Reversing EphB2 depletion rescues cognitive functions in Alzheimer model
Open accessAbstract
Amyloid-β oligomers may cause cognitive deficits in Alzheimer's disease by impairing neuronal NMDA-type glutamate receptors, whose function is regulated by the receptor tyrosine kinase EphB2. Here we show that amyloid-β oligomers bind to the fibronectin repeats domain of EphB2 and trigger EphB2 degradation in the proteasome. To determine the pathogenic importance of EphB2 depletions in Alzheimer's disease and related models, we used lentiviral constructs to reduce or increase neuronal expression of EphB2 in memory centres of the mouse brain. In nontransgenic mice, knockdown of EphB2 mediated by short hairpin RNA reduced NMDA receptor currents and impaired long-term potentiation in the dentate gyrus, which are important for memory formation. Increasing EphB2 expression in the dentate gyrus of human amyloid precursor protein transgenic mice reversed deficits in NMDA receptor-dependent long-term potentiation and memory impairments. Thus, depletion of EphB2 is critical in amyloid-β-induced neuronal dysfunction. Increasing EphB2 levels or function could be beneficial in Alzheimer's disease.
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oAβ binds to the fibronectin repeat region of EphB2, triggering EphB2 endocytosis and degradation.
“oAβ binds to the fibronectin repeat region of EphB2, thereby triggering EphB2 endocytosis and degradation.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [76]
Overexpression of EphB2 in the dentate gyrus region in an AD mouse model reversed impairments in LTP and cognitive memory.
“Remarkably, overexpression of EphB2 in the dentate gyrus region in an AD mouse model reversed impairments in LTP and cognitive memory [76].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [76]
EphB2 overexpression can restore reductions in AMPAR and NMDAR levels induced by oAβ.
“In addition, EphB2 overexpression can restore reductions in AMPAR and NMDAR levels induced by oAβ.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [76]
Interventions that improve cognitive performance, behaviors, or neuropathology in rodents have frequently not led to accelerated therapeutic development, notably in Alzheimer's disease.
“Interventions that improve cognitive performance, behaviors, or neuropathology in rodents have frequently not led to accelerated therapeutic development, most notably in Alzheimer’s disease where reports abound of cured mouse models despite repeated clinical failures (Cisse et al., 2011; Gandy and DeKosky, 2013; Malenka and Malinow, 2011; Vaillend et al., 2002).”
From Modeling Autism by SHANK Gene Mutations in Mice (2013) · cites this paper as Cisse et al., 2011
Aβ oligomers bind to and trigger subsequent proteasomal degradation of the receptor tyrosine kinase EphB2.
“Aβ oligomers bind to and trigger subsequent proteasomal degradation of the receptor tyrosine kinase EphB2.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Cisse et al., 2011
These receptor pathologies discovered in cell culture have been confirmed in transgenic mouse models and human Alzheimer's disease brain.
“These receptor pathologies discovered in cell culture have been confirmed in tg-mouse models and human AD brain (Cisse et al., 2011; Moloney et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Cisse et al., 2011
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- Authors
- Cissé, M., Halabisky, B., Harris, J., Devidze, N., Dubal, D. B., Sun, B., Orr, A., Lotz, G., Kim, D. H., Hamto, P., Ho, K., Yu, G.-Q., & Mucke, L.
- Affiliations
- Gladstone Institutes (US)
- Corresponding author
- Mucke, Lennart
- ORCID
- Venue
- Nature
- Published
- 2010-11-28
- Volume
- 469
- Issue
- 7328
- Pages
- 47-52
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3030448
- OpenAlex
- W2057815562
- Cited by
- 433
- References
- 62
- Citations by year
- 2026: 17 · 2025: 15 · 2024: 21 · 2023: 20 · 2022: 13 · 2021: 22 · 2020: 23 · 2019: 17 · 2018: 27 · 2017: 34 · 2016: 34 · 2015: 29 · 2014: 40 · 2013: 44 · 2012: 41
- FWCI
- 26.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Gladstone Institutes
- National Institutes of Health (1c06rr018928-01)
- National Institute on Aging (AG011385, R37AG011385, AG022074, P01AG022074, R01AG011385, F32AG039220)
- National Institute of Neurological Disorders and Stroke (R01NS041787, NS041787)
- National Center for Research Resources (RR 18928-01, C06-RR-018928)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- EphB2, Alzheimer's disease, amyloid-beta oligomers, NMDA receptor, long-term potentiation, memory impairment, proteasomal degradation, dentate gyrus, amyloid precursor protein transgenic mice, receptor tyrosine kinase, therapeutic target
- MeSH terms
- Alzheimer Disease, Animals, Cell Line, Cells, Cultured, Cognition, Disease Models, Animal, Humans, Memory, Mice, Transgenic, Neuronal Plasticity, Protein Binding, Synapses, Receptors, N-Methyl-D-Aspartate, Amyloid beta-Peptides, Protein Structure, Tertiary, Long-Term Potentiation, Dentate Gyrus, Receptor, EphB2, Proteasome Endopeptidase Complex, Mice, Rats
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