Neuronal NLRP1 inflammasome activation of Caspase-1 coordinately regulates inflammatory interleukin-1-beta production and axonal degeneration-associated Caspase-6 activation
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Neuronal active Caspase-6 (Casp6) is associated with Alzheimer disease (AD), cognitive impairment, and axonal degeneration. Caspase-1 (Casp1) can activate Casp6 but the expression and functionality of Casp1-activating inflammasomes has not been well-defined in human neurons. Here, we show that primary cultures of human CNS neurons expressed functional Nod-like receptor protein 1 (NLRP1), absent in melanoma 2, and ICE protease activating factor, but not the NLRP3, inflammasome receptor components. NLRP1 neutralizing antibodies in a cell-free system, and NLRP1 siRNAs in neurons hampered stress-induced Casp1 activation. NLRP1 and Casp1 siRNAs also abolished stress-induced Casp6 activation in neurons. The functionality of the NLRP1 inflammasome in serum-deprived neurons was also demonstrated by NLRP1 siRNA-mediated inhibition of speck formation of the apoptosis-associated speck-like protein containing a caspase recruitment domain conjugated to green fluorescent protein. These results indicated a novel stress-induced intraneuronal NLRP1/Casp1/Casp6 pathway. Lipopolysaccharide induced Casp1 and Casp6 activation in wild-type mice brain cortex, but not in that of Nlrp1(-/-) and Casp1(-/-) mice. NLRP1 immunopositive neurons were increased 25- to 30-fold in AD brains compared with non-AD brains. NLRP1 immunoreactivity in these neurons co-localized with Casp6 activity. Furthermore, the NLRP1/Casp1/Casp6 pathway increased amyloid beta peptide 42 ratio in serum-deprived neurons. Therefore, CNS human neurons express functional NLRP1 inflammasomes, which activate Casp1 and subsequently Casp6, thus revealing a fundamental mechanism linking intraneuronal inflammasome activation to Casp1-generated interleukin-1-β-mediated neuroinflammation and Casp6-mediated axonal degeneration.
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Mitochondrial abnormalities, synaptic loss and dysfunction, altered axonal transport, and activation of cell death pathways have been implicated as consequences of tau mislocalization or oligomerization.
“Mitochondrial abnormalities, synaptic loss and dysfunction, altered axonal transport, and activation of cell death pathways (including caspase activation and inflammatory responses) have all been directly or indirectly implicated as consequences of tau mislocalization or oligomerization (20, 40, 43–52).”
From All the Tau We Cannot See (2023) · cites this paper as [46]
Neuronal NLRP1 inflammasome and caspase-1 activation in Alzheimer's disease can induce neuronal injury and death.
“neuronal NLRP1 (NACHT, LRR and PYD domains-containing protein 1) inflammasome and caspase-1 activation in Alzheimer’s disease can induce neuronal injury and death10,11”
From Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight (2018) · cites this paper as [10]
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Self-citation
- Authors
- Kaushal, V, Dye, R., Pakavathkumar, P., Foveau, B., Flores, J., Hyman, B., Ghetti, B., Koller, B. H., & LeBlanc, A. C.
- Affiliations
- Jewish General Hospital (CA)
- University of North Carolina at Chapel Hill (US)
- Massachusetts General Hospital (US)
- Indiana University Indianapolis (US)
- Corresponding author
- LeBlanc, A C
- Venue
- Cell Death & Differentiation
- Published
- 2015-03-06
- Volume
- 22
- Issue
- 10
- Pages
- 1676-1686
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- PMC
- PMC4563782
- OpenAlex
- W1980930214
- Cited by
- 297
- References
- 58
- Citations by year
- 2026: 12 · 2025: 20 · 2024: 24 · 2023: 34 · 2022: 39 · 2021: 38 · 2020: 34 · 2019: 26 · 2018: 27 · 2017: 22 · 2016: 17 · 2015: 4
- FWCI
- 10.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Death and Differentiation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- IUScholarWorks (Indiana University) (submittedVersion)
- PMC
- Funders
- McGill University
- Alzheimer Society
- Journal of Gastroenterology and Hepatology Foundation
- National Institutes of Health
- Canadian Institutes of Health Research (MOP-243413-BCA-CGAG-45097)
- National Institute on Aging (P30AG010133)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- NLRP1 inflammasome, caspase-1, caspase-6, IL-1β, axonal degeneration, neuroinflammation, Alzheimer's disease, neuronal stress response, serum deprivation, lipopolysaccharide, amyloid-beta 42, inflammasome activation
- MeSH terms
- NLR Proteins, Alzheimer Disease, Animals, Axons, Cells, Cultured, Humans, Inflammation, Male, Neurons, Signal Transduction, Amyloid beta-Peptides, Caspase 1, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, Mice, Caspase 6, Interleukin-1beta, Inflammasomes
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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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