NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Open accessAbstract
Alzheimer’s disease is the world’s most common dementing illness. Deposition of amyloid-β peptide drives cerebral neuroinflammation by activating microglia. Indeed, amyloid-β activation of the NLRP3 inflammasome in microglia is fundamental for interleukin-1β maturation and subsequent inflammatory events. However, it remains unknown whether NLRP3 activation contributes to Alzheimer’s disease in vivo. Here we demonstrate strongly enhanced active caspase-1 expression in human mild cognitive impairment and brains with Alzheimer’s disease, suggesting a role for the inflammasome in this neurodegenerative disease. Nlrp3−/− or Casp1−/− mice carrying mutations associated with familial Alzheimer’s disease were largely protected from loss of spatial memory and other sequelae associated with Alzheimer’s disease, and demonstrated reduced brain caspase-1 and interleukin-1β activation as well as enhanced amyloid-β clearance. Furthermore, NLRP3 inflammasome deficiency skewed microglial cells to an M2 phenotype and resulted in the decreased deposition of amyloid-β in the APP/PS1 model of Alzheimer’s disease. These results show an important role for the NLRP3/caspase-1 axis in the pathogenesis of Alzheimer’s disease, and suggest that NLRP3 inflammasome inhibition represents a new therapeutic intervention for the disease.
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Rat research has identified the NLRP3-ASC inflammasome as a major mechanism through which microglia may drive pathological features of AD.
“Rat research has identified the NLRP3-ASC inflammasome as a major mechanism through which microglia may drive pathological features of AD [92,93,94].”
From The Role of Cortisol in Chronic Stress, Neurodegenerative Diseases, and Psychological Disorders (2023) · cites this paper as [92]
The supplied passages (labelled Abstract; no page given) link the microglial NLRP3 inflammasome to AD-related pathology and identify ASC specks in activated microglia. But the experimental animals were APP/PS1 mice, not rats, so this source does not support the claim's species designation. (LLM, conf=0.90)
Experimental — accuracy not yet measuredBoth beta-amyloids and tau can activate the NLRP3-ASC inflammasome within microglia.
“Both beta-amyloids and tau can activate the NLRP3-ASC inflammasome within microglia [92,93].”
From The Role of Cortisol in Chronic Stress, Neurodegenerative Diseases, and Psychological Disorders (2023) · cites this paper as [92]
The Abstract states that Aβ activates the NLRP3 inflammasome in microglia, and the Methods summary reports detecting microglial ASC specks. The copy does not establish that tau activates this inflammasome; a search for tau found no supporting passage. (LLM, conf=0.90)
Experimental — accuracy not yet measuredThe NLRP3 within microglia recruits the adaptor protein ASC to form an inflammasome complex.
“The nucleotide-binding oligomerization domain-like receptor, pyrin domain-containing 3 (NLRP3), within microglia recruits the adaptor protein apoptosis-associated speck-like protein containing a C-terminal caspase recruitment domain (ASC) to form an inflammasome complex.”
From The Role of Cortisol in Chronic Stress, Neurodegenerative Diseases, and Psychological Disorders (2023) · cites this paper as [92]
The paper reports microglial expression of NLRP3 and ASC and describes ASC speck formation in APP/PS1 microglia as consistent with inflammasome activation (Fig. 1d; page unavailable in our copy). It does not state or directly demonstrate the specific step that NLRP3 recruits ASC to form the complex. (LLM, conf=0.82)
Experimental — accuracy not yet measuredIn APP/PS1 mice model, NLRP3 knockout reduced Aβ deposition by enhancing phagocytic clearance capacity and increasing extracellular Aβ degradation by IDE.
“In APP/PS1 mice model, NLRP3 knockout reduced Aβ deposition by enhancing phagocytic clearance capacity and increasing extracellular Aβ degradation by insulin- degrading enzyme (IDE).354”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [354]
The passages labelled Abstract report reduced Aβ deposition and greater microglial Aβ uptake in APP/PS1/NLRP3−/− mice. They also report increased IDE, but say it is “likely” to enhance Aβ degradation; they do not establish increased extracellular degradation by IDE as a measured mechanism. (LLM, conf=0.85)
Experimental — accuracy not yet measuredActivation of hippocampal NLRP3 inflammasome-mediated pyroptosis is associated with neuronal damage, cognitive decline, and neuronal death.
“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 Heneka et al., 2013
The Results passages (page not provided) report that NLRP3 or caspase-1 deficiency protected APP/PS1 mice from memory deficits, hippocampal LTP suppression, and reduced neuronal spine density. They support an association with cognitive decline and neuronal dysfunction, but do not establish inflammasome-mediated pyroptosis or neuronal death. (LLM, conf=0.88)
Experimental — accuracy not yet measured
NLRP3 or caspase-1 knockdown in AD mouse models decreases Aβ accumulation, improves spatial memory, and alleviates other AD-related symptoms.
“NLRP3 or caspase-1 knockdown in AD mouse models has yielded promising results in decreasing Aβ accumulation, improving spatial memory, and alleviating other AD-related symptoms (Heneka et al., 2013).”
From Picroside II Alleviates the Progression of Alzheimer’s Disease via the NLRP3/Caspase-1/GSDMD Pathway (2025) · cites this paper as Heneka et al., 2013
The Abstract reports reduced Aβ deposition and protection from spatial-memory loss and other AD-associated effects in APP/PS1 mice deficient in NLRP3 or caspase-1. The Methods summary identifies these mice as gene knockouts, not knockdowns; the claimed intervention is therefore inaccurate. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAblation of Nlrp3 or Casp1 in APP/PS1 mice rescues spatial memory and behavioral deficits, LTP suppression and spine loss.
“Ablation of Nlrp3 or Casp1 in APP/PS1 mice rescued spatial memory and behavioral deficits, LTP suppression and spine loss observed in these mice [77].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [77]
The paper’s results passage (indexed under Abstract; page unavailable) reports that NLRP3 or caspase-1 deficiency largely protected APP/PS1 mice from spatial-memory impairment and prevented LTP suppression and reduced spine density. It reports improved open-field behavior for NLRP3-deficient mice, but does not establish that caspase-1 deficiency rescued those behavioral deficits. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAnother study reported strongly increased levels of active caspase-1 in early-onset Alzheimer's disease and late-onset Alzheimer's disease patients as well as in mildly cognitively impaired individuals.
“However, another study reported strongly increased levels of active caspase-1 in early-onset AD and LOAD patients as well as in MCI individuals [77].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [77]
The passage describing the human brain analysis (indexed under Abstract; no page given) reports substantially increased cleaved caspase-1 in AD, early-onset AD, and MCI patients compared with controls. It does not explicitly identify the separate AD group as late-onset AD, so that part of the claim is not fully established by our copy. (LLM, conf=0.83)
Experimental — accuracy not yet measuredThe inflammasome complex is responsible for the production of IL-1 beta, a proinflammatory cytokine.
“This inflammasome complex is responsible for the production of IL-1 beta, which is a proinflammatory cytokine.”
From The Role of Cortisol in Chronic Stress, Neurodegenerative Diseases, and Psychological Disorders (2023) · cites this paper as [92]
IL-1 beta exacerbates tau pathologies and reduces microglial phagocytic activity.
“IL-1 beta was shown to exacerbate tau pathologies [97] and reduce microglial phagocytic activity [92,93,94].”
From The Role of Cortisol in Chronic Stress, Neurodegenerative Diseases, and Psychological Disorders (2023) · cites this paper as [92]
Microglial function may be relevant to cognitive performance, as suggested by experimental data showing improved microglial clearance was protective for memory function.
“Furthermore, microglial function may also be of relevance to cognitive performance, as suggested by recent experimental data, which showed that improved microglial clearance was protective in terms of memory function (17).”
From SUCLG2 identified as both a determinator of CSF Aβ1–42 levels and an attenuator of cognitive decline in Alzheimer's disease (2014) · cites this paper as [17]
Proinflammatory environments and signalling are a prominent observation in AD brain pathology.
“Proinflammatory environments and signalling are a prominent observation in AD brain pathology [39].”
From Heterozygous expression of the Alzheimer’s disease-protective PLCγ2 P522R variant enhances Aβ clearance while preserving synapses (2022) · cites this paper as [39]
Inhibiting or downregulating NLRP3 inflammasome ameliorates AD neuropathology in animal models.
“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 [77]
APP/PS1/Nlrp3−/− and APP/PS1/Casp1−/− mice display decreased Aβ plaque deposition.
“APP/PS1/Nlrp3−/− and APP/PS1/Casp1−/− mice also displayed decreased Aβ plaque deposition, suggesting that NLRP3 inflammasome activation impairs microglial capacity to clear Aβ [77].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [77]
NLRP3 inflammasome activation impairs microglial capacity to clear Aβ.
“APP/PS1/Nlrp3−/− and APP/PS1/Casp1−/− mice also displayed decreased Aβ plaque deposition, suggesting that NLRP3 inflammasome activation impairs microglial capacity to clear Aβ [77].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [77]
Decreased plaque deposition in APP/PS1/Nlrp3−/− and APP/PS1/Casp1−/− mice is related to increased levels of IDE.
“The decreased plaque deposition was also related to increased levels of the proteolytic enzyme insulin-degrading enzyme (IDE) [77], previously reported to degrade Aβ [83].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [77]
One of the key biological functions of CASP1 is the cleavage of prointerleukin-1β (IL-1β) into the mature biological active cytokine, which is largely overexpressed in brains of patients with AD.
“One of the key biological functions of CASP1 is the cleavage of prointerleukin-1β (IL-1β) into the mature biological active cytokine, which is largely overexpressed in brains of patients with AD.44”
From APOE*E2 allele delays age of onset in PSEN1 E280A Alzheimer’s disease (2016) · cites this paper as [44]
Preclinical studies support the concept that CASP1-directed increase of IL-1β can augment the deposition of β-amyloid within the brain to worsen Alzheimer's symptoms.
“Preclinical studies support the concept that CASP1-directed increase of IL-1β can augment the deposition of β-amyloid within the brain to worsen Alzheimer's symptoms.44”
From APOE*E2 allele delays age of onset in PSEN1 E280A Alzheimer’s disease (2016) · cites this paper as [44]
CASP1, an essential component of NLPR3 inflammasomes, encodes a cysteine protease that is largely overexpressed in brains of patients with AD.
“CASP1, an essential component of NLPR3 inflammasomes, encodes a cysteine protease that is largely overexpressed in brains of patients with AD.44”
From APOE*E2 allele delays age of onset in PSEN1 E280A Alzheimer’s disease (2016) · cites this paper as [44]
Aβ activates NF-κB signaling and the NLRP3-ASC inflammasome.
“Notably, Aβ also can activate NF-κB signaling and the NLRP3-ASC inflammasome [426, 427], suggesting that Aβ and tau share common mechanisms in microglia activation.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [427]
The NLRP3 inflammasome is critical for maturation of IL-1β, and loss of NLRP3 in APP/PS1 mice decreases amyloid burden.
“The NLRP3 inflammasome is critical for maturation of IL-1β, and loss of NLRP3 in APP/PS1 decreased amyloid burden (131).”
From Microglia in Alzheimer's disease (2017) · cites this paper as [131]
Microglia express several receptors that bind amyloid-beta and trigger inflammation, including CD36, TLR2, TLR4, TLR6, and NLRP3.
“Microglia express multiple receptors that can bind Aβ and trigger inflammation, such as CD36 (105), TLR2, TLR4, TLR6 (17), and NLRP3 (106)”
From Microglia Function in the Central Nervous System During Health and Neurodegeneration (2017) · cites this paper as [106]
NLRP3 and caspase-1 deletion decreases Aβ deposition, reduces microglial IL-1β release, and improves cognition in APPPS1 mice.
“NLRP3 and caspase-1 genetic deletion results in decreased Aβ deposition, reduced IL-1β release from microglia and improved cognitive performance in APPPS1 mice (Heneka et al., 2013).”
From Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019) · cites this paper as Heneka et al., 2013
Toll-like receptors and NOD-like receptors have been implicated in the microglia response to Aβ accumulation and mediate an inflammatory response that contributes to pathology.
“Toll-like receptors and NOD-like receptors have been previously implicated in the microglia response to Aβ accumulation and shown to mediate an inflammatory response that contributes to pathology”
From TREM2 Maintains Microglial Metabolic Fitness in Alzheimer’s Disease (2017) · cites this paper as Heneka et al., 2013
ITGAM/CD11b is a cell surface receptor involved in activation, migration and phagocytosis of immune cells, and is used as a marker of activated microglia.
“ITGAM/CD11b (or CR3A), is a cell surface receptor involved in activation, migration and phagocytosis of immune cells, so much so that ITGAM/CD11b is used as a marker of activated microglia (Matsuoka et al., 2001; Heneka et al., 2013; Kamphuis et al., 2016).”
From Genetic variability in response to amyloid beta deposition influences Alzheimer’s disease risk (2019) · cites this paper as Heneka et al., 2013
APP/PS1 mice lacking ASC, caspase-1, or NLRP3 had significantly reduced hippocampal and cortical amyloid plaque deposition and ameliorated disease outcome.
“Animal studies confirmed this significant involvement of NLRP activation, as APP/PS1 mice, lacking the expression of ASC, caspase-1, or NLRP3 had significantly reduced hippocampal and cortical amyloid plaque deposition and ameliorated disease outcome (229, 230).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [230]
An alternative pathway has been described for intracellular signaling produced by the binding of Aβ to microglial cells, activating NLRP3 inflammasome.
“Recently, an alternative pathway has been described for intracellular signaling produced by the binding of Aβ to microglial cells, activating NLRP3 inflammasome (Heneka et al., 2013; Sheedy et al., 2013).”
From The role of microglia in retinal neurodegeneration: Alzheimer’s disease, parkinson, and glaucoma. (2017) · cites this paper as Heneka et al., 2013
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- Authors
- Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., Gelpi, E., Halle, A., Korte, M., Latz, E., & Golenbock, D. T.
- Affiliations
- University of Bonn (DE)
- Technische Universität Braunschweig (DE)
- University of Massachusetts Chan Medical School (US)
- Center of Advanced European Studies and Research (DE)
- Corresponding author
- Heneka, Michael T.
- Latz, Eicke
- Golenbock, Douglas T.
- ORCID
- Venue
- Nature
- Published
- 2012-12-19
- Volume
- 493
- Issue
- 7434
- Pages
- 674-678
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3812809
- OpenAlex
- W1993976394
- Semantic Scholar
- 3a962c33176c94bc0dd8bfea4ebe2eb83be8a01e
- Cited by
- 2,898
- References
- 34
- Citations by year
- 2026: 274 · 2025: 270 · 2024: 273 · 2023: 270 · 2022: 306 · 2021: 314 · 2020: 261 · 2019: 203 · 2018: 187 · 2017: 147 · 2016: 117 · 2015: 112 · 2014: 99 · 2013: 62
- FWCI
- 35.07
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion, other-oa)
- HZI (Helmholtz Centre for Infection Research) (submittedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Max Planck Digital Library (submittedVersion)
- DZNE Pub (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- Genentech
- National Heart, Lung, and Blood Institute (R01HL093262)
- National Institute of General Medical Sciences (R01GM054060)
- National Institute of Allergy and Infectious Diseases (U19AI084048, R01AI083713)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- NLRP3 inflammasome, caspase-1, Alzheimer's disease, amyloid-beta, APP/PS1 mice, microglia, neuroinflammation, IL-1β, amyloid-beta clearance, spatial memory, NLRP3 knockout mice, cognitive impairment, therapeutic target
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Aged, Aged, 80 and over, Alzheimer Disease, Animals, Behavior, Animal, Brain, Carrier Proteins, Humans, Memory, Mice, Inbred C57BL, Mice, Transgenic, Phagocytosis, Gene Expression Regulation, Enzymologic, Amyloid beta-Peptides, Caspase 1, Mice, Nitric Oxide Synthase Type II, Interleukin-1beta, Inflammasomes, Cognitive Dysfunction
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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