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The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response
Open accessAbstract
Assembly of the NLRP3 inflammasome activates caspase-1 and mediates the processing and release of the leaderless cytokine IL-1β and thereby serves a central role in the inflammatory response and in diverse human diseases. Here we found that upon activation of caspase-1, oligomeric NLRP3 inflammasome particles were released from macrophages. Recombinant oligomeric protein particles composed of the adaptor ASC or the p.D303N mutant form of NLRP3 associated with cryopyrin-associated periodic syndromes (CAPS) stimulated further activation of caspase-1 extracellularly, as well as intracellularly after phagocytosis by surrounding macrophages. We found oligomeric ASC particles in the serum of patients with active CAPS but not in that of patients with other inherited autoinflammatory diseases. Our findings support a model whereby the NLRP3 inflammasome, acting as an extracellular oligomeric complex, amplifies the inflammatory response.
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“They can also be recognized by neighboring microglia as a danger signal and induce inflammatory responses including activation of the NLRP3 inflammasome, thereby propagating inflammation [70–72].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [71]
In the citing paper
“In turn, NLRP3 inflammasome activity leads to the extracellular release of ASC particles that may function as danger signals (246).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [246]
In the citing paper
“Increased expression and activity of the NLRP3 inflammasome machinery in circulating immune cells of patients affected by depression (245), bipolar disorder (246), and ASD (226), have been reported.”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [246]
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“%) decrease in PCSK9 secretion compared with that in the WT mice (Figure 2D), suggesting that IL-1β may have a more robust effect on PCSK9 release as compared with IL-18 following exposure to inflammatory stimuli.”
BackgroundInfluentialMultistability in Macrophage Activation Pathways and Metabolic Implications
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Targeting NLRP3 inflammasome for neurodegenerative disorders
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PARK7/DJ-1 in microglia: implications in Parkinson’s disease and relevance as a therapeutic target
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“Extracellular ASC specks are able to recruit and activate both pro-caspase-1 and pro-IL-1β [4, 16].”
BackgroundDownregulation of the NLRP3 inflammasome by adiponectin rescues Duchenne muscular dystrophy
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MethodBanerjee, S., Ghosh, S., Mandal, A., Ghosh, N., & Sil, P. C. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02801-7 · Cited by 74
“These released NLRP3 and ASC act as danger signals and activate caspase 1, thereby amplifying the inflammatory response (Baroja-Mazo et al. 2014).”
BackgroundMitostasis, Calcium and Free Radicals in Health, Aging and Neurodegeneration
Godoy, J. A., Ríos, J. A., Picón-Pagès, P., Herrera-Fernández, V., Swaby, B., Crepin, G., Vicente, R., Fernández‐Fernández, J. M., & Muñoz, F. J. (2021) · Biomolecules · doi:10.3390/biom11071012 · Cited by 73
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“It has been demonstrated that the NLRP3 inflammasome particles are released from caspase‐1-activated macrophages and act as a particulate danger signal that amplifies the inflammatory response [35].”
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MethodThe inflammasome pathway in stable COPD and acute exacerbations
Faner, R., Sobradillo, P., Noguera, A., Gómez, C., Cruz, T., López-Giraldo, A., Ballester, E., Soler, N., Aróstegui, J. I., Pelegrín, P., et al. (2016) · ERJ Open Research · doi:10.1183/23120541.00002-2016 · Cited by 74
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“Franklin (79) and Baroja-Mazo (77) reported that inflammasome specks or particles are present in the extracellular environment, perhaps through the release of intracellular contents during pyroptotic cell death.”
BackgroundResultInfluentialXie, L., Gu, Z., Liu, H., Jia, B., Wang, Y., Cao, M., Song, R., Zhang, Z., & Bian, Y. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01251 · Cited by 70
The Role of NF-κB Triggered Inflammation in Cerebral Ischemia
Jover‐Mengual, T., Hwang, J.-Y., Byun, H.-R., Court-Vazquez, B. L., Centeno, J. M., Burguete, M. C., & Zukin, R. S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.633610 · Cited by 69
“…expression, among others, of the nuclear factor-kappaB (NF-κB), a proinflammatory transcription factor involved in the activation of the inflammasome (Shih et al., 2015) and a central player in triggering the inflammatory response (Savage et al., 2012; Baroja-Mazo et al., 2014; Gao et al., 2017).”
BackgroundIdentification of an ASC oligomerization inhibitor for the treatment of inflammatory diseases
Soriano‐Teruel, P. M., García‐Laínez, G., Marco-Salvador, M., Pardo, J., Arias, M. A., DeFord, C., Merfort, I., Vicent, M. J., Pelegrı́n, P., Sancho, M., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04420-1 · Cited by 70
“0 × 10(5) cells/ml in 6-well plates and transfected with ASC-YFP construct [22] according to standard procedure for Lipofectamine 2000 reagent (Invitrogen).”
BackgroundMethodZika virus induces inflammasome activation in the glial cell line U87-MG
Tricarico, P. M., Caracciolo, I., Crovella, S., & D’Agaro, P. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.01.158 · Cited by 70
“NLRP3 a cytosolic multiprotein complex, through the activation of pro-caspase-1, induces proteolysis and release of pro-inflammatory cytokines, such as IL-1b; this release could prompt pyroptotic cell death [21,22].”
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A systematic approach to autoinflammatory syndromes: a spelling booklet for the beginner
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“The release of inflammasomes in the serum of CINCA patients with low-grade somatic mosaicism might explain the severity of phenotype in at least some of these patients, providing a potential transfer inflammasome activity to wild-type cells and a disease-amplifying mechanism [52].”
BackgroundATP binding by NLRP7 is required for inflammasome activation in response to bacterial lipopeptides
Radian, A. D., Khare, S., Chu, L. H., Dorfleutner, A., & Stehlik, C. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.06.013 · Cited by 70
“, 1995), induction of pyroptosis (Fink and Cookson, 2006) and the release of alarmins and danger signals, including IL-1#, HMGB1 and inflammasome particles (Baroja-Mazo et al., 2014; Franklin et al., 2014; Groß et al., 2012; Lamkanfi et al., 2010; Willingham et al., 2009).”
BackgroundInhibition of the NLRP3 inflammasome by HSP90 inhibitors
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The role of pyroptosis in inflammatory diseases
Chai, R., Li, Y., Shui, L., Ni, L., & Zhang, A. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1173235 · Cited by 68
“In addition, wedelolactone promotes phosphorylation at the Ser/Thr site of NLRP3 and inhibits inflammasome activation and pyroptosis by activating protein kinase A (PKA) signaling (Baroja-Mazo et al., 2014).”
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“Under these conditions, release of damage-associated molecular patterns (DAMPs), including dsRNA, crystalline urea, extracellular ATP, cholesterol and degraded extracellular matrix components [7–11] can lead to activation of NLRP3 inflammasome, a key driver of inflammation that is formed after the oligomerization of N…”
BackgroundChronic Infantile Neurological Cutaneous and Articular (CINCA) syndrome: a review
Finetti, M., Omenetti, A., Federici, S., Caorsi, R., & Gattorno, M. (2016) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-016-0542-8 · Cited by 69
“cross-talking signaling potentially involved [41].”
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The ASC Speck and NLRP3 Inflammasome Function Are Spatially and Temporally Distinct
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“While exploration of this hypothesis is needed, the seminal studies of extracellular inflammasomes/specks do not appear to be contradictory (Baroja-Mazo et al., 2014; Franklin et al., 2014).”
BackgroundRegulation of the NLRP3 Inflammasome by Posttranslational Modifications
Zangiabadi, S., & Sater, A. A. A. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2100734 · Cited by 63
Dynamics of in vivo ASC speck formation
Kuri, P., Schieber, N. L., Thumberger, T., Wittbrodt, J., Schwab, Y., & Leptin, M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201703103 · Cited by 69
“…had been shown to remain as stable aggregates in the extracellular space after ASC overexpression in COS-7 cells and in the supernatant of macrophage cell cultures upon exposure to inflammasome-activating stimuli (Balci-Peynircioglu et al., 2008; Baroja-Mazo et al., 2014; Franklin et al., 2014).”
Bat ASC2 suppresses inflammasomes and ameliorates inflammatory diseases
Ahn, M., Chen, V. C.-W., Rozario, P., Ng, W. L., Kong, P. S., Sia, W. R., Kang, A. E. Z., Su, Q., Nguyen, L. H., Zhu, F., et al. (2023) · Cell · doi:10.1016/j.cell.2023.03.036 · Cited by 67
Macrophage-specific MHCII expression is regulated by a remote Ciita enhancer controlled by NFAT5
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“iBMDMs have been described (Baroja-Mazo et al., 2014) and were provided by P.”
MethodPrion-Like Polymerization in Immunity and InflammationPreprint
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Pattern recognition receptors as potential therapeutic targets in inflammatory rheumatic disease
Mullen, L., Chamberlain, G., & Sacre, S. M. (2015) · Arthritis Research & Therapy · doi:10.1186/s13075-015-0645-y · Cited by 61
“Activation of the NLRP3 inflammasome also results in pyroptosis releasing the inflammasome complex as a speck from the cell into the extracellular environment; specks can then be taken up by neighbouring cells, further triggering activation of the inflammasome in these cells [9].”
BackgroundInflammasomes as polyvalent cell death platforms
de Vasconcelos, N. M., Opdenbosch, N. V., & Lamkanfi, M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2204-3 · Cited by 65
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Bronchopulmonary dysplasia: Pathophysiology and potential anti-inflammatory therapies
Papagianis, P. C., Pillow, J. J., & Moss, T. J. M. (2018) · Paediatric Respiratory Reviews · doi:10.1016/j.prrv.2018.07.007 · Cited by 60
Hulse, J. P., & Bhaskar, K. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.805169 · Cited by 63
“This work confirmed and expanded upon similar work that showed that NLRP3 inflammasome particles are secreted extracellularly where they can continue to mature caspase-1 in the extracellular space as well as within other macrophage cells upon phagocytosis of the particle (Baroja-Mazo et al., 2014).”
BackgroundInhibiting the inflammasome: one domain at a time
Dorfleutner, A., Chu, L. H., & Stehlik, C. (2015) · Immunological Reviews · doi:10.1111/imr.12290 · Cited by 61
“A biological relevance for prion-like ASC particles was revealed, as these are present in sera of inflammatory disease patients, are phagocytized by neighboring cells and trigger polymerization of endogenous ASC without the need of inflammasome activation by a sensor (26, 27).”
Châlons, P., Amor, S., Courtaut, F., Cantos‐Villar, E., Richard, T., Auger, C., Chabert, P., Schini‐Kerth, V. B., Aires, V., & Delmas, D. (2018) · Nutrients · doi:10.3390/nu10121856 · Cited by 58
“Once formed, the NLRP3 inflammasome causes cleavage of pro-caspase-1 in active caspase-1, which in turn will cleave pro-IL-1β to IL-1β, which will then be excreted [37].”
BackgroundWang, F., Gong, S., Wang, T., Li, L., Luo, H., Wang, J., Huang, C., Zhou, H., Chen, G., Liu, Z., et al. (2020) · Theranostics · doi:10.7150/thno.40128 · Cited by 57
Zheng, R., Ruan, Y., Yan, Y., Lin, Z., Xue, N., Yan, Y., Tian, J., Yin, X., Pu, J., & Zhang, B. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s317672 · Cited by 60
Role of Pyroptosis in Inflammatory Bowel Disease (IBD): From Gasdermins to DAMPs
Zhang, S., Liang, Y., Yao, J., Li, D., & Wang, L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.833588 · Cited by 58
Li, Y., Nanayakkara, G., Sun, Y., Li, X., Wang, L., Cueto, R., Shao, Y., Fu, H., Johnson, C., Cheng, J., et al. (2017) · Journal of Hematology & Oncology · doi:10.1186/s13045-017-0406-2 · Cited by 58
The PYRIN domain-only protein POP2 inhibits inflammasome priming and activation
Ratsimandresy, R. A., Chu, L. H., Khare, S., de Almeida, L., Gangopadhyay, A., Indramohan, M., Misharin, A. V., Greaves, D. R., Perlman, H., Dorfleutner, A., et al. (2017) · Nature Communications · doi:10.1038/ncomms15556 · Cited by 64
Demirel, I., Persson, A., Brauner, A., Särndahl, E., Kruse, R. L., & Persson, K. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00081 · Cited by 57
“Scale bar: 1,000µm. can be released extracellular and by that act as a danger signal that amplifies inflammation (Baroja-Mazo et al., 2014).”
BackgroundXin, L., Che, B., Zhai, B., Luo, Q., Zhang, C., Wang, J., Wang, S., Fan, G., Liu, Z., Feng, J., et al. (2018) · Inflammation · doi:10.1007/s10753-018-0928-y · Cited by 57
Directly targeting ASC by lonidamine alleviates inflammasome-driven diseases
Chen, C., Zhou, Y., Ning, X., Li, S., Xue, D., Wei, C., Zhu, Z., Sheng, L., Lu, B., Li, Y., et al. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02682-w · Cited by 59
The crystal-induced activation of NLRP3 inflammasomes in atherosclerosis
Karasawa, T., & Takahashi, M. (2017) · Inflammation and Regeneration · doi:10.1186/s41232-017-0050-9 · Cited by 59
“The assembly of NLRP3 inflammasome components causes the formation of aggregates called speck, which are released to the extracellular space after NLRP3 inflammasome activation [35, 36].”
NLRP3 Inflammasome: A Promising Therapeutic Target for Drug-Induced Toxicity
Wei, S., Ma, W., Zhang, B., & Li, W. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.634607 · Cited by 60
“Moreover, a later stage of injury mediated by the secreted inflammatory factors (mainly IL-1β) and recruitment of inflammatory cells further contributed to toxicity (Baroja-Mazo et al., 2014).”
BackgroundKadhim, H., Deltenre, P., Martin, J.-J., & Sébire, G. (2016) · Medical Hypotheses · doi:10.1016/j.mehy.2015.11.022 · Cited by 54
Nedd8 Regulates Inflammasome-Dependent Caspase-1 Activation
Segovia, J. A., Tsai, S.-Y., Chang, T.-H., Shil, N. K., Weintraub, S. T., Short, J. D., & Bose, S. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00775-14 · Cited by 54
“Our results corroborated results from previous studies (58) that demonstrated NLRP3 inflammasome activation in BMDMs (by ATP or nigericin) triggering rapid release of p10 and p17 in the medium supernatant following cleavage of pro-caspase-1 and pro-IL-1 , respectively.”
BackgroundResultInfluentialLipinski, S., Pfeuffer, S., Arnold, P., Treitz, C., Aden, K., Ebsen, H., Falk‐Paulsen, M., Gisch, N., Fazio, A., Kuiper, J. W., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018101266 · Cited by 55
“An extracellular role of the inflammasome and its components has already been suggested (Baroja-Mazo et al , 2014; Franklin et al , 2014; Mitra et al , 2015).”
Zhao, P., Zhou, W., Zhang, Y., Li, J., Zhao, Y., Pan, L., Shen, Z., Chen, W., & Hui, J. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14972 · Cited by 54
Yu, Q., Guo, M., Zeng, W., Zeng, M., Zhang, X., Zhang, Y., Zhang, W., Jiang, X., & Yu, B. (2021) · Immunity Inflammation and Disease · doi:10.1002/iid3.581 · Cited by 52
“Recent results in inflammation research have identified the critical role of NLRP3 inflammasome in macrophages responding to chronic inflammation.(22,23) NLRP3 specific ligands such as cholesterol crystals (CC), ATP, Lipopolysaccharidepore (LPS), forming toxins (nigericin) and monosodium urate (MSU) crystals, activate…”
BackgroundBryant, C. E., Orr, S. J., Ferguson, B. J., Symmons, M. F., Boyle, J. P., & Monie, T. P. (2015) · Pharmacological Reviews · doi:10.1124/pr.114.009928 · Cited by 54
“The recent observations using electron microscopy of helical filaments formed by inflammasome components (Baroja-Mazo et al., 2014; Franklin et al., 2014; Lu et al., 2014) (Fig.”
BackgroundHsieh, C., Li, L., Rao, Y. K., Ju, T., Nai, Y., Chen, Y., & Hua, K. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27204 · Cited by 54
“It has been demonstrated that the NLRP3 inflammasome particles are released from caspase‐1 activated macrophages and act as a particulate danger signal that amplifies the inflammatory response (Baroja‐Mazo et al., 2014).”
BackgroundThe Impact of Mitochondrial Deficiencies in Neuromuscular Diseases
Cantó, J., Grau‐Junyent, J. M., & Garrabou, G. (2020) · Antioxidants · doi:10.3390/antiox9100964 · Cited by 54
“The inflammasome priming and assembly signal is induced by NF-κB, which acts downstream of TLRs and other immune receptors [142].”
BackgroundPyroptosis and Redox Balance in Kidney Diseases
Cuevas, S., & Pelegrı́n, P. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8243 · Cited by 55
Sagers, J. E., Şahin, M. İ., Moon, I. S., Ahmed, S., Stemmer-Rachamimov, A. O., Brenner, G. J., & Stanković, K. M. (2019) · Hearing Research · doi:10.1016/j.heares.2019.07.007 · Cited by 54
Mouasni, S., Gonzalez, V., Schmitt, A., Bennana, E., Guillonneau, F., Mistou, S., Avouac, J., Ea, H., Devauchelle‐Pensec, V., Gottenberg, J., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1412-9 · Cited by 55
Jämsen, E., Pajarinen, J., Kouri, V., Rahikkala, A., Goodman, S. B., Manninen, M. J., Nordström, D., Eklund, K. K., & Nurmi, K. (2020) · Acta Biomaterialia · doi:10.1016/j.actbio.2020.03.017 · Cited by 52
What are NLRP3-ASC specks? an experimental progress of 22 years of inflammasome research
Nagar, A., Bharadwaj, R., Shaikh, M. O. F., & Roy, A. G. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1188864 · Cited by 55
“of NLRP3 activation (19, 39, 40, 67, 68) and thus precedes inflammasome formation.”
BackgroundAldhamen, Y. A., Pepelyayeva, Y., Rastall, D. P. W., Seregin, S. S., Zervoudi, E., Koumantou, D., Aylsworth, C. F., Quiroga, D. M., Godbehere, S., Georgiadis, D., et al. (2015) · Journal of Innate Immunity · doi:10.1159/000368899 · Cited by 50
The alarmin interleukin-1α causes preterm birth through the NLRP3 inflammasome
Motomura, K., Romero, R. J., Garcia‐Flores, V., Leng, Y., Xu, Y., Galaz, J., Slutsky, R., Levenson, D., & Gomez‐Lopez, N. (2020) · Molecular Human Reproduction · doi:10.1093/molehr/gaaa054 · Cited by 51
“, 2018b), the adaptor protein of the inflammasome that is released upon activation (Baroja-Mazo et al., 2014; Franklin et al., 2014).”
BackgroundNotch signaling in cerebrovascular diseases (Review)
Cai, Z., Zhao, B., Deng, Y., Shangguan, S., Zhou, F., Zhou, W., Li, X., Li, Y., & Chen, G. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5641 · Cited by 50
“Apoptosis is induced by either the extrinsic or intrinsic pathways (167,168).”
The role of NLRP3 inflammasome in stroke and central poststroke pain
Li, S., Zhang, Y., Ma, S., Yi, Y., Yu, H., Pei, L., & Feng, D. (2018) · Medicine · doi:10.1097/md.0000000000011861 · Cited by 50
López‐Abente, J., Correa‐Rocha, R., & Pion, M. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00192 · Cited by 52
“The impact of extracellular ATP on the immune system is critical since its increase induces the activation of the inflammosome and subsequent release of cytokines, such as IL-1β (68, 69), in response to damage-associated molecular patterns (DAMPS) and pathogen-associated molecular patterns (PAMPS) (70).”
Background
Metadata
- Authors
- Baroja-Mazo, A., Martín-Sánchez, F., Gomez, A. I., Martínez, C. M., Amores-Iniesta, J., Compan, V., Barberà-Cremades, M., Yagüe, J., Ruiz-Ortiz, E., Antón, J., Buján, S., Couillin, I., Brough, D., Arostegui, J. I., & Pelegrín, P.
- Affiliations
- Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (ES)
- University of Manchester (GB)
- Hospital Clínic de Barcelona (ES)
- Hospital Sant Joan de Déu Barcelona (ES)
- Vall d'Hebron Hospital Universitari (ES)
- Université d'Orléans (FR)
- ORCID
- Venue
- Nature Immunology
- Published
- 2014-06-22
- Volume
- 15
- Issue
- 8
- Pages
- 738-748
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- OpenAlex
- W2143119237
- Cited by
- 790
- References
- 50
- Citations by year
- 2026: 28 · 2025: 39 · 2024: 41 · 2023: 63 · 2022: 81 · 2021: 84 · 2020: 86 · 2019: 68 · 2018: 74 · 2017: 88 · 2016: 60 · 2015: 57 · 2014: 20
- FWCI
- 30.77
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- cc-by-nc-nd
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- Hispana (publishedVersion, cc-by-nc-nd)
- Research Explorer (The University of Manchester) (submittedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Health Sciences › Medicine › Hematology › Autoimmune and Inflammatory Disorders Research
- Keywords
- NLRP3 inflammasome, caspase-1, IL-1β processing, cryopyrin-associated periodic syndromes, macrophages, autoinflammatory disease, phagocytosis
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Carrier Proteins, Cells, Cultured, Cytoskeletal Proteins, Humans, Inflammation, Macrophages, Mice, Inbred C57BL, Phagocytosis, Signal Transduction, Mice, Knockout, Caspases, Caspase 1, Apoptosis Regulatory Proteins, Mice, CARD Signaling Adaptor Proteins, Caspases, Initiator, Interleukin-1beta, Cryopyrin-Associated Periodic Syndromes, HEK293 Cells, Inflammasomes
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