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The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Open accessAbstract
The fibrillar peptide amyloid-beta (A beta) has a chief function in the pathogenesis of Alzheimer's disease. Interleukin 1 beta (IL-1 beta) is a key cytokine in the inflammatory response to A beta. Insoluble materials such as crystals activate the inflammasome formed by the cytoplasmic receptor NALP3, which results in the release of IL-1 beta. Here we identify the NALP3 inflammasome as a sensor of A beta in a process involving the phagocytosis of A beta and subsequent lysosomal damage and release of cathepsin B. Furthermore, the IL-1 beta pathway was essential for the microglial synthesis of proinflammatory and neurotoxic factors, and the inflammasome, caspase-1 and IL-1 beta were critical for the recruitment of microglia to exogenous A beta in the brain. Our findings suggest that activation of the NALP3 inflammasome is important for inflammation and tissue damage in Alzheimer's disease.
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“Based on the previous literature42,43,46, we reasoned that cathepsin B leaking from the destabilized lysosomes may mediate the NLRP3 inflammasome activation upon SHIP1 inhibition11.”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [43]
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
“Fibrillar Aβ (fAβ), following phagocytosis by microglia, activates the NLRP3 inflammasome and leads to increases in secretion of IL-1β and IL-18.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
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
“Sustained elevations of IL-1β have been postulated to play a key role in AD pathogenesis [6, 12–14].”
From 25-Hydroxycholesterol amplifies microglial IL-1β production in an apoE isoform-dependent manner (2020) · cites this paper as [13]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Halle et al. found that fibrillar Aβ can induce the secretion of IL-1β which depends on the presence of NLRP3.352,353”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [352]
The cited source says what the claim attributes to it.
In the citing paper
“lysosomal cathepsins, such as cathepsin B, can induce NLRP3 inflammasome activation upon leaking into the cytosol following lysosomal membrane permeabilization (LMP)42,43”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [43]
The cited source says what the claim attributes to it.
In the citing paper
“fAβ phagocytosis results in lysosomal dysfunction and release of lysosomal contents into the cytoplasm, including the lysosomal protease cathepsin B, which is a mediator of inflammasome activation induced by Aβ [78].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
The cited source says what the claim attributes to it.
In the citing paper
“In line with these findings, another study showed that aggregated tau seeds activated the NLRP3 inflammasome in primary mouse microglia by inducing lysosomal destabilization and release of the lysosomal protease cathepsin B, similar to fAβ [78, 82].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
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In the citing paper
“In parallel, reduction of SHIP1 activity is poised to disinhibit signaling pathways that are involved in the phagocytosis of Aβ, which is a required step for Aβ-induced activation of the NLRP3 inflammasome [78].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
In the citing paper
“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 [426]
In the citing paper
“Following phagocytosis by microglia, Aβ activates the NLRP3 inflammasome leading to caspase-1 activation and IL-1β maturation and release (Halle et al., 2008).”
From Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019) · cites this paper as Halle et al., 2008
In the citing paper
“Fibrillar Aβ amyloids can induce the secretion of IL-1β from microglia, via the NLRP3 inflammasome (228, 249).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [228]
In the citing paper
“Importantly, researchers also found that ASC-, caspase-1-, IL-1 receptor-, and MyD88-deficient mice had less recruitment of microglia and mononuclear phagocytes to Aβ in the brain as compared to the wild type control after the injection of Aβ into the striatum (228).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [228]
In the citing paper
“NLRP3 has been shown to respond to sterile stimuli, including asbestos, silica, MSU and CPPD crystals55, cholesterol crystals and β-amyloid fibrils56.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
In the citing paper
“Furthermore, there is only partial inhibition of the neutrophil infiltration and IL-1β production associated with sterile inflammation in response to cholesterol crystals44,56,59,67.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
In the citing paper
“However, cathepsin b-deficient macrophages have no impairment in IL-1β production in response to certain NLRP3 agonists, including LPS plus ATP, or MSU crystals, despite the impairment in their response to silica44,56,59,67.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
In the citing paper
“evidence to support this are the observations that artificial lysosomal rupture alone can activate NLRP3 and that pharmacological inhibition or genetic depletion of cathepsin b results in inhibition of caspase 1 activation, although this inhibition was only partial44,56,59.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
In the citing paper
“In support of this, direct treatment of ATP on primed microglia is sufficient for maturation and release of IL-1β in vitro (Halle et al, 2008) and does so via the P2X 7 receptor (Colomar et al, 2003) expressed on microglia (Monif et al, 2009).”
From Repeated Social Defeat, Neuroinflammation, and Behavior: Monocytes Carry the Signal (2017) · cites this paper as Halle et al, 2008
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 Halle et al, 2008
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Self-citation
Metadata
- Authors
- Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Harvard University (US)
- University of Freiburg (DE)
- Corresponding author
- Golenbock, Douglas T
- ORCID
- Venue
- Nature Immunology
- Published
- 2008-07-11
- Volume
- 9
- Issue
- 8
- Pages
- 857-865
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- PMC
- PMC3101478
- OpenAlex
- W2119098586
- Cited by
- 2,441
- References
- 50
- Citations by year
- 2026: 92 · 2025: 124 · 2024: 143 · 2023: 165 · 2022: 191 · 2021: 188 · 2020: 169 · 2019: 151 · 2018: 136 · 2017: 139 · 2016: 138 · 2015: 146 · 2014: 149 · 2013: 153 · 2012: 98
- FWCI
- 35.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship@UMassChan (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- National Institute on Aging (R01AG020255, AG20255)
- National Institute of General Medical Sciences (R37GM054060, R01GM054060, GM 54060)
- National Institute of Allergy and Infectious Diseases (AI065483, R01AI065483)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- NLRP3 inflammasome, amyloid-beta, Alzheimer's disease, innate immunity, IL-1β, caspase-1, microglia, phagocytosis, lysosomal damage, cathepsin B, neuroinflammation, neurotoxicity
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Alzheimer Disease, Carrier Proteins, Immunity, Innate, Inflammation, Amyloid beta-Peptides, Inflammation Mediators
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