Cited by 103Alzheimer's disease research and treatmentsAdvanced Glycation End Products researchDementia and Cognitive Impairment Research

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RAGE mediates Aβ accumulation in a mouse model of Alzheimer’s disease via modulation of β- and γ-secretase activity

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Fang, Fang, Yu, Qing, Arancio, Ottavio, Chen, Doris, Gore, Smruti S, Yan, Shirley ShiDu, Yan, Shi Fang·2018·Human Molecular Genetics

DOI 10.1093/hmg/ddy017PMC PMC6075512

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Abstract

Receptor for Advanced Glycation End products (RAGE) has been implicated in amyloid β-peptide (Aβ)-induced perturbation relevant to the pathogenesis of Alzheimer's disease (AD). However, whether and how RAGE regulates Aβ metabolism remains largely unknown. Aβ formation arises from aberrant cleavage of amyloid pre-cursor protein (APP) by β- and γ-secretase. To investigate whether RAGE modulates β- and γ-secretase activity potentiating Aβ formation, we generated mAPP mice with genetic deletion of RAGE (mAPP/RO). These mice displayed reduced cerebral amyloid pathology, inhibited aberrant APP-Aβ metabolism by reducing β- and γ-secretases activity, and attenuated impairment of learning and memory compared with mAPP mice. Similarly, RAGE signal transduction deficient mAPP mice (mAPP/DN-RAGE) exhibited the reduction in Aβ40 and Aβ42 production and decreased β-and γ-secretase activity compared with mAPP mice. Furthermore, RAGE-deficient mAPP brain revealed suppression of activation of p38 MAP kinase and glycogen synthase kinase 3β (GSK3β). Finally, RAGE siRNA-mediated gene silencing or DN-RAGE-mediated signaling deficiency in the enriched human APP neuronal cells demonstrated suppression of activation of GSK3β, accompanied with reduction in Aβ levels and decrease in β- and γ-secretases activity. Our findings highlight that RAGE-dependent signaling pathway regulates β- and γ-secretase cleavage of APP to generate Aβ, at least in part through activation of GSK3β and p38 MAP kinase. RAGE is a potential therapeutic target to limit aberrant APP-Aβ metabolism in halting progression of AD.

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1 retracted

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Authors: Fang, F., Yu, Q., Arancio, O., Chen, D., Gore, S. S., Yan, S. S., & Yan, S. F.
Affiliations: University of Kansas (US)
Columbia University (US)
Corresponding author: Yan, Shirley ShiDu
Yan, Shi Fang
ORCID: Arancio, Ottavio
Chen, Doris
Gore, Smruti S
Yan, Shirley ShiDu
Yan, Shi Fang
Venue: Human Molecular Genetics
Publisher: Oxford University Press (OUP)
Published: 2018-01-10
Volume: 27
Issue: 6
Pages: 1002-1014
ISSN: 0964-6906 (ISSN-L)
1460-2083
DOI: 10.1093/hmg/ddy017
PMC: PMC6075512
OpenAlex: W2782715813
Cited by: 103
References: 72
Citations by year: 2026: 16 · 2025: 12 · 2024: 11 · 2023: 12 · 2022: 17 · 2021: 17 · 2020: 13 · 2019: 2 · 2018: 3
FWCI: 6.00
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Human Molecular Genetics (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Health (R37AG037319, R01AG044793, R01AG053041, R01NS089116)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: receptor for advanced glycation end products, Alzheimer's disease, amyloid-beta deposition, beta-secretase, gamma-secretase, amyloid precursor protein, GSK3β, p38 MAPK, APP processing, learning and memory impairment, therapeutic target
MeSH terms: Receptor for Advanced Glycation End Products, Glycogen Synthase Kinase 3 beta, Alzheimer Disease, Animals, Brain, Disease Models, Animal, Humans, Memory, Mice, Transgenic, Neurons, Signal Transduction, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, p38 Mitogen-Activated Protein Kinases, Mice, Amyloid Precursor Protein Secretases

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RAGE mediates Aβ accumulation in a mouse model of Alzheimer’s disease via modulation of β- and γ-secretase activity

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