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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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Interleukin‐1 Links Autoimmune and Autoinflammatory Pathophysiology in Mixed‐Pattern Psoriasis
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“Inflammasome activation is accompanied by pyroptosis, that is characterized by the activation of caspase-1 and the release of large amounts of functional oligomeric inflammasome particles containing both NLRP3 and ASC into the extracellular space to further potentiate the inflammation [2,22,32].”
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“It has been demonstrated that upon the activation of inflammasome, inflammasome components are released from macrophages, act as extracellular danger signals and amplify the inflammatory response (27).”
BackgroundVarela, M., van der Vaart, M., Groenewoud, A., & Meijer, A. H. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/514125 · Cited by 16
“ASC aggregates are stable and can trigger prolonged inflammation even when they are released to the extracellular space (Baroja-Mazo et al., 2014; Franklin et al., 2014).”
BackgroundCARD-only proteins regulate in vivo inflammasome responses and ameliorate gout
Devi, S., Indramohan, M., Jäger, E. J., Carrière, J., Chu, L. H., de Almeida, L., Greaves, D. R., Stehlik, C., & Dorfleutner, A. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112265 · Cited by 17
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“Recently, soluble forms of P2X7R and NLRP3 (sP2X7R and sNLRP3) were shown to be elevated in inflammation and sepsis, and tentatively added to the panoply of inflammatory mediators (29, 31, 32).”
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“Recently, elegant studies using CAPS mutant knockin mice revealed ongoing inflammation despite the inability to make or respond to IL-18 and IL-1 (47).”
BackgroundInfluentialAcid-dependent Interleukin-1 (IL-1) Cleavage Limits Available Pro-IL-1β for Caspase-1 Cleavage
Edye, M. E., Brough, D., & Allan, S. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.667162 · Cited by 15
“Nearly 50% of pro-IL-1 produced in response to nigericin is released from bone marrow-derived macrophages without any further cleavage (23).”
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“There are noteworthy differences between our lung results and that of other reports that need comment pertaining to ASC specks in lung (11) or blood (13, 30).”
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Role of Caspase-1 as a Biomarker of Ocular Surface Damage
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“NLRP3 inflammasome components released from pyroptotic macrophages serve as particulate danger signals that amplify the inflammatory response (24).”
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“During this process, activated caspases cleave gasdermin D (GSDMD) to generate the N-terminal domain (GSDMD-N), which forms membrane oligomeric pores that disrupt ionic homeostasis and ultimately cause cellular demise [11, 12].”
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“Key words: autoinflammatory disease, familial Mediterranean fever, MEFV, IL-18 Abbreviations: FMF, familial Mediterranean fever; IL, interleukin; NLRP3, nucleotidebinding domain and leucine-rich repeat pyrin containing protein-3.”
InfluentialHigh-sensitivity C-reactive protein mediates age-related vascular dysfunction: the Rotterdam study
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“some components in the extracellular space has been hypothesized to provide endogenous danger signals to further amplify the inflammatory response [47].”
The inflammasome in biomaterial‐driven immunomodulation
Vasconcelos, D. P., Águas, A. P., & Barbosa, J. N. (2022) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.3361 · Cited by 13
“proteins to restore tissue homeostasis, such as fibroblast growth factor (FGF)‐2 that has an important role in tissue repair and homeostasis, therefore directly associating inflammation to regeneration (Baroja‐Mazo et al., 2014; Keller et al., 2008).”
BackgroundArtificial Loading of ASC Specks with Cytosolic Antigens
Sahillioğlu, A. C., & Özören, N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134912 · Cited by 17
“Two recent studies showed that extracellular ASC specks are involved in propagation of inflammation [36,37].”
BackgroundSangare, R., Madhi, I., Kim, J.-H., & Kim, Y. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45030134 · Cited by 12
“Thus, extracellular ASC specks can directly activate caspase-1 and can be engulfed by the surrounding cells, resulting in danger signals that activate and trigger an inflammatory cascade and participate in antigen presentation [32,34,35].”
BackgroundYu, T.-G., Cha, J. S., Kim, G., Sohn, Y., Yoo, Y., Kim, U., Song, J., Cho, H., & Kim, H. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01438-6 · Cited by 13
“Following pyroptosis, inflammasome components, including caspase-1 and ASC specks, are released outside the cells, further amplifying inflammatory responses in the extracellular space [15].”
BackgroundInfluentialIFIH1 loss of function predisposes to inflammatory and SARS‐CoV ‐2‐related infectious diseases
Najm, R., Yavuz, L., Jain, R., Naofal, M. E., Ramaswamy, S., Abuhammour, W., Loney, T., Nowotny, N. R., Alsheikh-Ali, A. A. A., Tayoun, A. N. A., et al. (2024) · Scandinavian Journal of Immunology · doi:10.1111/sji.13373 · Cited by 12
“32 All patients received immunosuppressive medication such as corticosteroids.”
Inflammasomes in Cardiovascular Diseases: Current Knowledge and Future Perspectives
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Cox, L. A. (2019) · Environmental Research · doi:10.1016/j.envres.2019.109026 · Cited by 12
Inflammasome assembly: The wheels are turning
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How Microglia Manages Non-cell Autonomous Vicious Cycling of Aβ Toxicity in the Pathogenesis of AD
Seol, Y., Ki, S., Ryu, H. L., Chung, S., Lee, J.-H., & Ryu, H. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.593724 · Cited by 12
“Released ASC or ASC specks can be functionally built into NLRP3 inflammasomes of neighboring microglia and trigger the ongoing immune response via microglial activity (Baroja-Mazo et al., 2014; Franklin et al., 2014; Venegas et al., 2017; Tejera et al., 2019; Friker et al., 2020).”
BackgroundReimers, D., Vallejo-Muñoz, M., Casarejos, M. J., Jiménez‐Escrig, A., Gonzalo‐Gobernado, R., & Bazán, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168697 · Cited by 12
“In this location, they might be sensed as a danger signal by these astrocytes, which might capture them in order to remove them from the extracellular space, similarly to the described behavior of macrophages [23,48].”
BackgroundChu, C., Ran, H., Zhou, Y., Zhao, K., Zhang, Y., Fan, Y.-Y., Wu, L.-Y., Liang, L.-X., Huang, J.-W., Guo, L.-H., et al. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116453 · Cited by 12
SOHO State of the Art Update and Next Questions: Biology and Treatment of Myelodysplastic Syndromes
Sallman, D. A., Tanaka, T. N., List, A. F., & Bejar, R. L. (2017) · Clinical Lymphoma Myeloma & Leukemia · doi:10.1016/j.clml.2017.09.018 · Cited by 12
“”(31) Overall, S100A9mediated pyroptosis induces a feed-forward amplification loop that drives further pyroptosis and the production of inflammatory cytokines.(14,33) In MDS, we have recently described a common pathway in which founder somatic mutations and/or damageassociated molecular pattern signals (i.”
The respiratory health effects of geogenic (earth derived) PM 10
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“The NRLP-3 inflammasome is thought to be one of the most important particle-induced damage response pathways (Baroja-Mazo et al., 2014; McIlwain et al., 2013) and responds to changes in mitochondrial activity in response to exogenous stimuli (Tschopp, 2011).”
BackgroundIndoxyl Sulfate Mediates the Low Inducibility of the NLRP3 Inflammasome in Hemodialysis Patients
Ho, L., Wu, T.-Y., Lin, T., Liou, H., & Hung, S. (2021) · Toxins · doi:10.3390/toxins13010038 · Cited by 11
“The reduced intracellular level of ASC in our HD patients, but not in the IS-treated macrophages, could also be a result of chronic inflammation, as the ASC specks and the NLRP3 inflammasome might leak extracellularly [21,22].”
BackgroundLage, S. L., Wong, C.-S., Amaral, E. P., Sturdevant, D. E., Hsu, D. C., Rupert, A. W., Wilson, E. M. P., Qasba, S. S., Naqvi, N., Laidlaw, E., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009435 · Cited by 11
“Of note, although the inflammasome complex can be released to the extracellular milieu at the late stages of pyroptosis [35,36], we also found FLICAASC-speck monocytes within the Live/Dead gate (Fig 3B), representing cells in early stages of pyroptotic cell death.”
BackgroundJohnson, A. M., Ou, Z.-Y. A., Gordon, R., & Saminathan, H. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.106113 · Cited by 11
Association between Nod‑like receptor protein 3 inflammasome and gouty nephropathy
Zhang, Y., Sui, X., Xu, Y., Gu, F., Zhang, A., & Chen, J. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8694 · Cited by 11
“One of the most thoroughly investigated members is the intracellular pattern recognition receptor NLRP3 inflammasome complex consisting of NLRP3, ASC and caspase‐1 (27).”
BackgroundIschemic, Traumatic and Neurodegenerative Brain Inflammatory Changes
Dugue, R., & Barone, F. C. (2016) · Future Neurology · doi:10.2217/fnl.16.5 · Cited by 11
Design, synthesis, and screening of sulfonylurea-derived NLRP3 inflammasome inhibitors
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“This cell line was cultured in Dulbecco’s Modified Eagle Medium F-12 (DMEM/F-12) growth media in the presence of Geneticin G418 (2 mg/ml) to maintain mutation (Baroja-Mazo et al., 2014).”
MethodSystemic injury caused by taurocholate‑induced severe acute pancreatitis in rats
Hong, X., Wang, H., Yang, J., Lin, B., Min, Q., Liang, Y.-Z., Huang, P.-D., Zhong, Z.-Y., Guo, S., Huang, B., et al. (2022) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2022.11395 · Cited by 10
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Caspase-1 als Regulator der Autoinflammation bei rheumatischen Erkrankungen
Winkler, S., Hedrich, C. M., & Rösen‐Wolff, A. (2016) · Zeitschrift für Rheumatologie · doi:10.1007/s00393-016-0077-3 · Cited by 10
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“Similar to the type I interferons and the interferon stimulated innate genes, the induction of a strong pro-inflammatory response in macrophages is important for early inhibition of viral dissemination (Baroja-Mazo et al., 2014; Zoja et al., 1991).”
ResultInvolvement of NLRP10 in IL-1α induction of oral epithelial cells by periodontal pathogens
Lee, S.-J., & Choi, B. (2017) · Innate Immunity · doi:10.1177/1753425917722610 · Cited by 10
“Recently, oligomeric NLRP3/ ASC inflammasome particles were demonstrated to be extracellularly released and function as danger signals to activate caspase-1.(48) Active caspase-1 cleaves the Nterminal of gasdermin D, which forms pores on cellular membranes.”
BackgroundSui, Y., Zhang, Y., Dong, C., Xu, B., & Sun, X. (2019) · Brain Research · doi:10.1016/j.brainres.2019.05.022 · Cited by 11
Huang, S., Jia, R., Hu, R., Zhai, W., Jiang, S., Li, W., Wang, F.-X., & Xu, Q. (2021) · Journal of Fish Biology · doi:10.1111/jfb.14908 · Cited by 10
Supramolecular organizing centers at the interface of inflammation and neurodegeneration
Sušjan, P., Ramuta, T. Ž., Boršić, E., Orehek, S., & Hafner‐Bratkovič, I. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.940969 · Cited by 11
“In the case of inflammasomes, extracellular ASC specks were shown to seed nascent aggregates from cytosolic soluble ASC upon phagocytosis by recipient cells (388, 389).”
BackgroundThe involvement of DDX3X in compression-induced nucleus pulposus pyroptosis
Chi, S., Li, S., Xu, Z., Yang, G., Song, Y., Liao, Z., Cao, Y., & Wu, X. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.02.074 · Cited by 9
Revealing the dance of NLRP3: spatiotemporal patterns in inflammasome activation
Spector, L., & Subramanian, N. (2025) · Immunometabolism · doi:10.1097/in9.0000000000000053 · Cited by 9
Molina‐López, C., Hurtado‐Navarro, L., O'Neill, L. A. J., & Pelegrín, P. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05699-5 · Cited by 10
“Activated caspase-1 then cleaves and matures interleukin (IL)−1b and IL-18 cytokines [4–6].”
Bidirectional Interplay Between Microglia and Mast Cells
Lakatos, S., & Rosta, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157556 · Cited by 13
“Microglia Polarization: From M1 to M2 or from M2 to M1 Several lines of evidence indicate the polarization of microglia to the M1 phenotype in the pathogenesis of neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, or amyotrophic lateral sclerosis (ALS) [81–83].”
Zheng, R., Zhang, J., Han, X., Wu, Y., Yan, J., Song, P., Wang, Y., Wu, X., & Zhang, H. (2021) · Environmental Science Nano · doi:10.1039/d1en00361e · Cited by 9
Alfadul, H., Sabico, S., Ansari, M. G. A., Alnaami, A. M., Amer, O. E., Hussain, S. D., Wani, K., Khattak, M. N. K., Clerici, M., & Al‐Daghri, N. M. (2023) · Biomedicines · doi:10.3390/biomedicines11051315 · Cited by 9
“The caspase-1 secretome consists of the well-analyzed IL-18 and IL-1β, plus the proteins that are not immediate protease substrates, such as IL-1α [10].”
BackgroundInflammatory/Noninflammatory Adjuvants and Nanotechnology—The Secret to Vaccine Design
Wilson, K., Xiang, S. D., & Plebanski, M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-323-39981-4.00006-3 · Cited by 9
Kaneko, J., Okinaga, T., Ariyoshi, W., Hikiji, H., Fujii, S., Iwanaga, K., Tominaga, K., & Nishihara, T. (2018) · Cell Biology International · doi:10.1002/cbin.11058 · Cited by 9
How to prescribe a genetic test for the diagnosis of autoinflammatory diseases?
Rowczenio, D. M., & Lachmann, H. J. (2019) · La Presse Médicale · doi:10.1016/j.lpm.2018.08.015 · Cited by 9
Role of Inflammasome Activation in Systemic Lupus Erythematosus: Are Innate Immune Cells Activated?
Pérez-Alamino, R., Cuchacovich, R., Espinoza, L. R., Porretta, C. P., & Zea, A. H. (2020) · Reumatología Clínica · doi:10.1016/j.reuma.2019.10.007 · Cited by 9
Cui, C., Liu, Q., Duan, B., Liu, X., Wei, H., & Peng, J. (2022) · Food & Function · doi:10.1039/d1fo03891e · Cited by 9
Induced Pluripotent Stem Cell-Derived Monocytes/Macrophages in Autoinflammatory Diseases
Tanaka, T., Shiba, T., Honda, Y., Izawa, K., Yasumi, T., Saito, M. K., & Nishikomori, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.870535 · Cited by 9
“used patient-derived MDMs to show that upon activation of caspase-1, oligomeric NLRP3 inflammasome particles are released from activated macrophages and phagocytosed by surrounding macrophages, leading to further activation of caspase-1 (43).”
Burn the house, save the day: pyroptosis in pathogen restriction
Boucher, D., Chen, K. W., & Schroder, K. (2015) · Inflammasome · doi:10.1515/infl-2015-0001 · Cited by 9
Kot, A., Koszewska, D., Ochman, B., & Świętochowska, E. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46120826 · Cited by 9
Inflammasomes in Alzheimer’s Progression: Nrf2 as a Preventive Target
López-Hernández, R., de la Torre-Álamo, M. M., García-Bueno, B., Baroja‐Mazo, A., Fenoy, F. J., & Cuevas, S. (2025) · Antioxidants · doi:10.3390/antiox14020121 · Cited by 9
IC100 blocks inflammasome activation induced by α-synuclein aggregates and ASC specks
Cyr, B. S., Vontell, R., Hadad, R., Vaccari, J. P. D. R., & Keane, R. W. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-00963-8 · Cited by 11
Zhang, S., Feng, C., Yu, N., Fang, R., Zhang, Y., Chen, S., Cao, L., & Zhang, J. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103877 · Cited by 8
Mitochondria in pyroptosis: Mechanisms and implications
Eldakhakhny, B. M., Abdulaal, W. H., Khan, J., Ajoolabady, A., Praticò, D., Bahijri, S., Tuomilehto, J. O., Borai, A., Kim, B., & Ren, J. (2025) · Molecular Immunology · doi:10.1016/j.molimm.2025.12.002 · Cited by 9
Alendronate augments lipid A‑induced IL‑1β release by ASC‑deficient RAW264 cells via AP‑1 activation
Watanabe, N., Tamai, R., & Kiyoura, Y. (2023) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2023.12276 · Cited by 8
“ASC is a small molecule that constitutes an inflammasome with nucleotide‑binding oligomerization domain (NOD)‑like receptor and caspase‑1 (15).”
Malhotra, M., Chotaliya, D., Debnath, M., Patel, R. K., & Kulkarni, A. A. (2024) · Biomaterials Science · doi:10.1039/d4bm00580e · Cited by 8
The NLRC4 inflammasome: The pieces of the puzzle are falling into place
Hafner‐Bratkovič, I. (2017) · Inflammasome · doi:10.1515/infl-2017-0002 · Cited by 10
No shortcuts: new findings reinforce why nuance is the rule in genetic autoinflammatory syndromes
Tsoukas, P., & Canna, S. (2017) · Current Opinion in Rheumatology · doi:10.1097/bor.0000000000000422 · Cited by 8
Wang, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.613729 · Cited by 8
Yuan, W., Wu, J., Zhang, Q., Liang, Y., Zhang, M., Qin, H., & Li, C. (2021) · Acta Cirúrgica Brasileira · doi:10.1590/acb360405 · Cited by 8
Hua, K., Hsu, H.-T., Huang, M.-S., Chiu, H., Wong, W.-T., Peng, C.-H., Lin, Y.-B., Chen, A., Wang, C.-C., Hsu, C.-H., et al. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s454221 · Cited by 7
“23 We observed that N. gonorrhoeae infection leads to the extracellular release of NLRP3 and ASC, and honokiol reduces the extracellular release of NLRP3 (Figure 2C) and ASC (Figure 2D) in N. gonorrhoeae -infected macrophages.”
BackgroundDieteren, S., Franz, N., Köhler, K., Nowak, A. J., Ehnert, S., Surov, A., Krüger, M., Marzi, İ., Wagner, N., & Relja, B. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.562904 · Cited by 7
“Here, notably pyroptosis, a specific form of inflammasome- and inflammationinduced cell death can amplify the inflammatory response (58).”
BackgroundHuang, W., Kraynak, C. A., Bender, E. C., Farrar, R. P., & Suggs, L. J. (2022) · Cytotherapy · doi:10.1016/j.jcyt.2022.11.010 · Cited by 7
Jia, X., Ju, J., Li, Z., Peng, X., Wang, J., & Gao, F. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176428 · Cited by 7
Decoding Cell Death: From a Veritable Library of Babel toVade Mecum?
Hughes, L. D., Wang, Y., Meli, A. P., Rothlin, C. V., & Ghosh, S. (2021) · Annual Review of Immunology · doi:10.1146/annurev-immunol-102819-072601 · Cited by 8
ASC nanobodies to counteract the consequences of inflammasome activation
Adriouch, S., & Pelegrín, P. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202216087 · Cited by 6
“…diseases, such as chronic obstructive pulmonary disease, cryopyrin-associated periodic syndromes, sepsis, Alzheimer’s disease, nonalcoholic fatty liver disease and liver fibrosis (Baroja-Mazo et al, 2014; Franklin et al, 2014; Venegas et al, 2017; Mart ınez-Garc ıa et al, 2019; Gaul et al, 2020).”
BackgroundShyfrin, S. R., Ferren, M., Perrin‐Cocon, L., Espi, M., Charmetant, X., Brailly, M., Décimo, D., Iampietro, M., Canus, L., Horvat, B., et al. (2022) · Journal of Tissue Engineering · doi:10.1177/20417314221122130 · Cited by 5
Purinergic Signaling Within the Tumor Microenvironment
Draganov, D., & Lee, P. P. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-47189-7_5 · Cited by 7
Jenster, L., Ribeiro, L. S., Franklin, B. S., & Bertheloot, D. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3350-2_5 · Cited by 6
Pyroptosis leads to loss of centrosomal integrity in macrophages
Bai, S., Martín‐Sánchez, F., Brough, D., & López‐Castejón, G. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02093-1 · Cited by 8
Li, S., Gong, W.-L., Liu, L., Shao, B., Jiang, S., Li, H., Song, Y., Han, G., & Zhang, Z. (2025) · Food and Chemical Toxicology · doi:10.1016/j.fct.2025.115520 · Cited by 6
Gomes, S. M., Aróstegui, J. I., Mensa‐Vilaró, A., Omoyinmi, E., Hong, Y., McCreary, D., Rowczenio, D. M., Hawkins, P. N., & Brogan, P. A. (2025) · Frontiers in Pediatrics · doi:10.3389/fped.2025.1598748 · Cited by 6
Huang, J., Zhuang, W.-H., Lin, Y., Xu, J., Zhang, Y., Li, J., Huang, M., Xie, C., & Xu, R. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03590-5 · Cited by 7
“Caspase-1 also cleaves gasdermin D (GSDMD), forming membrane pores that trigger pyroptosis and amplify inflammation [14].”
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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