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RAGE-mediated signaling contributes to intraneuronal transport of amyloid-β and neuronal dysfunction
Open accessAbstract
Intracellular amyloid-β peptide (Aβ) has been implicated in neuronal death associated with Alzheimer's disease. Although Aβ is predominantly secreted into the extracellular space, mechanisms of Aβ transport at the level of the neuronal cell membrane remain to be fully elucidated. We demonstrate that receptor for advanced glycation end products (RAGE) contributes to transport of Aβ from the cell surface to the intracellular space. Mouse cortical neurons exposed to extracellular human Aβ subsequently showed detectable peptide intracellularly in the cytosol and mitochondria by confocal microscope and immunogold electron microscopy. Pretreatment of cultured neurons from wild-type mice with neutralizing antibody to RAGE, and neurons from RAGE knockout mice displayed decreased uptake of Aβ and protection from Aβ-mediated mitochondrial dysfunction. Aβ activated p38 MAPK, but not SAPK/JNK, and then stimulated intracellular uptake of Aβ-RAGE complex. Similar intraneuronal co-localization of Aβ and RAGE was observed in the hippocampus of transgenic mice overexpressing mutant amyloid precursor protein. These findings indicate that RAGE contributes to mechanisms involved in the translocation of Aβ from the extracellular to the intracellular space, thereby enhancing Aβ cytotoxicity.
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“As shown by us and others, ApoE facilitates but it is not required for Ab uptake, because neurons grown in the absence of ApoE can internalize Ab. 28”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [28]
In the citing paper
“In contrast, evidence suggests that internalization of Ab not associated with ApoE occurs through nonendocytotic mechanisms, which are based on the translocation of the cell surface bound Ab directly to the cytosol and results in accumulation of Ab primarily outside the endosomal/lysosomal compartment.28,45,46”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [28]
In the citing paper
“RAGE, a member of the immunoglobulin superfamily of pattern recognition receptors, is not known to be related to oxytocin or oxytocin signalling22–33.”
From Vascular RAGE transports oxytocin into the brain to elicit its maternal bonding behaviour in mice (2019) · cites this paper as [25]
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Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · cited 1×
“Consistent with these in vitro results, recent studies in brains of AD patients (48) and another mouse AD model (49) displayed striking accumulation of A in hippocampal pyramidal cells.”
ResultRAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012
Self-citationIntracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · cited 1×
“Recent studies demonstrate that several plasma membrane receptors, such as N-methyl-D-aspartate receptors (14), 7 nicotinic acetylcholine receptors (15), and low-density lipoprotein receptor-related proteins (LRP) (16), have the capacity to bind to A and, potentially, promote intracellular accumulation of A .”
BackgroundNeeper, M. P., Schmidt, A. M., Brett, J., Yan, S. D., Wang, F., Pan, Y., Elliston, K. O., Stern, D., & SHAW, A. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42138-2 · Cited by 1,545
Self-citationRAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Self-citationABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303
Self-citationUnderstanding RAGE, the receptor for advanced glycation end products
Bierhaus, A., Humpert, P. M., Morcos, M., Wendt, T., Chavakis, T., Arnold, B., Stern, D. M., & Nawroth, P. P. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0688-7 · Cited by 1,297
Self-citationThe multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
Schmidt, A. M., Yan, S. D., Yan, S. F., & Stern, D. M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci14002 · Cited by 1,256
Self-citationManczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104
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Shi, C., Duan, Y., Li, Z., Zhou, Y., Cao, Y., Sun, Y., Chui, D., & Guo, X. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.01.012 · Cited by 21
Jia, K., Tian, J., Wang, T., Guo, L., Xuan, Z., Swerdlow, R. H., & Du, H. (2023) · JCI Insight · doi:10.1172/jci.insight.174290 · Cited by 20
Self-citationLin, T.-S., Tsai, H.-J., Lee, C.-H., Song, Y.-Q., Huang, R., Hsieh-Li, H.-M., Liang, M., & Lin, Y. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160898 · Cited by 20
Vidal, C., & Li, Z. (2021) · Cells · doi:10.3390/cells10030546 · Cited by 20
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Vangavaragu, J. R., Valasani, K. R., Du, F., Williams, T. D., & Yan, S. S. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140252 · Cited by 19
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Takeuchi, S., Kawanai, T., Yamauchi, R., Chen, L., Miyaoka, T., Yamada, M., Asano, S., Hayata‐Takano, A., Nakazawa, T., Yano, K., et al. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00521 · Cited by 19
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Shityakov, S., Hayashi, K., Störk, S., Scheper, V., Lenarz, T., & Förster, C. Y. (2021) · Biomolecules · doi:10.3390/biom11060900 · Cited by 18
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Choi, K., Lim, K. S., Shin, J., Kim, S. H., Suh, Y., Hong, H., Kim, H. Y., Ha, H.-J., Kim, Y.-H., Lee, J., et al. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.05.022 · Cited by 16
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Lee, H., Jeong, H.-R., Park, J.-H., & Hoe, H. (2021) · Biology · doi:10.3390/biology10090938 · Cited by 15
Du, H., & Yan, S. S. (2010) · Pharmaceuticals · doi:10.3390/ph3061936 · Cited by 15
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Piccinni, A., Origlia, N., Veltri, A., Vizzaccaro, C., Marazziti, D., Vanelli, F., Moroni, I., Domenici, L., & Dell’Osso, L. (2012) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.3879 · Cited by 14
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Patil, G. V., Joshi, R. S., Kazi, R. S., Kulsange, S. E., & Kulkarni, M. J. (2020) · Medical Hypotheses · doi:10.1016/j.mehy.2020.109799 · Cited by 9
Juranek, J. K., Kordas, B., Podlasz, P., Bossowska, A., & Banach, M. D. (2025) · Pathophysiology · doi:10.3390/pathophysiology32030043 · Cited by 8
Kim, C., Lee, J., Ko, Y. U., & Oh, Y. J. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.10.053 · Cited by 8
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Pang, Q., Lee, S., Cho, E. J., & Kim, J.-H. (2023) · Life · doi:10.3390/life13071453 · Cited by 3
Takei, S., Ochi, M., Shiraoka, A., Matsumoto, S., Fujishita, S., Okada, Y., Miura, S., Ochi, H., Igase, M., & Ohyagi, Y. (2024) · Archives of Gerontology and Geriatrics Plus · doi:10.1016/j.aggp.2024.100071 · Cited by 3
Hu, W. T., Butts, B., Misiura, M. B., Verble, D. D., Swatson, E., Park, C., Watson, J., Hammerschlag, B. L., Nayyar, A., Korrapati, N., et al. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03657-3 · Cited by 3
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Knepp, B., Ander, B. P., Jickling, G. C., Hull, H., Yee, A., Ng, K., Rodríguez, F., Carmona-Mora, P., Amini, H., Zhan, X., et al. (2022) · Brain Hemorrhages · doi:10.1016/j.hest.2022.04.003 · Cited by 2
Fin, N. A. S. H., Georgevsky, D., Sukkar, M. B., & Golzan, M. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1156084 · Cited by 2
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Fulopova, B., Bennett, W. R., Summers, B. S., Stuart, K. E., King, A. E., Vickers, J. C., & Canty, A. J. (2022) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2022.03.007 · Cited by 1
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Wijesooriya, C. S., Rahman, S., & Smith, E. A. (2025) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2025.184485 · Cited by 1
Bhargavan, B., Annadurai, N., & Kanmogne, G. D. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02197-4 · Cited by 1
Zhang, N., Chen, W. H., & Wang, M. (2026) · Animal Models and Experimental Medicine · doi:10.1002/ame2.70262 · Cited by 1
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Colombo, J., Arora, R. R., DePace, N. L., & Vinik, A. I. (2014) · Springer eBooks · doi:10.1007/978-3-319-07371-2_14
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Hans, S., Stanton, J. E., Sauer, A. K., Shiels, K., Saha, S. K., Lordan, R., Tsoupras, A., Zabetakis, I., & Grabrucker, A. M. (2024) · Figshare · doi:10.6084/m9.figshare.25658630
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Metadata
- Authors
- Takuma, K., Fang, F., Zhang, W., Yan, S., Fukuzaki, E., Du, H., Sosunov, A., McKhann, G., Funatsu, Y., Nakamichi, N., Nagai, T., Mizoguchi, H., Ibi, D., Hori, O., Ogawa, S., Stern, D. M., Yamada, K., & Yan, S. S.
- Affiliations
- Kanazawa University (JP)
- Columbia University Irving Medical Center (US)
- Beijing Normal University (CN)
- University of Cincinnati (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2009-11-24
- Volume
- 106
- Issue
- 47
- Pages
- 20021-20026
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2785285
- OpenAlex
- W2165298830
- Cited by
- 290
- References
- 51
- Citations by year
- 2026: 8 · 2025: 15 · 2024: 14 · 2023: 13 · 2022: 15 · 2021: 14 · 2020: 10 · 2019: 13 · 2018: 12 · 2017: 20 · 2016: 18 · 2015: 28 · 2014: 21 · 2013: 18 · 2012: 28
- FWCI
- 15.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Lanzhou University Institutional Repository (submittedVersion, cc-by-nc-nd)
- Funders
- National Institute on Aging (P01AG017490, P01 AG 17490)
- 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
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- receptor for advanced glycation end products, amyloid-beta, Alzheimer's disease, mitochondrial dysfunction, p38 MAPK, RAGE knockout mice, amyloid precursor protein transgenic mice, neuronal cell death, hippocampus
- MeSH terms
- Animals, Biological Transport, Brain, Cells, Cultured, Enzyme Activation, Humans, Mice, Inbred C57BL, Mice, Transgenic, Mitochondria, Neurons, Signal Transduction, Amyloid beta-Peptides, Mice, Knockout, Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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