Epothilone D inhibits microglia-mediated spread of alpha-synuclein aggregates
Open accessAbstract
Multiple System Atrophy (MSA) is a progressive neurodegenerative disease characterized by chronic neuroinflammation and widespread α-synuclein (α-syn) cytoplasmic inclusions. Neuroinflammation associated with microglial cells is typically located in brain regions with α-syn deposits. The potential link between microglial cell migration and the transport of pathological α-syn protein in MSA was investigated. Qualitative analysis via immunofluorescence of MSA cases (n = 4) revealed microglial cells bearing α-syn inclusions distal from oligodendrocytes bearing α-syn cytoplasmic inclusions, as well as close interactions between microglia and oligodendrocytes bearing α-syn, suggestive of a potential transfer mechanism between microglia and α-syn bearing cells in MSA and the possibility of microglia acting as a mobile vehicle to spread α-syn between anatomically connected brain regions. Further In vitro experiments using microglial-like differentiated THP-1 cells were conducted to investigate if microglial cells could act as potential transporters of α-syn. Monomeric or aggregated α-syn was immobilized at the centre of glass coverslips and treated with either cell free medium, undifferentiated THP-1 cells or microglial-like phorbol-12-myristate-13-acetate differentiated THP-1 cells (48 h; n = 3). A significant difference in residual immobilized α-syn density was observed between cell free controls and differentiated (p = 0.016) as well as undifferentiated and differentiated THP-1 cells (p = 0.032) when analysed by quantitative immunofluorescence. Furthermore, a significantly greater proportion of differentiated cells were observed bearing α-syn aggregates distal from the immobilized protein than their non-differentiated counterparts (p = 0.025). Similar results were observed with Highly Aggressive Proliferating Immortalised (HAPI) microglial cells, with cells exposed to aggregated α-syn yielding lower residual immobilized α-syn (p = 0.004) and a higher proportion of α-syn positive distal cells (p = 0.001) than cells exposed to monomeric α-syn. Co-treatment of THP-1 groups with the tubulin depolymerisation inhibitor, Epothilone D (EpoD; 10 nM), was conducted to investigate if inhibition of microtubule activity had an effect on cell migration and residual immobilized α-syn density. There was a significant increase in both residual immobilized α-syn between EpoD treated and non-treated differentiated cells exposed to monomeric (p = 0.037) and aggregated (p = 0.018) α-syn, but not with undifferentiated cells. Differentiated THP-1 cells exposed to immobilized aggregated α-syn showed a significant difference in the proportion of distal aggregate bearing cells between EpoD treated and untreated (p = 0.027). The results suggest microglia could play a role in α-syn transport in MSA, a role which could potentially be inhibited therapeutically by EpoD.
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Some α-syn-containing microglia were distal from GCI-containing oligodendrocytes in MSA patient brain sections.
“A recent study observed the brain tissue sections of MSA patients by immunofluorescence and found that some α-syn-containing microglia were distal from GCI-containing oligodendrocytes,300”
From Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets (2023) · cites this paper as [300]
The ability of microglia to transport α-syn distally was impaired when microtubule activity was inhibited with Epothilone D.
“The ability of microglia to transport α-syn distally was impaired when microtubule activity was inhibited with Epothilone D (EpoD)300”
From Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets (2023) · cites this paper as [300]
In an in vitro culture system, the proportion of α-syn-containing differentiated THP-1 cells was significantly increased in distant regions of α-syn compared with undifferentiated cells.
“The proportion of α-syn-containing differentiated THP-1 cells was significantly increased in distant regions of α-syn compared with undifferentiated cells.300”
From Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets (2023) · cites this paper as [300]
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Alpha-Synuclein Aggregates Associated with Mitochondria in Tunnelling Nanotubes
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[Protective effect of Epothilone D against traumatic optic nerve injury in rats].
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Emerging Therapeutic Approaches for Neurodegenerative Diseases
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- Authors
- Valdinocci, D., Grant, G. D., Dickson, T. C., & Pountney, D. L.
- Affiliations
- Griffith University (AU)
- University of Tasmania (AU)
- Corresponding author
- Pountney, Dean L.
- Venue
- Molecular and Cellular Neuroscience
- Publisher
- Elsevier BV
- Published
- 2018-06
- Volume
- 89
- Pages
- 80-94
- ISSN
- 1044-7431 (ISSN-L)
- OpenAlex
- W2801538862
- Cited by
- 20
- References
- 79
- Citations by year
- 2024: 1 · 2023: 2 · 2022: 4 · 2021: 2 · 2020: 8 · 2019: 2 · 2018: 1
- FWCI
- 2.20
- Type
- journal article
- Language
- en
- Open access
- green
- figshare.com
- Licence
- Locations
- Molecular and Cellular Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- eCite Digital Repository (University of Tasmania) (submittedVersion)
- UTAS Research Repository (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Griffith Research Online (submittedVersion, cc-by-nc-nd)
- Funders
- Griffith University, Menzies Health Institute Queensland
- Australian Research Council
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- multiple system atrophy, alpha-synuclein aggregates, microglia, neuroinflammation, epothilone D, microglial migration, oligodendrocytes, THP-1 cells, neurodegeneration, synucleinopathies
- MeSH terms
- Aged, Animals, Brain, Cell Line, Cell Movement, Humans, Microglia, Multiple System Atrophy, Epothilones, Cell Line, Tumor, Tubulin Modulators, Rats, alpha-Synuclein
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