Amyloid plaque structure and cell surface interactions of β-amyloid fibrils revealed by electron tomography
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The deposition of amyloid fibrils as plaques is a key feature of several neurodegenerative diseases including in particular Alzheimer’s. This disease is characterized, if not provoked, by amyloid aggregates formed from Aβ peptide that deposit inside the brain or are toxic to neuronal cells. We here used scanning transmission electron microscopy (STEM) to determine the fibril network structure and interactions of Aβ fibrils within a cell culture model of Alzheimer’s disease. STEM images taken from the formed Aβ amyloid deposits revealed three main types of fibril network structures, termed amorphous meshwork, fibril bundle and amyloid star. All three were infiltrated by different types of lipid inclusions from small-sized exosome-like structures (50–100 nm diameter) to large-sized extracellular vesicles (up to 300 nm). The fibrils also presented strong interactions with the surrounding cells such that fibril bundles extended into tubular invaginations of the plasma membrane. Amyloid formation in the cell model was previously found to have an intracellular origin and we show here that it functionally destroys the integrity of the intracellular membranes as it leads to lysosomal leakage. These data provide a mechanistic link to explain why intracellular fibril formation is toxic to the cell.
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Exogenous Aβ fibrils lead to cell death and disruption of membrane integrity in a cell culture model.
“More recent studies demonstrate that exogenous Aβ fibrils lead to cell death and disruption of membrane integrity in a cell culture model [41].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [41]
The Results section (“Formation of Aβ amyloid plaques in cell culture”; page not provided) reports cell toxicity and membrane damage after exposure to Aβ peptide, with cell death following fibril formation. But the paper describes adding extracellular peptide that cells internalize and convert into amyloid; it does not establish that exogenous, preformed Aβ fibrils caused those effects. (LLM, conf=0.88)
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- Authors
- Han, S., Kollmer, M., Markx, D., Claus, S., Walther, P., & Fändrich, M.
- Affiliations
- Universität Ulm (DE)
- Corresponding author
- Walther, Paul
- Fändrich, Marcus
- Venue
- Scientific Reports
- Published
- 2017-02-27
- Volume
- 7
- Issue
- 1
- Pages
- 43577-43577
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC5327471
- OpenAlex
- W2592429228
- Cited by
- 95
- References
- 44
- Citations by year
- 2026: 3 · 2025: 10 · 2024: 10 · 2023: 17 · 2022: 8 · 2021: 4 · 2020: 14 · 2019: 15 · 2018: 13 · 2017: 1
- FWCI
- 8.70
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Carl-Zeiss-Stiftung
- Deutsche Forschungsgemeinschaft (FA 456/12-1)
- Universität Ulm
- 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
- amyloid plaques, amyloid-beta fibrils, Alzheimer's disease, extracellular vesicles, exosomes, lipid inclusions, plasma membrane invaginations, neurodegeneration, cell-surface interactions
- MeSH terms
- Alzheimer Disease, Amyloid, Cell Membrane, Cell Survival, Cells, Cultured, Humans, Lipids, Amyloid beta-Peptides, Electron Microscope Tomography, Plaque, Amyloid, Protein Aggregation, Pathological, Protein Aggregates
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