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Amyloid-β Activates Microglia and Regulates Protein Expression in a Manner Similar to Prions
Jian Tu1, Baian Chen, Lifeng Yang
1State Key Laboratories for Agrobiotechnology, National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, 100193, Beijing, China, tujian1980@126.com.
Abstract:
Prions are the only convincingly demonstrated proteinaceous infectious particle, yet recent studies find that amyloid-β peptide (Aβ) aggregates are capable of self-propagation, which induces amyloidosis pathology in Alzheimer's disease (AD) model mice that is similar to the self-propagation phenomenon of prions in neurons. Gliosis is a common hallmark of AD and prion diseases, in which activated microglia accumulate around abnormal protein deposits. Analyses of the characteristics of activated microglia induced by Aβ in comparison with those induced by prions will provide new insight into the pathogenesis of AD. Therefore, we compared the characteristics of BV-2 cells (model microglia) activated by Aβ fibrillar peptides (Aβ1-42) and prions (PrP106-126). Aβ1-42 and PrP106-126, as well as the supernatants of the media collected from BV-2 cells cocultured with Aβ1-42 and PrP106-126, were potent activators of BV-2 microglial activity, but the chemotaxis index (CI) induced by Aβ1-42 was significantly higher than that induced by PrP106-126 at each concentration. Aβ1-42 and PrP106-126 increased the proliferation index (PI) and upregulated monocyte chemoattractant protein-1 (MCP-1) and transforming growth factor beta 1 (TGF-β1) expression after 12 h of exposure. Our results show that Aβ activates microglia and regulates microglial protein expression in a manner similar to prions and, thus, provide new insight into the pathogenesis of AD.
Insights
Amyloid-beta (Aβ) aggregates activate microglia similarly to prions, offering new insights into Alzheimer's disease (AD) pathogenesis. Aβ showed higher microglial activation and chemotaxis compared to prions.
Area of Science:
- Neuroscience
- Immunology
- Protein Misfolding Diseases
Background:
- Prions are known proteinaceous infectious particles.
- Amyloid-beta (Aβ) aggregates exhibit self-propagation, inducing pathology similar to prion diseases in Alzheimer's disease (AD) models.
- Gliosis, characterized by activated microglia, is a hallmark of both AD and prion diseases.
Purpose of the Study:
- To compare the characteristics of microglia activated by Aβ and prions.
- To gain new insights into the pathogenesis of Alzheimer's disease by analyzing microglial responses.
Main Methods:
- Utilized BV-2 cells (a model microglia cell line).
- Exposed BV-2 cells to amyloid-beta 1-42 (Aβ1-42) fibrils and prion peptide (PrP106-126).
- Assessed microglial activation, proliferation index (PI), chemotaxis index (CI), and expression of monocyte chemoattractant protein-1 (MCP-1) and transforming growth factor beta 1 (TGF-β1).
Main Results:
- Both Aβ1-42 and PrP106-126 activated BV-2 microglial activity.
- Aβ1-42 induced a significantly higher chemotaxis index (CI) than PrP106-126 at all tested concentrations.
- Both Aβ1-42 and PrP106-126 increased the proliferation index (PI) and upregulated MCP-1 and TGF-β1 expression after 12 hours.
Conclusions:
- Amyloid-beta activates microglia and regulates their protein expression in a manner comparable to prions.
- These findings provide novel insights into the pathogenesis of Alzheimer's disease, highlighting shared mechanisms with prion diseases.
- The study underscores the importance of microglial activation in AD pathology.
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