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Review
. 2019 Sep 12;20(18):4508.
doi: 10.3390/ijms20184508.

Heat Shock Proteins and Inflammasomes

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Free PMC article
Review

Heat Shock Proteins and Inflammasomes

Pierre Martine et al. Int J Mol Sci. .
Free PMC article

Abstract

Heat shock proteins (HSP) regulate inflammation in many physiological contexts. However, inflammation is a broad process, involving numerous cytokines produced by different molecular pathways with multiple functions. In this review, we focused on the particular role of HSP on the inflammasomes intracellular platforms activated by danger signals and that enable activation of inflammatory caspases, mainly caspase-1, leading to the production of the pro-inflammatory cytokine IL-1β. Interestingly, some members of the HSP family favor inflammasomes activation whereas others inhibit it, suggesting that HSP modulators for therapeutic purposes, must be carefully chosen.

Keywords: IL-1β; caspase-1; heat shock proteins; inflammasomes.

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
HSP70 (Heat Shock Protein 70) expression regulates NLRP3 (NOD-leucine rich repeat and pyrin containing protein 3) inflammasome activation. Left panel: HSP70 deficiency leads to an overactivation of NLRP3 inflammasome and caspase-1 and to an increased secretion of IL (interleukin)-1β. Middle panel: In physiologic conditions, NLRP3 inflammasome activation and IL-1β secretion are regulated. Right panel: HSP70 overexpression (artificially or through a heat shock) leads to the continued interaction between HSP70 and NLRP3, preventing the interaction between NLRP3 and ASC (Apoptosis associated Speck-like protein containing a CARD domain) and the subsequent caspase-1 activation and IL-1β secretion.

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