Cited by 526Advanced Glycation End Products researchAlzheimer's disease research and treatmentsDementia and Cognitive Impairment Research

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Advanced glycation endproducts and their receptor RAGE in Alzheimer's disease

Srikanth, Velandai, Maczurek, Annette, Phan, Thanh, Steele, Megan, Westcott, Bernadette, Juskiw, Damian, Münch, Gerald·2011·Neurobiology of Aging

DOI 10.1016/j.neurobiolaging.2009.04.016

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Abstract

Alzheimer's disease (AD) is the most common dementing disorder of late life. Although there might be various different triggering events in the early stages of the disease, they seem to converge on a few characteristic final pathways in the late stages, characterized by inflammation and neurodegeneration. In this review, we revisit the hypothesis that advanced glycation endproducts (AGEs) and their receptor RAGE may play an important role in disease pathogenesis. Accumulation of AGEs in cells and tissues is a normal feature of aging, but is accelerated in AD. In AD, AGEs can be detected in pathological deposits such as amyloid plaques and neurofibrillary tangles. AGEs explain many of the neuropathological and biochemical features of AD such as extensive protein crosslinking, glial induction of oxidative stress and neuronal cell death. Oxidative stress and AGEs initiate a positive feedback loop, where normal age-related changes develop into a pathophysiological cascade. RAGE and its decoy receptor soluble RAGE, may contribute to or protect against AD pathogenesis by influencing transport of β-amyloid into the brain or by manipulating inflammatory mechanisms. Targeted pharmacological interventions using AGE-inhibitors, RAGE-antagonists, RAGE-antibodies, soluble RAGE or RAGE signalling inhibitors such as membrane-permeable antioxidants may be promising therapeutic strategies to slow down the progression of AD.

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Background
Skin autofluorescence, reflecting accumulation of advanced glycation end products, and the risk of dementia in a population-based cohort
Mooldijk, S. S., Lu, T., Waqas, K., Chen, J., Vernooij, M. W., Ikram, M. A., Zillikens, M. C., & Ikram, M. A. (2024) · Scientific Reports · doi:10.1038/s41598-024-51703-6 · Cited by 23
“…suggests that AGEs in the brain induce inflammation and oxidative stress, resulting in synaptic dysfunction and neuronal damage, and contribute to deposition and accumulation of dementia related pathologies both intracellularly (e.g. tau) and extracellularly (e.g. amyloid β) 5,6,10,11,14,33,34 .”
Background
Voltammetric Detection of S100B Protein Using His-Tagged Receptor Domains for Advanced Glycation End Products (RAGE) Immobilized onto a Gold Electrode Surface
Mikuła, E., Wysłouch‐Cieszyńska, A., Zhukova, L., Puchalska, M., Verwilst, P., Dehaen, W., Radecki, J., & Radecka, H. (2014) · Sensors · doi:10.3390/s140610650 · Cited by 24
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Background
Therapeutic Effectiveness of Anti-RAGE Antibody Administration in a Rat Model of Crush Injury
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Ascorbic acid leads to glycation and interferes with neurite outgrowth
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“Glycation is a process that correlates with many age-related diseases, especially in the metabolically active nervous system (Münch et al., 1997; Srikanth et al., 2011).”
Differential contribution of possible pattern‐recognition receptors to advanced glycation end product–induced cellular responses in macrophage‐like RAW264.7 cells
Watanabe, M., Toyomura, T., Wake, H., Liu, K., Teshigawara, K., Takahashi, H. K., Nishibori, M., & Mori, S. (2019) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1843 · Cited by 24
Type 3 diabetes (Alzheimer's disease): new insight for promising therapeutic avenues
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Background
Ketogenic Diet: A Promising Neuroprotective Composition for Managing Alzheimer’s Diseases and its Pathological Mechanisms
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Influence of ADAM10 Polymorphisms on Plasma Level of Soluble Receptor for Advanced Glycation End Products and The Association With Alzheimer’s Disease Risk
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RAGE signaling is required for AMPA receptor dysfunction in the hippocampus of hyperglycemic mice
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Qifu-Yin attenuates AGEs-induced Alzheimer-like pathophysiological changes through the RAGE/NF-κB pathway
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“, have been implicated as important contributors in the pathogenesis of Alzheimer’s disease ([40]).”
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Alzheimer's Disease and Frontotemporal Dementia: A Review of Pathophysiology and Therapeutic Approaches
Kelliny, S., Zhou, X., & Bobrovskaya, L. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70046 · Cited by 27
“Accumulation of AGEs is a feature of aging (Srikanth et al. 2011) and age-related diseases such as diabetes mellitus (Münch et al. 1998).”
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Yu, J. H., Kim, R. E. Y., Park, S. Y., Lee, D. Y., Cho, H. J., Kim, N. H., Yoo, H. J., Seo, J. A., Kim, S. G., Choi, K. M., et al. (2022) · Diabetes Obesity and Metabolism · doi:10.1111/dom.14958 · Cited by 24
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The Circulating Level of Soluble Receptor for Advanced Glycation End Products Displays Different Patterns in Ulcerative Colitis and Crohn’s Disease: A Cross-Sectional Study
Ciccocioppo, R., Imbesi, V., Betti, E., Boccaccio, V., Kružliak, P., Gallia, A., Cangemi, G. C., Maffè, G. C., Vanoli, A., Merante, S., et al. (2015) · Digestive Diseases and Sciences · doi:10.1007/s10620-015-3619-7 · Cited by 22
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Role of the Glyoxalase System in Alzheimer’s Disease
Jiang, L., Wang, J., Wang, Z., Huang, W., Yang, Y., Cai, Z., & Li, K. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180413 · Cited by 20
“…the Schiff base undergoes a special intramolecular reforming reaction to produce a chemically stable ketoamine compound that undergoes a slow molecular rearrangement, dehydration, and condensation to form the irreversible binding of AGEs with protein or an amine-containing substrate [43, 60, 61].”
Influential
Preparation of 4-Flexible Amino-2-Arylethenyl-Quinoline Derivatives as Multi-Target Agents for the Treatment of Alzheimer’s Disease
Wang, X., Zhao, C.-P., Zhong, L.-C., Zhu, D.-L., Mai, D.-H., Liang, M.-G., & He, M. (2018) · Molecules · doi:10.3390/molecules23123100 · Cited by 22
Activation of α7nAChR by PNU282987 improves cognitive impairment through inhibiting oxidative stress and neuroinflammation in D-galactose induced aging via regulating α7nAChR/Nrf2/HO-1 signaling pathway
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An integrated proteomics and metabolomics analysis of methylglyoxal-induced neurotoxicity in a human neuroblastoma cell line
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“Furthermore, AGEs could induce cell dysfunction through interacting with the receptor for AGEs (RAGE), triggering oxidative stress and in ﬂ ammatory responses 10 .”
Glycation in Alzheimer’s Disease and Type 2 Diabetes: The Prospect of Dual Drug Approaches for Therapeutic Interventions
Ayoub, S., Arabi, M., Al-Najjar, Y. A., Laswi, I., Outeiro, T. F., & Châari, A. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05051-9 · Cited by 23
“Cross-linked AGE-modiﬁed Aβ and tau aggregates accumulate and resist clearance, disrupting proteostasis and accelerating synaptic loss [53].”
Targeting Scavenger Receptors in Inflammatory Disorders and Oxidative Stress
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“, these conditions can be cleared by the application of therapeutic strategies targeting membrane-permeable antioxidants and AGE-inhibiting molecules by blocking AGE–RAGE-induced inflammation or the transportation of harmful molecules [79].”
Background
Co-Expression Network Analysis Identifies Molecular Determinants of Loneliness Associated with Neuropsychiatric and Neurodegenerative Diseases
Potashkin, J., Santiago, J., & Quinn, J. P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065909 · Cited by 22
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“Furthermore, RAGE overexpression in microglia has also been found to exacerbate interleukin-6 (IL-6) and TNF-a production, and Ab deposition within AD-related vulnerable brain loci of mutant APP/ RAGE rodents (Fang et al., 2010; Srikanth et al., 2011).”
Background
Current Perspectives and Mechanisms of Relationship between Intestinal Microbiota Dysfunction and Dementia: A Review
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Cornuside ameliorates cognitive impairments via RAGE/TXNIP/NF-κB signaling in Aβ1-42 induced Alzheimer’s disease mice
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“After a RAGE is one of receptors mediating the toxicity of A β in the brain, the abnormal overexpression of RAGE is found in the brain of AD patients, as well as in AD mice (Choi et al. 2014; Srikanth et al. 2011).”
Bidirectional modulation of Alzheimer’s disease via gut microbiota: rescue by fecal transplantation from healthy donors and aggravation by colitis-associated dysbiosis
Zhou, C., Feng, X., Liu, H., Cai, T., Li, Y., & Fan, H. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1593854 · Cited by 19
Nonenzymatic Browning and Protein Aggregation in Royal Jelly during Room-Temperature Storage
Qiao, J., Wang, X., Liu, L., & Zhang, H. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b04955 · Cited by 19
RAGE pathways play an important role in regulation of organ fibrosis
Liu, J., Jin, Z., Wang, X., Jakoš, T., Zhu, J., & Yuan, Y. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121713 · Cited by 20
In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR
Li, R., Rajan, R., Wong, W. C. V., Reid, D. G., Duer, M. J., Somovilla, V. J., Martínez‐Sáez, N., Bernardes, G. J. L., Hayward, R., & Shanahan, C. M. (2017) · Chemical Communications · doi:10.1039/c7cc06624d · Cited by 18
Intellectual Disability Associated With Pyridoxine-Responsive Epilepsies: The Need to Protect Cognitive Development
Hassel, B., Rogne, A. G., & Hope, S. (2019) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2019.00116 · Cited by 19
“AGEs may trigger pathological inflammation reactions through their activation of AGE receptors [RAGEs; (47)].”
Background
RAGE Signaling in Melanoma Tumors
Olaoba, O. T., Kadasah, S. F., Vetter, S. W., & Leclerc, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238989 · Cited by 28
Contributive Role of Hyperglycemia and Hypoglycemia Towards the Development of Alzheimer’s Disease
Chakrabarty, R., Yousuf, S., & Singh, M. P. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02846-y · Cited by 20
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The Rationale for Insulin Therapy in Alzheimer’s Disease
Ribarič, S. (2016) · Molecules · doi:10.3390/molecules21060689 · Cited by 20
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Pulse pressure is associated with plasma amyloid-β transport dysfunction
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“In addition to the possible role of RAGE-Aβ interaction for the activation of nuclear factor-κB signaling pathways, which may promote apoptosis and neuroinflammation [41], the RAGE-mediated influx of peripheral Aβ into the brain may increase amyloid load.”
Background
Perforin Promotes Amyloid Beta Internalisation in Neurons
Lana, E., Khanbolouki, M., Degavre, C., Samuelsson, E., Åkesson, E., Winblad, B. G., Alici, E., Lithner, C. U., & Behbahani, H. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9685-9 · Cited by 18
“chronic disorders and neurodegeneration processes), its level increases [8].”
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Therapeutic Potential of Direct Clearance of the Amyloid-β in Alzheimer’s Disease
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“transgenic presenilin-1 (PS1)-APP mice yield an inverse correlation between cytokine production and Aβ clearance [15].”
BackgroundInfluential

Authors: Srikanth, V., Maczurek, A., Phan, T., Steele, M., Westcott, B., Juskiw, D., & Münch, G.
Affiliations: Monash University (AU)
Western Sydney University (AU)
James Cook University (AU)
ORCID: Srikanth, Velandai
Phan, Thanh
Steele, Megan
Münch, Gerald
Venue: Neurobiology of Aging
Publisher: Elsevier BV
Published: 2011-05
Volume: 32
Issue: 5
Pages: 763-777
ISSN: 0197-4580 (ISSN-L)
DOI: 10.1016/j.neurobiolaging.2009.04.016
OpenAlex: W2027183895
Cited by: 524
References: 132
Citations by year: 2026: 20 · 2025: 25 · 2024: 31 · 2023: 25 · 2022: 34 · 2021: 46 · 2020: 32 · 2019: 43 · 2018: 26 · 2017: 46 · 2016: 33 · 2015: 39 · 2014: 38 · 2013: 26 · 2012: 32
FWCI: 2.34
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Neurobiology of Aging (publishedVersion)
PubMed (publishedVersion)
ResearchOnline at James Cook University (James Cook University) (submittedVersion)
Funders: National Health and Medical Research Council (436797, 491109)
Alzheimer's Australia
Deutsche Forschungsgemeinschaft (Mu 1011/14-1, Mu1011/15-1)
Alzheimer Forschung Initiative
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: advanced glycation end products, RAGE, Alzheimer's disease, soluble RAGE, amyloid plaques, neurofibrillary tangles, oxidative stress, neuroinflammation, neurodegeneration, protein cross-linking, RAGE antagonists, AGE inhibitors, pathogenesis
MeSH terms: Receptor for Advanced Glycation End Products, Aging, Alzheimer Disease, Diabetes Mellitus, Type 2, Humans, Macrophages, Receptors, Immunologic, Neurofibrillary Tangles, Glycation End Products, Advanced, Microglia, Oxidative Stress, Disease Progression, Plaque, Amyloid

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Advanced glycation endproducts and their receptor RAGE in Alzheimer's disease

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