Programmed necrotic cell death of macrophages: Focus on pyroptosis, necroptosis, and parthanatos

Robinson, Nirmal; Ganesan, Raja; Hegedűs, Csaba; Kovács, Katalin; Kufer, Thomas A.; Virág, László

doi:10.1016/j.redox.2019.101239

Cited by 238 publications

(188 citation statements)

References 115 publications

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“…Caspase-1 and caspase-11 (gene name Casp4) can activate gasdermin D to induce pyroptosis [15,16], a form of programmed cell death that leads to the release of cytosolic contents of affected cells [55]. As IL-37 inhibits the activation of caspase-1, we subsequently investigated the effect of IL-37 on pyroptosis.…”

Section: Discussionmentioning

confidence: 99%

“…While IL-37 did not reduce LPS-induced mRNA expression of Casp1, Casp4, and Gsdmd in murine macrophages, it substantially reduced pyroptosis. Being an inflammatory form of cell death [14,55], pyroptosis has been linked to the clearance of infections [56], but also to disease progression in sepsis, vascular inflammation, and cardiovascular disease [57,58]. Therefore, the inhibition of pyroptosis by IL-37 and the corresponding reduction of the release of inflammatory mediators by affected cells can be regarded as another means by which IL-37 inhibits excessive inflammation.…”

Section: Discussionmentioning

confidence: 99%

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Parsing the IL-37-Mediated Suppression of Inflammasome Function

Rudloff

Ung

Dowling

et al. 2020

Cells

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Interleukin (IL)-37 is a member of the IL-1 family of cytokines. Although its broad anti-inflammatory properties are well described, the effects of IL-37 on inflammasome function remain poorly understood. Performing gene expression analyses, ASC oligomerization/speck assays and caspase-1 assays in bone marrow-derived macrophages (BMDM), and employing an in vivo endotoxemia model, we studied how IL-37 affects the expression and maturation of IL-1β and IL-18, inflammasome activation, and pyroptosis in detail. IL-37 inhibited IL-1β production by NLRP3 and AIM2 inflammasomes, and IL-18 production by the NLRP3 inflammasome. This inhibition was partially attributable to effects on gene expression: whereas IL-37 did not affect lipopolysaccharide (LPS)-induced mRNA expression of Il18 or inflammasome components, IL-37-transgenic BMDM displayed an up to 83% inhibition of baseline and LPS-stimulated Il1b compared to their wild-type counterparts. Importantly, we observed that IL-37 suppresses nigericin- and silica-induced ASC oligomerization/speck formation (a step in inflammasome activation and subsequent caspase-1 activation), and pyroptosis (−50%). In mice subjected to endotoxemia, IL-37 inhibited plasma IL-1β (−78% compared to wild-type animals) and IL-18 (−61%). Thus, our study adds suppression of inflammasome activity to the portfolio of anti-inflammatory pathways employed by IL-37, highlighting this cytokine as a potential tool for treating inflammasome-driven diseases.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Parsing the IL-37-Mediated Suppression of Inflammasome Function

Rudloff

Ung

Dowling

et al. 2020

Cells

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“…In addition, hydrolysis of PAR chains as well as OAADPR has been reported for ARH3 Kasamatsu et al 2011;Mashimo and Moss 2016;Fontana et al 2017), but in this case, alternative hydrolases exist in the cells. PAR-removing activity of ARH3 has been linked to the regulation of parthanatos, a special type of apoptosis (Mashimo et al 2013;Dawson et al 2017;Robinson et al 2019).…”

Section: Arh3mentioning

confidence: 99%

(ADP-ribosyl)hydrolases: structure, function, and biology

2020

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ADP-ribosylation is an intricate and versatile posttranslational modification involved in the regulation of a vast variety of cellular processes in all kingdoms of life. Its complexity derives from the varied range of different chemical linkages, including to several amino acid side chains as well as nucleic acids termini and bases, it can adopt. In this review, we provide an overview of the different families of (ADP-ribosyl)hydrolases. We discuss their molecular functions, physiological roles, and influence on human health and disease. Together, the accumulated data support the increasingly compelling view that (ADP-ribosyl)hydrolases are a vital element within ADP-ribosyl signaling pathways and they hold the potential for novel therapeutic approaches as well as a deeper understanding of ADP-ribosylation as a whole.

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“…It is well known that programmed cell death has been classified into several distinct forms, including apoptosis, necroptosis, pyroptosis and ferroptosis (Ashkenazi and Salvesen, 2014;Su et al, 2015;Robinson et al, 2019). As a relatively newly discovered programmed cell death, necroptosis is essential for many kinds of physiological and pathological processes, including embryonic development (Zhang et al, 2011;Newton et al, 2016), tissue injury (Degterev et al, 2005;Zhang T. et al, 2016), inflammation (Pasparakis and Vandenabeele, 2015;Lin et al, 2016) and host defense (Mocarski et al, 2012;Nogusa et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

TRADD Mediates RIPK1-Independent Necroptosis Induced by Tumor Necrosis Factor

Wang¹,

Chang²,

Feng³

et al. 2020

Front. Cell Dev. Biol.

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As a programmed necrotic cell death, necroptosis has the intrinsic initiators, including receptor-interacting serine/threonine-protein kinase 1 (RIPK1), RIPK3 and mixed-lineage kinase domain-like protein (MLKL), which combine to form necroptotic signaling pathway and mediate necroptosis induced by various necroptotic stimuli, such as tumor necrosis factor (TNF). Although chemical inhibition of RIPK1 blocks TNFinduced necroptosis, genetic elimination of RIPK1 does not suppress but facilitate necroptosis triggered by TNF. Moreover, RIPK3 has been reported to mediate the RIPK1-independent necroptosis, but the involved mechanism is unclear. In this study, we found that TRADD was essential for TNF-induced necroptosis in RIPK1-knockdown L929 and HT-22 cells. Mechanistic study demonstrated that TRADD bound RIPK3 to form new protein complex, which then promoted RIPK3 phosphorylation via facilitating RIPK3 oligomerization, leading to RIPK3-MLKL signaling pathway activation. Therefore, TRADD acted as a partner of RIPK3 to initiate necroptosis in RIPK1-knockdown L929 and HT-22 cells in response to TNF stimulation. In addition, TRADD was critical for the accumulation of reactive oxygen species (ROS), which contributed to RIPK1independent necroptosis triggered by TNF. Collectively, our data demonstrate that TRADD acts as the new target protein for TNF-induced RIPK3 activation and the subsequent necroptosis in a RIPK1-independent manner.

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Programmed necrotic cell death of macrophages: Focus on pyroptosis, necroptosis, and parthanatos

Cited by 238 publications

References 115 publications

Parsing the IL-37-Mediated Suppression of Inflammasome Function

Parsing the IL-37-Mediated Suppression of Inflammasome Function

(ADP-ribosyl)hydrolases: structure, function, and biology

TRADD Mediates RIPK1-Independent Necroptosis Induced by Tumor Necrosis Factor

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