The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Salmonella Infection Induces Recruitment of Caspase-8 to the Inflammasome To Modulate IL-1β Production
Open accessAbstract
Nucleotide-binding oligomerization domain–like receptors (NLRs) detect pathogens and danger-associated signals within the cell. Salmonella enterica serovar Typhimurium, an intracellular pathogen, activates caspase-1 required for the processing of the proinflammatory cytokines, pro–IL-1β and pro–IL-18, and pyroptosis. In this study, we show that Salmonella infection induces the formation of an apoptosis-associated specklike protein containing a CARD (ASC)–Caspase-8–Caspase-1 inflammasome in macrophages. Caspase-8 and caspase-1 are recruited to the ASC focus independently of one other. Salmonella infection initiates caspase-8 proteolysis in a manner dependent on NLRC4 and ASC, but not NLRP3, caspase-1 or caspase-11. Caspase-8 primarily mediates the synthesis of pro-IL-1β, but is dispensable for Salmonella-induced cell death. Overall, our findings highlight that the ASC inflammasome can recruit different members of the caspase family to induce distinct effector functions in response to Salmonella infection.
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Cites
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Gout-associated uric acid crystals activate the NALP3 inflammasome
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Cryopyrin activates the inflammasome in response to toxins and ATP
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Self-citationInnate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
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Non-canonical inflammasome activation targets caspase-11
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Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
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“Caspase-82/2 ripk32/2 BMMs were used because genetic ablation of caspase-8 in mice results in embryonic lethality, which can be rescued by ablation of RIPK3 (35, 36).”
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Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf
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RIP3 mediates the embryonic lethality of caspase-8-deficient mice
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Cited by
Inflammasomes: mechanism of action, role in disease, and therapeutics
Guo, H., Callaway, J. B., & Ting, J. P.-Y. (2015) · Nature Medicine · doi:10.1038/nm.3893 · Cited by 3,340
Wang, Y., & Kanneganti, T.-D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.038 · Cited by 545
Mitochondrial ROS promotes susceptibility to infection via gasdermin D-mediated necroptosis
Weindel, C. G., Martinez, E. L., Zhao, X., Mabry, C. J., Bell, S. L., Vail, K. J., Coleman, A. K., VanPortfliet, J. J., Zhao, B., Wagner, A. R., et al. (2022) · Cell · doi:10.1016/j.cell.2022.06.038 · Cited by 396
Inflammasome signaling and regulation of interleukin-1 family cytokines
Chan, A. H., & Schroder, K. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20190314 · Cited by 373
Microglia: Agents of the CNS Pro-Inflammatory Response
Rodríguez-Gómez, J. A., Kavanagh, E., Engskog-Vlachos, P., Engskog, M. K. R., Herrera, A. J., Espinosa-Oliva, A. M., Joseph, B., Hajji, N., Venero, J. L., & Burguillos, M. A. (2020) · Cells · doi:10.3390/cells9071717 · Cited by 365
Metadata
- Authors
- Man, S. M., Tourlomousis, P., Hopkins, L., Monie, T. P., Fitzgerald, K. A., & Bryant, C. E.
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-11
- Volume
- 191
- Issue
- 10
- Pages
- 5239-5246
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W2128008175
- Cited by
- 242
- References
- 12
- FWCI
- 7.93
- Type
- journal article
- Language
- en
- Open access
- green
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- Man, S. M., Tourlomousis, P., Hopkins, L., Monie, T. P., Fitzgerald, K. A., & Bryant, C. E. (2013). Salmonella Infection Induces Recruitment of Caspase-8 to the Inflammasome To Modulate IL-1β Production. The Journal of Immunology. https://doi.org/10.4049/jimmunol.1301581
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