S. (2022) · Food Science and Human Wellness · doi:10.1016/j.fshw.2021.12.012 · Cited by 50 · see citing works
Dong, L., Li, Y., Chen, Q., Liu, Y., Wu, Z., Pan, D., Yan, N., & Liu, L. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2213768 · Cited by 49 · see citing works
“Besides, the accumulation of AGEs was also a propulsive factor for oxidative stress and inflammation (Chaudhuri et al. 2018).”
The association between dietary and skin advanced glycation end products: the Rotterdam Study
Chen, J., Waqas, K., Tan, R. C., Voortman, T., Ikram, M. A., Nijsten, T. E. C., de Groot, C. P. G. M., Uitterlinden, A. G., & Zillikens, M. C. (2020) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqaa117 · Cited by 48 · see citing works
“Several human, animal, and in vitro studies have suggested the involvement of dietary AGEs (dAGEs) in, for example, metabolic diseases (8, 9), cardiovascular diseases (9, 10), diabetes (11), Alzheimer’s disease (12), food allergy (13), and hampered skeletal muscle growth and muscle contractile function (14).”
BackgroundDiverse proteins aggregate in mild cognitive impairment and Alzheimer’s disease brain
Kepchia, D., Huang, L., Dargusch, R., Rissman, R. A., Shokhirev, M. N., Fischer, W. H., & Schubert, D. A. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-00641-2 · Cited by 48 · see citing works
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“Hyperglycemia-mediated autoxidation normally results from the production of major AGE precursors, namely, methylglyoxal (MGO) and glyoxal (GO) [4].”
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“Our proteomic survey included a battery of PTMs de - scribed as advanced glycation and lipoxidation end products (AGEs and ALEs, respectively), whose accumulation are known to robustly track with age and age-associated diseases (Chaudhuri et al., 2018).”
MethodSerum AGE/RAGEs as potential biomarker in idiopathic pulmonary fibrosis
Machahua, C., Montes‐Worboys, A., Planas‐Cerezales, L., Buendia-Flores, R., Molina‐Molina, M., & Vicens‐Zygmunt, V. (2018) · Respiratory Research · doi:10.1186/s12931-018-0924-7 · Cited by 47 · see citing works
Dietary Advanced Glycation End Products: Their Role in the Insulin Resistance of Aging
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“In summary, enteral AGES, orally absorbed AGEs, or AGE precursors may contribute to the pathogenesis of IR by different underlying mechanisms: (1) direct modification of signaling molecules, such as insulin itself, which reduces its biological activity and affinity for the insulin receptor and therefore impairs insuli…”
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Overview of Metformin and Neurodegeneration: A Comprehensive Review
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Metagenomic analysis characterizes stage-specific gut microbiota in Alzheimer’s disease
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“We observed signi fi cant differences in cognitive behavior between the groups through behavioral tests.”
SARS‐CoV‐2 and the possible connection to ERs, ACE2, and RAGE: Focus on susceptibility factors
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Carbonyl Stress in Red Blood Cells and Hemoglobin
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Pivotal role of AGE-RAGE axis in brain aging with current interventions
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Eye on the horizon: The metabolic landscape of the RPE in aging and disease
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Public Health Risks Associated with Food Process Contaminants – A Review
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“AGEs activate RAGE (the receptors for AGEs) signaling and cause carbonyl stress, leading to activation of NF-kB, inflammatory response, ROS production, and endothelial dysfunction [162,163].”
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“[132] Chaudhuri J, Bains Y, Guha S, Kahn A, Hall D, Bose N, et al.”
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“Introduction 17 Glycation of circulating, cellular, and matrix proteins by glucose are thought to be a major factor in 18 pathogenesis of diabetes and related cardiovascular diseases.(1) This process is known as the Maillard 19 reaction and begins with the nucleophilic addition between an amino group of a protein and…”
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- 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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