FcγRIIb mediates amyloid-β neurotoxicity and memory impairment in Alzheimer’s disease
Open accessAbstract
Amyloid-β (Aβ) induces neuronal loss and cognitive deficits and is believed to be a prominent cause of Alzheimer's disease (AD); however, the cellular pathology of the disease is not fully understood. Here, we report that IgG Fcγ receptor II-b (FcγRIIb) mediates Aβ neurotoxicity and neurodegeneration. We found that FcγRIIb is significantly upregulated in the hippocampus of AD brains and neuronal cells exposed to synthetic Aβ. Neuronal FcγRIIb activated ER stress and caspase-12, and Fcgr2b KO primary neurons were resistant to synthetic Aβ-induced cell death in vitro. Fcgr2b deficiency ameliorated Aβ-induced inhibition of long-term potentiation and inhibited the reduction of synaptic density by naturally secreted Aβ. Moreover, genetic depletion of Fcgr2b rescued memory impairments in an AD mouse model. To determine the mechanism of action of FcγRIIb in Aβ neurotoxicity, we demonstrated that soluble Aβ oligomers interact with FcγRIIb in vitro and in AD brains, and that inhibition of their interaction blocks synthetic Aβ neurotoxicity. We conclude that FcγRIIb has an aberrant, but essential, role in Aβ-mediated neuronal dysfunction.
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Neuronal FcγRIIb binds Aβ42 with high affinity and mediates neurotoxicity and memory impairment triggered by Aβ.
“Neuronal FcγRIIb can bind to Aβ42 with a high affinity, and mediate neurotoxicity and memory impairment triggered by Aβ [240, 376–380].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [377]
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- Authors
- Kam, T.-I., Song, S., Gwon, Y., Park, H., Yan, J.-J., Im, I., Choi, J.-W., Choi, T.-Y., Kim, J., Song, D.-K., Takai, T., Kim, Y.-C., Kim, K.-S., Choi, S.-Y., Choi, S., Klein, W. L., Yuan, J., & Jung, Y.-K.
- Affiliations
- Seoul National University (KR)
- Hallym University (KR)
- Gwangju Institute of Science and Technology (KR)
- Korean Association Of Science and Technology Studies (KR)
- Tohoku University (JP)
- Northwestern University (US)
- Harvard University (US)
- Corresponding author
- Jung, Yong-Keun
- ORCID
- Venue
- Journal of Clinical Investigation
- Published
- 2013-06-10
- Volume
- 123
- Issue
- 7
- Pages
- 2791-2802
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC3696552
- OpenAlex
- W2166211238
- Cited by
- 128
- References
- 56
- Citations by year
- 2026: 9 · 2025: 8 · 2024: 5 · 2023: 10 · 2022: 7 · 2021: 14 · 2020: 9 · 2019: 7 · 2018: 12 · 2017: 12 · 2016: 13 · 2015: 10 · 2014: 9 · 2013: 3
- FWCI
- 8.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Seoul National University Open Repository (Seoul National University) (submittedVersion)
- Funders
- Ministry of Education, Science and Technology
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- FcγRIIB, amyloid-beta, Alzheimer's disease, neurotoxicity, memory impairment, endoplasmic reticulum stress, caspase-12, neuronal cell death, long-term potentiation, synaptic density, soluble amyloid-beta oligomers, hippocampus, Fc gamma receptor
- MeSH terms
- Alzheimer Disease, Amyloid, Animals, Female, Cricetinae, Hippocampus, Humans, Male, Memory Disorders, Mice, Inbred C57BL, Neurons, Peptide Fragments, Synapses, Signal Transduction, Transcriptional Activation, Amyloid beta-Peptides, CHO Cells, Receptors, IgG, Mice, Knockout, Excitatory Postsynaptic Potentials, Mice, Primary Cell Culture
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