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NLRP3 inflammasome activation drives tau pathology
Open accessAbstract
Alzheimer’s disease is characterized by the accumulation of amyloid-beta in plaques, aggregation of hyperphosphorylated tau in neurofibrillary tangles and neuroinflammation, together resulting in neurodegeneration and cognitive decline1. The NLRP3 inflammasome assembles inside of microglia on activation, leading to increased cleavage and activity of caspase-1 and downstream interleukin-1β release2. Although the NLRP3 inflammasome has been shown to be essential for the development and progression of amyloid-beta pathology in mice3, the precise effect on tau pathology remains unknown. Here we show that loss of NLRP3 inflammasome function reduced tau hyperphosphorylation and aggregation by regulating tau kinases and phosphatases. Tau activated the NLRP3 inflammasome and intracerebral injection of fibrillar amyloid-beta-containing brain homogenates induced tau pathology in an NLRP3-dependent manner. These data identify an important role of microglia and NLRP3 inflammasome activation in the pathogenesis of tauopathies and support the amyloid-cascade hypothesis in Alzheimer’s disease, demonstrating that neurofibrillary tangles develop downstream of amyloid-beta-induced microglial activation. The authors show that NLRP3 inflammasome is activated in microglia of patients with fronto-temporal dementia and in a mouse model of tau pathology, and that the loss of NLRP3 inflammasome function decreases tau pathology and improves cognition in mice.
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In the citing paper
“The NLRP3-ASC inflammasome mechanisms contributing to increased beta-amyloids and tau are thought to be a combination of kinases and phosphatases involved in tau phosphorylation [96] through the production of IL-1 beta.”
From The Role of Cortisol in Chronic Stress, Neurodegenerative Diseases, and Psychological Disorders (2023) · cites this paper as [96]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The activation of hippocampal NLRP3 inflammasome-mediated pyroptosis is associated with neuronal damage, cognitive decline, and neuronal death (Hanslik & Ulland, 2020; Heneka et al., 2013; Ising et al., 2019; Venegas et al., 2017).”
From Picroside II Alleviates the Progression of Alzheimer’s Disease via the NLRP3/Caspase-1/GSDMD Pathway (2025) · cites this paper as Ising et al., 2019
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“On the other hand, treatment of mouse primary hippocampal neurons with conditioned media from wild-type, but not Nlrp3−/− and Asc−/−, microglia primed with LPS resulted in elevated total and phosphorylated tau levels, suggesting that NLRP3 inflammasome activation in microglia can induce tau pathology in neurons.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Additionally, several cytokines, including IL-1β and IL-6, can directly induce tau phosphorylation in vitro, thus potentially contributing to the development of tau pathology.54”
From Amelioration of Tau and ApoE4-linked glial lipid accumulation and neurodegeneration with an LXR agonist (2024) · cites this paper as [56]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Research by Ising et al. suggests that tau proteins can activate the NLRP3 inflammasome, which then promotes excessive tau phosphorylation and aggregation by affecting specific tau kinases and phosphatases.252”
From Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies. (2024) · cites this paper as [252]
The cited source says what the claim attributes to it.
In the citing paper
“In turn, the NLRP3 inflammasome is essential for the development and progression of Aβ pathology in mice29 and may drive tau pathology through Aβ-induced microglial activation30.”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [30]
The cited source says what the claim attributes to it.
In the citing paper
“On the other hand, microglia could also drive tau spreading and toxicity by promoting neuroinflammation, such as activating NACHT-, LRR- and pyrin (PYD)-domain-containing protein 3 (NLRP3) inflammasome155 or inducing NF-kB signaling.”
From Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets (2023) · cites this paper as [155]
The cited source says what the claim attributes to it.
In the citing paper
“Tau oligomers and monomers can also activate NLRP3 inflammasomes, further perpetuating microglial activation [162] and potential progression of tau pathology.”
From Microglia and monocytes in inflammatory CNS disease: integrating phenotype and function (2022) · cites this paper as [162]
The cited source says what the claim attributes to it.
In the citing paper
“Treatment of wild-type primary microglia with recombinant wild-type tau and recombinant tau with a P301S mutation increased IL-1β secretion, an effect that was attenuated in Nlrp3−/− and Asc−/− microglia, suggesting that tau induces IL-1β secretion in a NLRP3-dependent manner [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Inhibiting or downregulating the NLRP3 inflammasome ameliorates AD neuropathology in animal models, which opens up a therapeutic avenue for modulators of NLRP3 activation in AD.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“On the other hand, treatment of mouse primary hippocampal neurons with conditioned media from wild-type, but not Nlrp3−/− and Asc−/−, microglia primed with LPS resulted in elevated total and phosphorylated tau levels, suggesting that NLRP3 inflammasome activation in microglia can induce tau pathology in neurons.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Treatment of wild-type primary microglia with recombinant wild-type tau and recombinant tau with a P301S mutation increased IL-1β secretion, an effect that was attenuated in Nlrp3−/− and Asc−/− microglia, suggesting that tau induces IL-1β secretion in a NLRP3-dependent manner [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“The NLRP3 inflammasome has a bidirectional relationship with AD-related tau pathology as well.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Evidence suggests that while some forms of tau can activate the NLRP3 inflammasome, inflammasome activation can exacerbate tau pathology by promoting elevated phosphorylation of tau [81, 82].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Moreover, treatment with brain homogenates from APP/PS1 mice induced tau hyperphosphorylation in a mouse model of tau aggregation pathology (Tau22) but not in Tau22/Nlrp3−/− and Tau22/Asc−/− mice, indicating the NLRP3 inflammasome as a mediator of Aβ-induced tau pathology [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Moreover, treatment with brain homogenates from APP/PS1 mice induced tau hyperphosphorylation in a mouse model of tau aggregation pathology (Tau22) but not in Tau22/Nlrp3−/− and Tau22/Asc−/− mice, indicating the NLRP3 inflammasome as a mediator of Aβ-induced tau pathology [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Evidence suggests that while some forms of tau can activate the NLRP3 inflammasome, inflammasome activation can exacerbate tau pathology by promoting elevated phosphorylation of tau [81, 82].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“In Tau22 mice, ablation of Nlrp3 or Asc reduced levels of hyperphosphorylated tau and tau aggregates and rescued tau-induced spatial memory deficits [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
In the citing paper
“Studies have demonstrated important roles of the NLRP3 inflammasome in aging and age-related diseases, such as atherosclerosis metabolic syndrome, type 2 diabetes, and Alzheimer’s disease (81–83).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [83]
In the citing paper
“For example, in AD and frontotemporal dementia, neuroinflammation and microglia activation potentiate the spreading of pathological tau neurofibrillary tangles (83, 175).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [83]
In the citing paper
“In AD, this relationship may be mediated by NLRP3 inflammasome activation in microglia, a process that activates tau kinases (e.g., GSK-3β and CaMKII-α) and results in tau hyperphosphorylation (83).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [83]
In the citing paper
“The knockout of ASC or NLRP3 ameliorates AD‐like brain pathology in animal models. 68”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [68]
In the citing paper
“The activation of the NLRP3 inflammasome drives tau pathology. 68”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [68]
In the citing paper
“Inflammaging can drive tau pathology and neurodegeneration in AD by impairing the clearance of Aβ peptides, altering BBB integrity, and affecting the synaptic functions. 68”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [68]
In the citing paper
“A recent study shows that NLR family pyrin domain-containing protein 3 (NLRP3) inflammasome activation induces tau hyperphosphorylation and aggregation through modulating tau kinases and phosphatases [159].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [159]
In the citing paper
“In the CNS, inflammasome activation has been mainly linked to neuroinflammatory conditions. As example, it has an essential role in the progression of several neurological disorders like MS, AD, PPD, and NPS (132, 193–197).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“In general, patients affected by tauopathies showed elevated levels of cleaved caspase-1 and ASC and mature IL-1β in the cortex (197).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“Injecting brain homogenates from APP/PS1 or wild-type mice into the hippocampus of Tau22 mice, induced tau hyperphosphorylation in the hippocampus of Tau22 wild-type but not Tau22/Pycard−/− or Tau22/Nlrp3−/− deficient mice”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“suggesting that NLRP3 activation is upstream the Aβ-tau cascade and tau pathology (197).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“Consistent with this, Tau22 mice lacking ASC or NLRP3 expression had lower levels of aggregated and hyperphosphorylated tau in the hippocampus, and their typical spatial memory deficits were rescued (197).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“Also, Tau22 mice, another model of AD and other tauopathies, had increased levels of cleaved caspase-1 and ASC in their brain at the age of 11 months compared to their 3-month-old counterparts.”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“Further, activated microglia promote tau phosphorylation and aggregation by activation of the NLRP3 (nucleotide binding oligomerisation domain (NOD)-, leucine-rich repeat (LRR)- and pyrin domain-containing protein 3) inflammasome in response to amyloid-β [22,23].”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [23]
In the citing paper
“Further, there is evidence tauopathy is driven by NLRP3 inflammasome activation in microglia in response to amyloid-β [23].”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [23]
In the citing paper
“ROS from NOX4 also contribute to activation of the NLRP3 inflammasome, a driver of both amyloid-β [156] and tau [23] pathology.”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [23]
In the citing paper
“Growing evidence indicates that Aβ accumulation stimulates tau phosphorylation and fibrillary tangle formation, leading to the process of neurodegeneration.112–114”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [112]
In the citing paper
“In particular, microglial NLRP3 has been shown to be a major driver of amyloid beta and tau toxicity in AD, suggesting its activation has important implications for disease progression (Halle et al, 2008; Venegas et al, 2017; Ising et al, 2019).”
From Mechanisms of DNA damage-mediated neurotoxicity in neurodegenerative disease (2022) · cites this paper as Ising et al, 2019
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Metadata
- Authors
- Ising, C., Venegas, C., Zhang, S., Scheiblich, H., Schmidt, S. V., Vieira-Saecker, A., Schwartz, S., Albasset, S., McManus, R. M., Tejera, D., Griep, A., Santarelli, F., Brosseron, F., Opitz, S., Stunden, J., Merten, M., Kayed, R., Golenbock, D. T., Blum, D., Latz, E., Buée, L., & Heneka, M. T.
- Affiliations
- University Hospital Bonn (DE)
- German Center for Neurodegenerative Diseases (DE)
- The University of Texas Medical Branch at Galveston (US)
- University of Massachusetts Chan Medical School (US)
- Inserm (FR)
- Corresponding author
- Heneka, Michael T.
- ORCID
- Venue
- Nature
- Published
- 2019-11-20
- Volume
- 575
- Issue
- 7784
- Pages
- 669-673
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7324015
- OpenAlex
- W2990312754
- Semantic Scholar
- 6a9d745a33a2d013c621f57586d9d719671530a7
- Cited by
- 1,487
- References
- 28
- Citations by year
- 2026: 189 · 2025: 226 · 2024: 255 · 2023: 226 · 2022: 248 · 2021: 193 · 2020: 143 · 2019: 3
- FWCI
- 101.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion, other-oa)
- HAL (submittedVersion, other-oa)
- RePEc: Research Papers in Economics (submittedVersion)
- Institutional Repository of the University of Granada (University of Granada) (submittedVersion, cc-by-nc-nd)
- DZNE Pub (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (R01 AG059752-02)
- Agence Nationale de la Recherche (ANR-11-LABX-0009)
- Deutsches Zentrum für Neurodegenerative Erkrankungen
- National Institutes of Health
- National Institute on Aging (R01AG059752, R01AG054025)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- NLRP3 inflammasome, tau hyperphosphorylation, tau aggregation, neurofibrillary tangles, Alzheimer's disease, amyloid-beta, microglia, amyloid hypothesis, frontotemporal dementia, neuroinflammation, caspase-1, IL-1β
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Gene Expression Regulation, Humans, Mice, Inbred C57BL, Phosphorylation, tau Proteins, Microglia, Cyclin-Dependent Kinase 5, Mice, Inflammasomes, Protein Aggregation, Pathological
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