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. 2021 Sep 14;11(9):152. doi: 10.1038/s41408-021-00547-8

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — MDSCs and NLRP3 are activated when DAMPS such as S100A8/S100A9 bind to CD33 and TLR4 receptors, respectively. Activated redox-sensitive NOD-like receptor protein 3 (NLRP3) recruits and causes polymerization of adapter apoptosis-associated speck-like protein containing a caspase-recruitment domain (ASC) proteins to form a complex termed as the inflammasome. This complex serves as a platform for recruitment and autocatalysis of pro-caspase 1 to give rise to active Caspase 1 and thereafter IL-18 and IL-1β from their precursors. Together with heightened ROS level, these cytokines add to the proinflammatory milieu of the cell. This process is followed by the release of proinflammatory cytokines in the cytosol via a lytic cell death called pyroptosis.