Cited by 790Inflammasome and immune disordersImmune Response and InflammationAutoimmune and Inflammatory Disorders Research

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The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response

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Baroja-Mazo, Alberto, Martín-Sánchez, Fatima, Gomez, Ana I, Martínez, Carlos M, Amores-Iniesta, Joaquín, Compan, Vincent, Barberà-Cremades, Maria, Yagüe, Jordi, Ruiz-Ortiz, Estibaliz, Antón, Jordi, Buján, Segundo, Couillin, Isabelle, Brough, David, Arostegui, Juan I, Pelegrín, Pablo·2014·Nature Immunology

DOI 10.1038/ni.2919

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Abstract

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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Background
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Background
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Background
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Background
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Background
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Background
Nanobodies dismantle post‐pyroptotic ASC specks and counteract inflammation in vivo
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Background
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Background
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Background
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“In addition, oligomeric inflammasome particles can be phagocytosed by surrounding macrophages to amplify the inflammatory response (29).”
Background
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Guo, Z., Yu, S., Chen, X., Zheng, P., Hu, T., Duan, Z., Liu, X., Liu, Q., Ye, R., Zhu, W., et al. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.12.009 · Cited by 44
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“Interestingly, the opposite T cell immune-polarizing role has been recently described for NOD-like receptor P3 (NLRP3) (18), with NLRP3 acting as a DNA-binding transcriptional factor to promote an IL-4–mediated Th2 program in CD4+ T cells (19).”
Background
The zebrafish: A research model to understand the evolution of vertebrate immunity
García‐Moreno, D., Tyrkalska, S. D., Valera, A., Gómez‐Abenza, E., Pérez‐Oliva, A. B., & Mulero, V. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.04.067 · Cited by 47
Dual Role of Inflammasome Adaptor ASC in Cancer
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“It has been shown that ASC assemble and form specks that are released by dying cells, and phagocytosis of ASC specks by macrophages leads to IL-1 maturation through caspase-1 activation (Baroja-Mazo et al., 2014; Franklin et al., 2014), suggesting that extracellular ASC specks serve as danger signals (Figure 1B).”
Background
Mechanistic insights into the role of pyroptosis in rheumatoid arthritis
Chadha, S., Behl, T., BUNGAU, S. G., Kumar, A., Arora, R., Gupta, A., Uddin, M. S., Zengin, G., Aleya, L., Setia, D., et al. (2020) · Current Research in Translational Medicine · doi:10.1016/j.retram.2020.07.003 · Cited by 46
The Role of Inflammasomes in Osteoarthritis and Secondary Joint Degeneration Diseases
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“Pyroptosis-released ASC specks can propagate inflammation [28,29].”
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“Extracellular ASC specks remain active and can propagate inflammation not only by maturating pro-IL-1b in the extracellular space but also by their phagocytosis by other cells [16,17,24].”
Background
Baeckein E suppressed NLRP3 inflammasome activation through inhibiting both the priming and assembly procedure: Implications for gout therapy.
Lin, X., Wang, H., An, X., Zhang, J., Kuang, J., Hou, J., & Yan, M. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153521 · Cited by 42
Priming of NLRP3 inflammasome activation by Msn kinase MINK1 in macrophages
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ASC specks exacerbate α‑synuclein pathology via amplifying NLRP3 inflammasome activities
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“1i–k), suggesting that ASC specks may be involved in the propagation of α‐synuclein pathology [9, 45].”
Background
Inflammasomes in CNS Diseases
Albornoz, E. A., Woodruff, T. M., & Gordon, R. (2018) · Experientia supplementum · doi:10.1007/978-3-319-89390-7_3 · Cited by 42
Prion Pathogenesis in the Absence of NLRP3/ASC Inflammasomes
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“Upon activation, NLRP3 enables the formation of a multi-protein complex named NLRP3 inflammasome, which involves the polymerization of the adaptor protein ASC and culminates in the activation of caspase-1 and in the proteolytic processing and subsequent secretion of IL-1 β and IL-18 [18 – 20].”
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Electronegative LDL induces priming and inflammasome activation leading to IL-1β release in human monocytes and macrophages
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Diverse small molecules prevent macrophage lysis during pyroptosis
Loomis, W. P., den Hartigh, A. B., Cookson, B. T., & Fink, S. L. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1559-4 · Cited by 41
3D chitosan scaffolds impair NLRP3 inflammasome response in macrophages
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The Ras GTPase‐activating‐like protein IQGAP1 bridges Gasdermin D to the ESCRT system to promote IL‐1β release via exosomes
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“One tantalizing hypothesis is that extracellular inflammasome activity (Baroja-Mazo et al , 2014; Franklin et al , 2014) along with other enzymes released during inflammatory response may facilitate the rupture of exosome membrane.”
Scoparone suppresses mitophagy-mediated NLRP3 inflammasome activation in inflammatory diseases
Feng, W.-D., Wang, Y., Luo, T., Jia, X., Cheng, C., Wang, H.-J., Zhang, M., Li, Q., Wang, X., Li, Y., et al. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-01028-9 · Cited by 42
“inflammasome activation, it has been found that the functional oligomeric inflammasome components NLRP3 and ASC are secreted out of the cell together with cleaved caspase-1 and mature IL-1β, amplifying the inflammatory response by activating caspase-1 intracellularly and extracellularly [45, 46].”
Background
Pathogenic NLRP3 mutants form constitutively active inflammasomes resulting in immune-metabolic limitation of IL-1β production
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“Typically, the first clinical presentation of hyperuricemia is the development of gouty arthritis, in which the buildup of monosodium urate (MSU) crystals causes an activation of the NLRP3 inflammasome response releasing IL-1β and IL-18 in an attempt to attract macrophages to remove the birefringent crystals [2].”
Background
Citral prevents UVB-induced skin carcinogenesis in hairless mice
Kremer, J. L., Melo, G. P., Marinello, P. C., Bordini, H. P., Rossaneis, A. C., Sábio, L. R., Cecchini, R., Cecchini, A. L., Verri, W. A., Jr., & Luiz, R. C. (2019) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2019.111565 · Cited by 41
Comprehensive review of ASC structure and function in immune homeostasis and disease
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Unknown/enigmatic functions of extracellular ASC
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“In agreement with animal models, synovial membranes from RA and osteoarthritis patients presented an abundant expression of NLRP3 and ASC in tissue cells, such as macrophages, neutrophils and B cells [17,46,47]. eASC specks function in these diseases’ worth further investigation.”
BackgroundInfluential
Mitochondrial dysfunction and mitophagy: crucial players in burn trauma and wound healing
Prabhakaran, H. S., Hu, D., He, W., Luo, G., & Liou, Y. (2023) · Burns & Trauma · doi:10.1093/burnst/tkad029 · Cited by 42
The p38 Mitogen-Activated Protein Kinase Critically Regulates Human Keratinocyte Inflammasome Activation
Fenini, G., Grossi, S., Gehrke, S., Beer, H., Satoh, T. K., Contassot, E., & French, L. E. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.10.037 · Cited by 39
Innate immune responses in RNA viral infection
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The discovery of NLRP3 and its function in cryopyrin‐associated periodic syndromes and innate immunity
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“112,113 Similarly, peripheral blood mononuclear cells isolated from patients with CAPS show increased inflammasome activity with IL-1 β and IL-18 secretion compared to healthy human controls at baseline or with minimal stimulation such as low dose LPS. 114,115”
Gasdermin D mediates a fast transient release of ATP after NLRP3 inflammasome activation before ninjurin 1-induced lytic cell death
Schachter, J., Guijarro, A., Angosto-Bazarra, D., Pinilla, M., Hurtado‐Navarro, L., Meunier, É., Pérez‐Oliva, A. B., Schwarzbaum, P. J., & Pelegrín, P. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115233 · Cited by 42
Prion-like polymerization as a signaling mechanism
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“Recent studies have suggested that activated ASC polymers are secreted by cells and taken up by neighboring cells to amplify inflammasome signaling [54,55].”
Background
Purinergic signalling in autoimmunity: A role for the P2X7R in systemic lupus erythematosus?
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NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation
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Auranofin Attenuates Non-Alcoholic Fatty Liver Disease by Suppressing Lipid Accumulation and NLRP3 Inflammasome-Mediated Hepatic Inflammation In Vivo and In Vitro
Hwangbo, H., Kim, M. Y., Ji, S. Y., Kim, S. Y., Lee, H., Kim, G., Park, C., Keum, Y., Hong, S. H., Cheong, J., et al. (2020) · Antioxidants · doi:10.3390/antiox9111040 · Cited by 38
“In general, NLRP3 inflammasome is composed of NLRP3, ASC, and pro-caspase-1, which activates caspase-1 [16,50].”
Background
In vivoevidence of inflammasome activation during spontaneous labor at term
Panaitescu, B., Romero, R. J., Gomez‐Lopez, N., Xu, Y., Leng, Y., Maymon, E., Pacora, P., Erez, O., Yeo, L., Hassan, S. S., et al. (2018) · The Journal of Maternal-Fetal & Neonatal Medicine · doi:10.1080/14767058.2017.1422714 · Cited by 36
“These findings indicate that the chorioamniotic membranes possess the inflammasome machinery capable of processing active caspase-1 and mature IL-1b, which are released into the amniotic cavity.”
BackgroundInfluential
Graft versus Host Disease: From Basic Pathogenic Principles to DNA Damage Response and Cellular Senescence
Kuba, A., & Raida, L. (2018) · Mediators of Inflammation · doi:10.1155/2018/9451950 · Cited by 41
NLRP3 inflammasome is involved in nerve recovery after sciatic nerve injury
Cui, M., Liang, J., Xu, D., Zhao, L., Zhang, X., Zhang, L., Ren, S., Liu, D., Niu, X., Zang, Y., et al. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106492 · Cited by 37
Microglia in Neurodegenerative Events—An Initiator or a Significant Other?
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“This then leads to either a pyroptotic cell death and/or the excretion of exosomes [93,94], or the oligomeric NLRP3 inflammasome particles [95,96].”
Background
Soluble P2X7 Receptor Is Elevated in the Plasma of COVID-19 Patients and Correlates With Disease Severity
García-Villalba, J., Hurtado‐Navarro, L., Peñín‐Franch, A., Molina‐López, C., Martínez-Alarcón, L., Angosto-Bazarra, D., Baroja‐Mazo, A., & Pelegrín, P. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.894470 · Cited by 37
An updated view on the structure and function of PYRIN domains
Chu, L. H., Gangopadhyay, A., Dorfleutner, A., & Stehlik, C. (2014) · APOPTOSIS · doi:10.1007/s10495-014-1065-1 · Cited by 38
“patients with Chronic obstructive pulmonary disease (COPD) and pneumonia [87, 88].”
Galvanic current activates the NLRP3 inflammasome to promote Type I collagen production in tendon
Peñín‐Franch, A., García-Vidal, J. A., Martínez, C. M., Escolar‐Reina, P., Martínez-Ojeda, R. M., Gómez, A. I., Bueno, J. M., Minaya‐Muñoz, F., Valera‐Garrido, F., Medina‐Mirapeix, F., et al. (2022) · eLife · doi:10.7554/elife.73675 · Cited by 44
“…gasdermin D protein (GSDMD), and its amino-terminal fragment (GSDMD NT ) oligomerizes in the plasma membrane forming pores, thus releasing IL-1 β and IL-18 cytokines, as well as other intra-cellular content, including inflammasome oligomers ( Baroja-Mazo et al., 2014 ; Broz et al., 2020 ).”
Neutrophil NLRP3 promotes cardiac injury following acute myocardial infarction through IL-1β production, VWF release and NET deposition in the myocardium
Heger, L. A., Schommer, N., Bruggen, S. V., Sheehy, C. E., Chan, W., & Wagner, D. D. (2024) · Scientific Reports · doi:10.1038/s41598-024-64710-4 · Cited by 39
“Interestingly, recent evidence shows that key constituents of the NLRP3 inflammasome, particularly the ASC speck, possess the capacity to function as “prionoids,” triggering the activation of monocytes/macrophages and other neutrophils upon ingestion 44–46 .”
Background
Macrophages in Vascular Inflammation: Origins and Functions
Decano, J. L., Mattson, P. C., & Aikawa, M. (2016) · Current Atherosclerosis Reports · doi:10.1007/s11883-016-0585-2 · Cited by 35
Single-Molecule Fluorescence Reveals the Oligomerization and Folding Steps Driving the Prion-like Behavior of ASC
Gambin, Y., Giles, N., O’Carroll, A., Polinkovsky, M. E., Hunter, D. J. B., & Sierecki, E. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.12.013 · Cited by 36
ADP/P2Y1 aggravates inflammatory bowel disease through ERK5-mediated NLRP3 inflammasome activation
Zhang, C., Qin, J., Zhang, S., Zhang, N., Tan, B., Siwko, S. K., Zhang, Y., Wang, Q., Chen, J., Qian, M., et al. (2020) · Mucosal Immunology · doi:10.1038/s41385-020-0307-5 · Cited by 37
The role of lysosomal ion channels in lysosome dysfunction
Kendall, R. L., & Holian, A. (2021) · Inhalation Toxicology · doi:10.1080/08958378.2021.1876188 · Cited by 38
“Within the cell, the formation of the NLRP3 inflammasome acts as a scaffold for the recruitment and activation of caspase 1 and secretion of proinflammatory cytokines IL-1b/IL-18, necessary to amplify the inflammatory response (Baroja-Mazo et al. 2014; Jo et al. 2016).”
Background
Genetics of somatic auto-inflammatory disorders
Poulter, J. A., & Savic, S. (2021) · Seminars in Hematology · doi:10.1053/j.seminhematol.2021.10.001 · Cited by 36
Activation of NLRP3 inflammasome in hepatocytes after exposure to cobalt nanoparticles: the role of oxidative stress
Feng, S., Zhang, Z., Mo, Y., Tong, R., Zhong, Z., Chen, Z., He, D., Wan, R., Gao, M., Mo, Y., et al. (2020) · Toxicology in Vitro · doi:10.1016/j.tiv.2020.104967 · Cited by 35
Roles of Inflammasome in Cigarette Smoke-Related Diseases and Physiopathological Disorders: Mechanisms and Therapeutic Opportunities
Ma, Y., Long, Y., & Chen, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.720049 · Cited by 36
“(57) reported that the NLRP3 inflammasome particle was released from macrophages after inflammasome activation; thus, the decreased cellular level of NLRP3 protein may be due to the secretion of NLRP3 protein as extracellular oligomeric complexes.”
Background
Emerging Role of NLRP3 Inflammasome and Pyroptosis in Liver Transplantation
Lucas‐Ruiz, F., Peñín‐Franch, A., Pons, J. A., Ramírez, P., Pelegrı́n, P., Cuevas, S., & Baroja‐Mazo, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214396 · Cited by 35
“and enabling the entry of water into the cytosol; this induces cellular blebbing and plasma membrane rupture, leading to pyroptotic cell death [5].”
Background
Intercellular communication for innate immunity
Nguyen, T. A., Pang, K. C., & Masters, S. L. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.10.002 · Cited by 35
Colon-targeted S100A8/A9-specific peptide systems ameliorate colitis and colitis-associated colorectal cancer in mouse models
Cho, E., Mun, S., Kim, H. K., Ham, Y. S., Gil, W. J., & Yang, C. (2023) · Acta Pharmacologica Sinica · doi:10.1038/s41401-023-01188-2 · Cited by 34
Outrunning the Red Queen: bystander activation as a means of outpacing innate immune subversion by intracellular pathogens
Holmgren, A. M., McConkey, C., & Shin, S. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.36 · Cited by 35
Adding Insult on Injury: Immunogenic Role for Donor-derived Cell-free DNA?
Dholakia, S., Vlaminck, I. D., & Khush, K. K. (2020) · Transplantation · doi:10.1097/tp.0000000000003240 · Cited by 35
“Signal 2 promotes caspase-1–dependent cleavage of pro– IL-1β, which produces IL-1β and pyroptosis.(44)”
Background
Curcumin attenuates renal interstitial fibrosis by regulating autophagy and retaining mitochondrial function in unilateral ureteral obstruction rats
Lu, M., Li, H., Liu, W., Zhang, X., Li, L., & Zhou, H. (2020) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13550 · Cited by 34
Ulinastatin protects against sepsis‑induced myocardial injury by inhibiting NLRP3 inflammasome activation
Qiu, J., Xiao, X., Gao, X. J., & Zhang, Y. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12369 · Cited by 34
The molecular pathogenesis of triptolide-induced hepatotoxicity
Hu, Y., Wu, Q., Wang, Y., Zhang, H., Liu, X., Zhou, H., & Yang, T. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.979307 · Cited by 38
“Activation of the NLRP3 inflammasome releases inflammatory factors IL-1β and IL-18, which initiate an inflammatory cascade (Baroja-Mazo et al., 2014; Bruchard et al., 2015; Tsai et al., 2017).”
Background
Development of a characterised tool kit for the interrogation of NLRP3 inflammasome-dependent responses
Redondo‐Castro, E., Faust, D., Fox, S. G., Baldwin, A. G., Osborne, S. A., Haley, M., Karran, E. H., Nuthall, H. N., Atkinson, P. J., Dawson, L. A., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-24029-3 · Cited by 35
Prostaglandin E2 Activates NLRP3 Inflammasome in Endothelial Cells to Promote Diabetic Retinopathy
Wang, Y., Tao, J., & Yao, Y. (2018) · Hormone and Metabolic Research · doi:10.1055/a-0664-0699 · Cited by 33
“The NLRP3 inflammasome is usually released as a particulate danger signal, which amplifies the inflammatory response [44].”
Background
N-acetylcysteine alleviates post-resuscitation myocardial dysfunction and improves survival outcomes via partly inhibiting NLRP3 inflammasome induced-pyroptosis
He, F., Zheng, G., Hou, J., Hu, Q., Ling, Q., Wu, G., Zhao, H., Yang, J., Wang, Y., Jiang, L., et al. (2020) · Journal of Inflammation · doi:10.1186/s12950-020-00255-3 · Cited by 33
Exploring the mechanism of Yizhi Tongmai decoction in the treatment of vascular dementia through network pharmacology and molecular docking
Shi, H., Dong, C., Wang, M., Liu, R., Wang, Y., Kan, Z., Wang, L., & Si, G. (2021) · Annals of Translational Medicine · doi:10.21037/atm-20-8165 · Cited by 33
“Once formed, these can also enter into the extracellular space and further exacerbate inflammatory reactions (33,34).”
Background
Cardamonin Inhibited IL-1β Induced Injury by Inhibition of NLRP3 Inflammasome via Activating Nrf2/NQO-1 Signaling Pathway in Chondrocyte
Jiang, J., & Cai, M. (2021) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2103.03057 · Cited by 33
“6 key element in inflammatory response, was proved to be implicated in OA advancement as the inhibition of NLRP3 inflammasome mitigated OA [26-28].”
Background
Intranasal curcumin and dexamethasone combination ameliorates inflammasome (NLRP3) activation in lipopolysachharide exposed asthma exacerbations
Jaiswal, A., Dash, D., & Singh, R. (2022) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2021.115861 · Cited by 33
Rubia cordifolia L. ameliorates DSS-induced ulcerative colitis in mice through dual inhibition of NLRP3 inflammasome and IL-6/JAK2/STAT3 pathways
Qin, W., Luo, H., Yang, L., Hu, D., Jiang, S., Peng, D., Hu, J., & Liu, S. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e10314 · Cited by 33
“On the one hand, activated caspase-1 promotes the maturation and secretion of several pro-inflammatory factors, including IL-1β and IL-18; on the other hand, it triggers pyroptosis of damaged cells and clears pathogens [45, 46].”
Background
Danger signals released during cold ischemia storage activate NLRP3 inflammasome in myeloid cells and influence early allograft function in liver transplantation
Lucas‐Ruiz, F., Mateo, S. V., Jover-Aguilar, M., Alconchel, F., Martínez-Alarcón, L., de Torre‐Minguela, C., Vidal-Correoso, D., Villalba-López, F., López‐López, V., Ríos, A., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104419 · Cited by 33
Measuring NLR Oligomerization II: Detection of ASC Speck Formation by Confocal Microscopy and Immunofluorescence
Beilharz, M., Nardo, D. D., Latz, E., & Franklin, B. S. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3566-6_9 · Cited by 34
Geoepidemiology and Immunologic Features of Autoinflammatory Diseases: a Comprehensive Review
Jamilloux, Y., Bélot, A., Magnotti, F., Benezech, S., Gerfaud‐Valentin, M., Bourdonnay, E., Walzer, T., Sève, P., & Henry, T. (2017) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-017-8613-8 · Cited by 33
Growth Hormone Reprograms Macrophages toward an Anti-Inflammatory and Reparative Profile in an MAFB-Dependent Manner
Palacios, B. S., Nieto, C., Fajardo, P., de la Aleja, A. G., Andrés, N., Domínguez‐Soto, Á., Lucas, P., Cuenda, A., Rodrı́guez-Frade, J. M., Martínez‐A, C., et al. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1901330 · Cited by 32
“As innate immune cells, macrophages efficiently phagocytose pathogens and stress-inducing agents (53), with M-Mf displaying a higher phagocytic activity than GM- Mf (22).”
Background
GYY4137 alleviates sepsis-induced acute lung injury in mice by inhibiting the PDGFRβ/Akt/NF-κB/NLRP3 pathway.
Li, J.-H., Ma, J.-M., Li, M., Tao, J., Chen, J.-Y., Yao, C.-Y., & Yao, S. (2021) · Life Science · doi:10.1016/j.lfs.2021.119192 · Cited by 29
Inflammasomes and Colorectal Cancer
Shahbaz, S. K., Koushki, K., Ayati, S. H., Bland, A. R., Bezsonov, E. E., & Sahebkar, A. (2021) · Cells · doi:10.3390/cells10092172 · Cited by 33
“DAMPs recruit immune cells and sustain the inflammatory cascade in the tissue [19,20].”
Background
Neutrophil-derived extracellular vesicles promote feed-forward inflammasome signaling in cystic fibrosis airways
Forrest, O. A., Dobosh, B., Ingersoll, S. A., Rao, S., Rojas, A., Laval, J., Alvarez, J. A., Brown, M. R., Tangpricha, V., & Tirouvanziam, R. M. (2022) · Journal of Leukocyte Biology · doi:10.1002/jlb.3ab0321-149r · Cited by 32
The Extracellular IFI16 Protein Propagates Inflammation in Endothelial Cells Via p38 MAPK and NF-κB p65 Activation
Bawadekar, M., Andrea, M. D., Cigno, I. L., Baldanzi, G., Caneparo, V., Graziani, A., Landolfo, S., & Gariglio, M. (2015) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2014.0168 · Cited by 34
Induced pluripotent stem cell-derived macrophages as a platform for modelling human disease
Tiwari, S. K., Wong, W. J., Moreira, M., Pasqualini, C., & Ginhoux, F. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01081-x · Cited by 36
“These studies give invaluable mechanistic insight into the pathogenesis associated with diseases underlying somatic mosaicism 68 .”
Aluminum and Neurodegenerative Diseases
Bondy, S. C., & Campbell, A. (2017) · Advances in neurotoxicology · doi:10.1016/bs.ant.2017.07.008 · Cited by 31
“The activation of the NLRP3 inflammasome plays a crucial role in amplifying the inflammatory response (Baroja-Mazo et al., 2014).”
Background
Synthetic 4-Hydroxy Auxarconjugatin B, a Novel Autophagy Inducer, Attenuates Gouty Inflammation by Inhibiting the NLRP3 Inflammasome
Hsieh, C., Li, L.-H., Lam, Y., Fang, Z., Gan, C. H., Rao, Y. K., Chiu, H., Wong, W.-T., Ju, T., Chen, F.-H., et al. (2020) · Cells · doi:10.3390/cells9020279 · Cited by 30
“Notably, the inflammasome component ASC is released from the membrane damage macrophages upon NLRP3 inflammasome activation and amplify the inflammatory response by stimulating the surrounding cells [29].”
Background
UV-B-Induced Inflammasome Activation Can Be Prevented by Cis-Urocanic Acid in Human Corneal Epithelial Cells
Korhonen, E., Bisevac, J., Hyttinen, J. M. T., Piippo, N., Hytti, M., Kaarniranta, K., Petrovski, G., & Kauppinen, A. (2020) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.61.4.7 · Cited by 31
Role of Apoptotic Cell Clearance in Pneumonia and Inflammatory Lung Disease
Zheng, D. J., Taka, M. A., & Heit, B. (2021) · Pathogens · doi:10.3390/pathogens10020134 · Cited by 32
“Unlike other caspases, these caspases do not induce apoptosis and rather mediate the cleavage-induced secretion of the inflammatory cytokines IL-1β and IL-18 [227].”
Background
Interleukin‐1 as a pharmacological target in acute brain injury
Brough, D., Rothwell, N. J., & Allan, S. M. (2015) · Experimental Physiology · doi:10.1113/ep085135 · Cited by 31
“Another interesting feature of inflammasomes is their appearance in extracellular fluids, where they can also exert pro-inflammatory actions (Baroja-Mazo et al. 2014; Franklin et al. 2014).”
Background
Detection of ASC Speck Formation by Flow Cytometry and Chemical Cross-linking
Hoß, F., Rolfes, V., Davanso, M. R., Braga, T. T., & Franklin, B. S. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7519-8_10 · Cited by 31

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: Martínez, Carlos M
Compan, Vincent
Yagüe, Jordi
Antón, Jordi
Couillin, Isabelle
Brough, David
Pelegrín, Pablo
Venue: Nature Immunology
Publisher: Springer Science and Business Media LLC
Published: 2014-06-22
Volume: 15
Issue: 8
Pages: 738-748
ISSN: 1529-2908 (ISSN-L)
1529-2916
DOI: 10.1038/ni.2919
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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The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response

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