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Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies
Open accessAbstract
Parkinson's disease (PD) is one of the most common neurodegenerative diseases. It is characterized by the loss of dopaminergic neurons in the substantia nigra pars compacta of the brain. Another feature is represented by the formation in these cells of inclusions called Lewy bodies (LB), principally constituted by fibrillar α-synuclein (αSyn). This protein is considered a key element in the aetiology of a group of neurodegenerative disorders termed synucleinopathies, which include PD, but the cellular and molecular mechanisms involved are not completely clear. It is established that the inflammatory process plays a crucial role in the pathogenesis and/or progression of PD; moreover, it is known that aggregated αSyn, released by neurons, activates microglia cells to produce pro-inflammatory mediators, such as IL-1β. IL-1β is one of the strongest pro-inflammatory cytokines; it is produced as an inactive mediator, and its maturation and activation requires inflammasome activation. In particular, the NLRP3 inflammasome is activated by a wide variety of stimuli, among which are crystallized and particulate material. In this work, we investigated the possibility that IL-1β production, induced by fibrillar αSyn, is involved the inflammasome activation. We demonstrated the competence of monomeric and fibrillar αSyn to induce synthesis of IL-1β, through TLR2 interaction; we found that the secretion of the mature cytokine was a peculiarity of the fibrillated protein. Moreover, we observed that the secretion of IL-1β involves NLRP3 inflammasome activation. The latter relies on the phagocytosis of fibrillar αSyn, followed by increased ROS production and cathepsin B release into the cytosol. Taken together, our data support the notion that fibrillar αSyn, likely released by neuronal degeneration, acts as an endogenous trigger inducing a strong inflammatory response in PD.
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“In an in vitro experiment, both monomeric and fibrillary α-synuclein can stimulate TLR2 and induce the expression of pro-IL-1β, but only fibrillary α-synuclein can activate the NLRP3 inflammasome, resulting in the secretion of active IL-1β.358”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [358]
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“Targeting caspase-1, a downstream molecule of NLRP3, is another promising method, which was found to decrease the secretion of IL-1β and attenuate the susceptibility of dopaminergic neurons.358”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [358]
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“The fibrillar, but not monomeric, form of α-synuclein induced NLRP3- and caspase-1–mediated IL-1β secretion in human monocytes and BV2 microglial cell line (238), or via TLR-2 signaling pathway in rodents microglial cells (250).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [238]
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Metadata
- Authors
- Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., & de Bernard, M.
- Affiliations
- University of Padua (IT)
- Veneto Institute of Molecular Medicine (IT)
- Institute of Nanostructured Materials (IT)
- Corresponding author
- Bubacco, Luigi
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-01-31
- Volume
- 8
- Issue
- 1
- Pages
- e55375
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3561263
- OpenAlex
- W2015283405
- Cited by
- 585
- References
- 67
- Citations by year
- 2026: 23 · 2025: 38 · 2024: 56 · 2023: 59 · 2022: 68 · 2021: 65 · 2020: 58 · 2019: 53 · 2018: 48 · 2017: 31 · 2016: 27 · 2015: 30 · 2014: 23 · 2013: 5
- FWCI
- 12.83
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Fondazione Cariplo (2011-0485)
- Università degli Studi di Padova
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- alpha-synuclein aggregation, NLRP3 inflammasome, IL-1β, Parkinson's disease, synucleinopathies, TLR2, microglial activation, phagocytosis, reactive oxygen species, cathepsin B, Lewy bodies, neuroinflammation, neurodegeneration
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Analysis of Variance, Carrier Proteins, Humans, Inflammation, Neurons, Parkinson Disease, Phagocytosis, Spectrometry, Fluorescence, Spectrophotometry, Ultraviolet, Thiazoles, Blotting, Western, Lewy Bodies, DNA Primers, Microscopy, Confocal, Microscopy, Atomic Force, Microscopy, Electron, Transmission, Toll-Like Receptor 2, alpha-Synuclein, Benzothiazoles, Interleukin-1beta, Chromatography, Reverse-Phase, Inflammasomes, Real-Time Polymerase Chain Reaction
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