The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Isolation and Characterization of Patient-derived, Toxic, High Mass Amyloid β-Protein (Aβ) Assembly from Alzheimer Disease Brains
Open accessAbstract
Amyloid beta-protein (Abeta) assemblies are thought to play primary roles in Alzheimer disease (AD). They are considered to acquire surface tertiary structures, not present in physiologic monomers, that are responsible for exerting toxicity, probably through abnormal interactions with their target(s). Therefore, Abeta assemblies having distinct surface tertiary structures should cause neurotoxicity through distinct mechanisms. Aiming to clarify the molecular basis of neuronal loss, which is a central phenotype in neurodegenerative diseases such as AD, we report here the selective immunoisolation of neurotoxic 10-15-nm spherical Abeta assemblies termed native amylospheroids (native ASPDs) from AD and dementia with Lewy bodies brains, using ASPD tertiary structure-dependent antibodies. In AD patients, the amount of native ASPDs was correlated with the pathologic severity of disease. Native ASPDs are anti-pan oligomer A11 antibody-negative, high mass (>100 kDa) assemblies that induce degeneration particularly of mature neurons, including those of human origin, in vitro. Importantly, their immunospecificity strongly suggests that native ASPDs have a distinct surface tertiary structure from other reported assemblies such as dimers, Abeta-derived diffusible ligands, and A11-positive assemblies. Only ASPD tertiary structure-dependent antibodies could block ASPD-induced neurodegeneration. ASPDs bind presynaptic target(s) on mature neurons and have a mode of toxicity different from those of other assemblies, which have been reported to exert their toxicity through binding postsynaptic targets and probably perturbing glutamatergic synaptic transmission. Thus, our findings indicate that native ASPDs with a distinct toxic surface induce neuronal loss through a different mechanism from other Abeta assemblies.
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Aβ Oligomers – a decade of discovery
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Cited by
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870
Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., & Ishii, Y. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2991 · Cited by 818
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Biochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer Disease
Masters, C. L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006262 · Cited by 542
Metadata
- Authors
- Noguchi, A., Matsumura, S., Dezawa, M., Tada, M., Yanazawa, M., Ito, A., Akioka, M., Kikuchi, S., Sato, M., Ideno, S., Noda, M., Fukunari, A., Muramatsu, S.-I., Itokazu, Y., Sato, K., Takahashi, H., Teplow, D. B., Nabeshima, Y.-I., Kakita, A., Imahori, K., & Hoshi, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-11
- Volume
- 284
- Issue
- 47
- Pages
- 32895-32905
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2132200081
- Cited by
- 173
- References
- 27
- FWCI
- 9.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Noguchi, A., Matsumura, S., Dezawa, M., Tada, M., Yanazawa, M., Ito, A., Akioka, M., Kikuchi, S., Sato, M., Ideno, S., Noda, M., Fukunari, A., Muramatsu, S.-I., Itokazu, Y., Sato, K., Takahashi, H., Teplow, D. B., Nabeshima, Y.-I., Kakita, A., . . . Hoshi, M. (2009). Isolation and Characterization of Patient-derived, Toxic, High Mass Amyloid β-Protein (Aβ) Assembly from Alzheimer Disease Brains. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m109.000208
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
