Cited by 669Advanced Glycation End Products researchGenetics, Aging, and Longevity in Model OrganismsPotato Plant Research

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The Role of Advanced Glycation End Products in Aging and Metabolic Diseases: Bridging Association and Causality

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Chaudhuri, Jyotiska, Bains, Yasmin, Guha, Sanjib, Kahn, Arnold, Hall, David, Bose, Neelanjan, Gugliucci, Alejandro, Kapahi, Pankaj·2018·Cell Metabolism

DOI 10.1016/j.cmet.2018.08.014PMC PMC6355252

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Abstract

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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Retracted: Advanced glycation endproduct (AGE) accumulation and AGE receptor (RAGE) up‐regulation contribute to the onset of diabetic cardiomyopathy
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Background
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Background
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“However, once glycated, proteins can undergo further oxidation of the Amadori compounds to generate a complex set of advanced glycation end (AGE) products, resulting in decreased bioactivity of the protein [34].”
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“AGEs can accumulate with age particularly in long-lived proteins such as collagens and crystallins and their formation, especially when it enters the circulation, renders irreversible damage to all biological macromolecules [10, 22].”
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“The AGE-RAGE signaling pathway, which is involved in binding advanced glycation end damage products produced by the Maillard reaction and is associated with diabetes, 48 is also downregulated in select neurons.”
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“The accumulation of advanced glycation end products (AGEs) on nucleotides, lipids, and peptides/proteins is an inevitable part of the ageing process in all organisms, including humans [40,41].”
Background
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“In addition, premature aging has been associated with elevated generation of AGEs leading to increase in oxidative stress [78]).”
Background
Purification Process and In Vitro and In Vivo Bioactivity Evaluation of Pectolinarin and Linarin from Cirsium japonicum
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“Furthermore, the inhibition activity of the two compounds in t e BSA-MGO model was higher than hat in the BSA-fructose model, which suggests that t e two compounds may be more selective in targeting MGO than other α-dicarbonyl compounds to stop the glycation progress [29].”
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“AGE is a harmful molecule formed by macromolecular glycosylation, and RAGE is one of its transmembrane receptors [30].”
Background
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“25 AGEs also alter MMP activity in the ECM.”
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“The Maillard reaction products accumulate in long-lived tissue proteins (such as collagens, cartilage, and crystallins) with age, even without any diseases [9–11], and are inevitable components of the aging process in all eukaryotic organisms, including humans [12].”
Background
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Background
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Background
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“An important causal factor in aging is AGEs accumulation (Chaudhuri et al. 2018).”
Background
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Background
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“…GLO I, has a vital part in mitigating this damage by detoxifying MG. gly-oxalase system, particularly GLO I, has a vital part in mitigating this damage by detoxifying Dysfunction in this system could exacerbate cardiovascular complications associated with metabolic syndrome [66] (Table 1).”
BackgroundInfluential
Curcumin as a promising therapeutic agent for diabetic neuropathy: from molecular mechanisms to functional recovery
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“The aforementioned factors have made it difficult to create a model in which an AGE is linked to a single specific target and a single specific age-related disease [35].”
Background
Biocatalytic Reversal of Advanced Glycation End Product Modification
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“shown to be responsible for the disposal of AGE-peptides that can be found in the urine of diabetic rats and patients [35].”
Background
Rice bran modulates renal disease risk factors in animals submitted to high sugar-fat diet
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“Overall, in vitro and in vivo experiments in different animal models support the hypothesis that strategies for lowering AGEs deposition are neuroprotective (Bélanger et al., 2011; Chaudhuri et al., 2018).”
Background
Notch/NICD/RBP-J signaling axis regulates M1 polarization of macrophages mediated by advanced glycation end products
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“AGEs, formed by the body metabolites, reducing sugars and proteins under the action of non-enzymatic glycosylation (Maillard reaction), have been revealed to accumulate during aging or the progression of diabetes, which further promote inflammation and cause damage to the body [1, 21].”
Background
Unambiguous Identification of Glucose-Induced Glycation in mAbs and other Proteins by NMR Spectroscopy
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“A major cause of increased crosslinking is due to reactions between ECM proteins like collagen and elastin with AGEs.(23)”
Background
Evaluation of potential aging biomarkers in healthy individuals: telomerase, AGEs, GDF11/15, sirtuin 1, NAD+, NLRP3, DNA/RNA damage, and klotho
Borský, P., Holmannová, D., Andrýs, C., Kremláček, J., Fiala, Z., Kovaříková, H., Řeháček, V., Švadláková, T., Býma, S., Kučera, O., et al. (2023) · Biogerontology · doi:10.1007/s10522-023-10054-x · Cited by 17
“Pathologies such as inflammation, metabolic diseases, excessive alcohol consumption, smoking, and a high-caloric diet can accelerate the production of AGEs and aging (Chaudhuri et al. 2018).”
Background
DNA Aptamer Raised against Advanced Glycation End Products Improves Sperm Concentration, Motility, and Viability by Suppressing Receptors for Advanced Glycation End Product-Induced Oxidative Stress and Inflammation in the Testes of Diabetic Mice
Mori, Y., Terasaki, M., Osaka, N., Fujikawa, T., Yashima, H., Saito, T., Kataoka, Y., Ohara, M., Higashimoto, Y., Matsui, T., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115947 · Cited by 14
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Background
Nutrients and Natural Substances for Hypoglycemic Effects and Management in Diabetic Retinopathy
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Activation of GPR40 Suppresses AGE-Induced Reduction of Type II Collagen and Aggrecan in Human SW1353 Chondrocytes
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Recent developments in in-vitro assessment of advanced glycation end products
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“AGEs may form during normal metabolism and are a known hallmark of the ageing process [91].”
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Advanced glycation end products are associated with cardiovascular risk in the Mexican population
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Dysregulation of hypoxia-inducible factor 1α in the sympathetic nervous system accelerates diabetic cardiomyopathy
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“Considering that the sympathetic system plays a crucial role in modulating glucose metabolism of target organs (as reviewed in [87, 88]), it is reasonable to hypothesize that a dysfunctional sympathetic system could potentially have an impact on glucose metabolism, glucose uptake, and/or lead to increased oxidative st…”
BackgroundInfluential
Empagliflozin decreases ageing-associated arterial stiffening and vascular fibrosis under normoglycemic conditions
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Mechanism of action of Panax ginseng alcohol extract based on orexin-mediated autophagy in the treatment of sleep and cognition in aged sleep-deprived rats
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Functional evaluation of laminarin butyl esters: Antioxidant, skin-whitening, and anti-wrinkle properties
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Type 2 diabetes and depression via microvascular dysfunction, neurodegeneration, inflammation, advanced glycation end products ( AGEs ), and arterial stiffness
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Dietary Betaine and Fatty Acids Change Circulating Single-Carbon Metabolites and Fatty Acids in the Dog
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Background
Anti-inflammaging effects of vitamin D in human gingival fibroblasts with advanced glycation end product stimulation
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Circulating Irisin and esRAGE as Early Biomarkers of Decline of Metabolic Health
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“An imbalance between production and detoxification leads to their accumulation and the onset and progression of different disorders, such as cardiometabolic diseases [39].”
Background
Dietary Intake of Nε-carboxymethyl-lysine, a Major Advanced Glycation End Product, is Not Associated with Increased Risk of Mortality in Japanese Adults in the Takayama Study
Nagata, C., Wada, K., Yamakawa, M., Nakashima, Y., Koda, S., Uji, T., & Oba, S. (2020) · Journal of Nutrition · doi:10.1093/jn/nxaa230 · Cited by 13
Dermal ultrasound measurements for bone quality assessment : An investigation of advanced glycation endproducts derived from confocal fluorescence microscopy
Haffer, H. P. H., Chiapparelli, E. A., Moser, M., Muellner, M., Dodo, Y., Amini, D. A., Zhu, J., Miller, T. T., Han, Y. X., Donnelly, E. L., et al. (2022) · Journal of Orthopaedic Research® · doi:10.1002/jor.25350 · Cited by 12
“According to the hypothesis, fAGEs as a marker of tissue aging, is expected to increase with age over time.(32,33) A possible explanation for our contradictory findings is supported by in vitro and animal model studies that consider the accumulation of AGEs as a marker of reduced bone turnover resulting from changed r…”
Result
Selective disruption of Drp1-independent mitophagy and mitolysosome trafficking by an Alzheimer’s disease relevant tau modification in a novelCaenorhabditis elegansmodel
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Self-citation
Investigation on the Contents of Nε-carboxymethyllysine, Nε-carboxyethyllysine, and N-nitrosamines in Commercial Sausages on the Chinese Market
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Background
Epigenetic meets metabolism: novel vulnerabilities to fight cancer
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“Due to the further oxidation and rearrangement, these early-stage products are able to be converted to advanced glycation end products (AGEs) that contain complicated aromatic ring structures (such as glucosepane) [81].”
Background
Non-Genomic Hallmarks of Aging—The Review
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“Aging is associated with increased levels of AGEs that depend on the increased production and degradation activity of glyoxalases [64–66].”
Background
Transcriptomic and proteomic investigation of the ameliorative effect of total polyphenolic glycoside extract on hepatic fibrosis in Lamiophlomis rotata Kudo via the AGE/RAGE pathway
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Raman Spectroscopy in Cellular and Tissue Aging Research
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“…lipids, and proteins throughout various tissues and cells as an individual ages, thereby altering the biophysical and bio-chemical properties of tissues or organs (Avery and Bailey 2006; DeGroot et al. 2001) and resulting in age-related diseases and complications (Chaudhuri et al. 2018).”
Functional Inactivation of Drosophila GCK Orthologs Causes Genomic Instability and Oxidative Stress in a Fly Model of MODY-2
Mascolo, E., Liguori, F., Mecarelli, L. S., Amoroso, N., Merigliano, C., Amadio, S., Volonté, C., Contestabile, R., Tramonti, A., & Vernı̀, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020918 · Cited by 12
“These toxic compounds are produced by hyperglycemia through non-enzymatic glycating reactions occurring between an excess of glucose and the amino groups of proteins and DNA [49].”
BackgroundInfluential
Carboxyl terminus of HSP70‐interacting protein attenuates advanced glycation end products‐induced cardiac injuries by promoting NFκB proteasomal degradation
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Cinnamaldehyde ameliorates diabetes-induced biochemical impairments and AGEs macromolecules in a pre-clinical model of diabetic nephropathy
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“Moreover, recent studies suggest that AGEs have been linked to various degenerative diseases [10–12] including diabetes [13], Alzheimer’s disease [14, 15], chronic kidney disease [16], atherosclerosis [17, 18], and cancer via receptor-mediated signaling cascade [19].”
Harnessing phytochemicals to combat diabetes: Insights into molecular pathways and therapeutic advances
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Background
Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation
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“In this regard, RCS-induced protein glycation and the derived accumulation of advanced glycation end products (AGEs) during the aging process have received great attention, because these events may be the key bridge connecting aging with different human diseases such as atherosclerosis, diabetes, or neurodegenerative…”
Background
Inhibition by pesticides of the DJ-1/Park7 protein related to Parkinson disease.
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Shanmugam, M. M., Chaudhuri, J., Sellegounder, D., Sahu, A. K., Guha, S. K., Chamoli, M., Hodge, B. A., Bose, N., Amber, C., Farrera, D. O., et al. (2023) · eLife · doi:10.7554/elife.82446 · Cited by 10
Self-citation
Pubertal exposure to dietary advanced glycation end products disrupts ductal morphogenesis and induces atypical hyperplasia in the mammary gland
Krisanits, B. A., Schuster, R., Randise, J. F., Nogueira, L. M., Lane, J. T., Panguluri, G. A., Li, H., Helke, K. L., Cuitiño, M. C., Koivisto, C. S., et al. (2023) · Breast Cancer Research · doi:10.1186/s13058-023-01714-4 · Cited by 12
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Background
Comprehensive Analyses of Advanced Glycation end Products and Heterocyclic Amines in Peanuts during the Roasting Process
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Background
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A Network Pharmacology Study on the Molecular Mechanism of Protocatechualdehyde in the Treatment of Diabetic Cataract
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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
ORCID: Chaudhuri, Jyotiska
Guha, Sanjib
Hall, David
Bose, Neelanjan
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)
DOI: 10.1016/j.cmet.2018.08.014
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 368 d)
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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The Role of Advanced Glycation End Products in Aging and Metabolic Diseases: Bridging Association and Causality

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