NLRP3 inflammasome activation drives tau pathology – Nature.com

  • 1.

    Ising, C. & Heneka, M. T. Functional and structural damage of neurons by innate immune mechanisms during neurodegeneration. Cell Death Dis. 9, 120 (2018).

  • 2.

    Heneka, M. T., McManus, R. M. & Latz, E. Inflammasome signalling in brain function and neurodegenerative disease. Nat. Rev. Neurosci. 19, 610–621 (2018).

  • 3.

    Venegas, C. et al. Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease. Nature 552, 355–361 (2017).

  • 4.

    Halle, A. et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat. Immunol. 9, 857–865 (2008).

  • 5.

    Heneka, M. T. et al. NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice. Nature 493, 674–678 (2013).

  • 6.

    Lewis, J. & Dickson, D. W. Propagation of tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies. Acta Neuropathol. 131, 27–48 (2016).

  • 7.

    Schindowski, K. et al. Alzheimer’s disease-like tau neuropathology leads to memory deficits and loss of functional synapses in a novel mutated tau transgenic mouse without any motor deficits. Am. J. Pathol. 169, 599–616 (2006).

  • 8.

    Youm, Y.-H. et al. Canonical Nlrp3 inflammasome links systemic low-grade inflammation to functional decline in aging. Cell Metab. 18, 519–532 (2013).

  • 9.

    Taylor, J. M. et al. Type-1 interferon signaling mediates neuro-inflammatory events in models of Alzheimer’s disease. Neurobiol. Aging 35, 1012–1023 (2014).

  • 10.

    Minter, M. R. et al. Soluble amyloid triggers a myeloid differentiation factor 88 and interferon regulatory factor 7 dependent neuronal type-1 interferon response in vitro. J. Neuroinflammation 12, 71 (2015).

  • 11.

    Iqbal, K. et al. Tau pathology in Alzheimer disease and other tauopathies. Biochim. Biophys. Acta 1739, 198–210 (2005).

  • 12.

    Ortega-Gutiérrez, S., Leung, D., Ficarro, S., Peters, E. C. & Cravatt, B. F. Targeted disruption of the PME-1 gene causes loss of demethylated PP2A and perinatal lethality in mice. PLoS ONE 3, e2486 (2008).

  • 13.

    Laurent, C. et al. Hippocampal T cell infiltration promotes neuroinflammation and cognitive decline in a mouse model of tauopathy. Brain J. Neurol. 140, 184–200 (2017).

  • 14.

    Peluffo, H. et al. Overexpression of the immunoreceptor CD300f has a neuroprotective role in a model of acute brain injury. Brain Pathol. 22, 318–328 (2012).

  • 15.

    Epstein, I. & Finkbeiner, S. The Arc of cognition: Signaling cascades regulating Arc and implications for cognitive function and disease. Semin. Cell Dev. Biol. 77, 63–72 (2018).

  • 16.

    Bhaskar, K. et al. Regulation of tau pathology by the microglial fractalkine receptor. Neuron 68, 19–31 (2010).

  • 17.

    Stancu, I.-C. et al. Aggregated Tau activates NLRP3-ASC inflammasome exacerbating exogenously seeded and non-exogenously seeded Tau pathology in vivo. Acta Neuropathol. 137, 599–617 (2019).

  • 18.

    Asai, H. et al. Depletion of microglia and inhibition of exosome synthesis halt tau propagation. Nat. Neurosci. 18, 1584–1593 (2015).

  • 19.

    Götz, J., Chen, F., van Dorpe, J. & Nitsch, R. M. Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils. Science 293, 1491–1495 (2001).

  • 20.

    Bolmont, T. et al. Induction of tau pathology by intracerebral infusion of amyloid-beta -containing brain extract and by amyloid-beta deposition in APP × Tau transgenic mice. Am. J. Pathol. 171, 2012–2020 (2007).

  • 21.

    Shafiei, S. S., Guerrero-Muñoz, M. J. & Castillo-Carranza, D. L. Tau oligomers: cytotoxicity, propagation, and mitochondrial damage. Front. Aging Neurosci. 9, 83 (2017).

  • 22.

    Usenovic, M. et al. Internalized tau oligomers cause neurodegeneration by inducing accumulation of pathogenic tau in human neurons derived from induced pluripotent stem cells. J. Neurosci. Off. J. Soc. Neurosci. 35, 14234–14250 (2015).

  • 23.

    Karch, C. M., Jeng, A. T. & Goate, A. M. Extracellular Tau levels are influenced by variability in Tau that is associated with tauopathies. J. Biol. Chem. 287, 42751–42762 (2012).

  • 24.

    Yamada, K. et al. Neuronal activity regulates extracellular tau in vivo. J. Exp. Med. 211, 387–393 (2014).

  • 25.

    Kanneganti, T.-D. et al. Bacterial RNA and small antiviral compounds activate c through cryopyrin/Nalp3. Nature 440, 233–236 (2006).

  • 26.

    Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muoz, M. J., Jackson, G. R. & Kayed, R. Preparation and characterization of neurotoxic tau oligomers. Biochemistry 49, 10039–10041 (2010).

  • 27.

    Ising, C. et al. AAV-mediated expression of anti-tau scFvs decreases tau accumulation in a mouse model of tauopathy. J. Exp. Med. 214, 1227–1238 (2017).

  • 28.

    Szklarczyk, D. et al. The STRING database in 2017: quality-controlled protein-protein association networks, made broadly accessible. Nucleic Acids Res. 45 (D1), D362–D368 (2017).

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