Gasdermin D as a cellular switch to orientate immune responses via IL-33 or IL-1β

Chauvin, Camille; Retnakumar, Sruthi Vijaya; Bayry, Jagadeesh

doi:10.1038/s41423-022-00950-6

Cited by 3 publications

(2 citation statements)

References 13 publications

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“…Moreover, emodin inhibits NLRP3 inflammasome‐mediated pyroptosis to alleviate lung injury 40 . Camille et al suggest the context‐dependent role of GSDMD in the release of IL‐1β 41 . The current study revealed that LIRI in vivo and OGD/R in vitro both elevated levels of GSDMD‐N, caspase‐1 p20 and IL‐1β, which were decreased following emodin administration, suggesting that emodin attenuated the endothelial pyroptosis.…”

Section: Discussionsupporting

confidence: 52%

Emodin alleviates lung ischemia–reperfusion injury by suppressing gasdermin D‐mediated pyroptosis in rats

Jin¹,

Zhou³

et al. 2023

Clinical Respiratory J

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Background Pyroptosis refers to programmed cell death associated with inflammation. Emodin has been reported to alleviate lung injuries caused by various pathological processes and attenuate ischemia–reperfusion (I/R) injuries in diverse tissues. Methods Lewis rats were assigned into the sham, the I/R, and the I/R + emodin groups. Emodin and phosphate‐buffered saline were intraperitoneally injected into rats of the emodin group and I/R group for 30 min, respectively. These rats were then subjected to left thoracotomy followed by 90‐min clamping of the left hilum and 120‐min reperfusion. Sham‐operated rats underwent 210‐min ventilation. Lung functions, histological changes, lung edema, and cytokine levels were assessed. Protein levels were measured by western blotting. Immunofluorescence staining was conducted to evaluate pyroptosis. Results Emodin alleviated the I/R‐induced lung dysfunction, lung damages, and inflammation. Protective effects of emodin against I/R‐mediated endothelial pyroptosis was observed in vivo and in vitro. Mechanistically, emodin inactivated the TLR4/MyD88/NF‐κB/NLRP3 pathway. Conclusion Emodin attenuates lung ischemia–reperfusion injury by inhibiting GSDMD‐mediated pyroptosis in rats.

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Section: Discussionsupporting

confidence: 52%

Emodin alleviates lung ischemia–reperfusion injury by suppressing gasdermin D‐mediated pyroptosis in rats

Jin¹,

Zhou³

et al. 2023

Clinical Respiratory J

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“…Of interest is the fact that most of these proteins are released in a way of non-classical and non-vesicular release, which is distinct from exocytosis, as seen in neurotransmitters and peptide hormones. Current studies have revealed that some of representative DAMPs/alarmins use the release modes via gasdermin D (GSDMD) and mixed-lineage kinase domain-like pseudokinase (MLKL) pores [ 9 , 10 ]. In the present review, the author introduces a new mechanism, the annexin A2 (ANXA2) flop-out mediated release of prothymosin α, a neuroprotective member of DAMPs/alarmins [ 11 ], as well as GSDMD or MLKL pore-mediated non-classical and non-vesicular release.…”

Section: Introductionmentioning

confidence: 99%

Non-Vesicular Release of Alarmin Prothymosin α Complex Associated with Annexin-2 Flop-Out

Ueda

2023

Cells

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Nuclear protein prothymosin α (ProTα) is a unique member of damage-associated molecular patterns (DAMPs)/alarmins. ProTα prevents neuronal necrosis by causing a cell death mode switch in serum-starving or ischemic/reperfusion models in vitro and in vivo. Underlying receptor mechanisms include Toll-like receptor 4 (TLR4) and Gi-coupled receptor. Recent studies have revealed that the mode of the fatal stress-induced extracellular release of nuclear ProTα from cortical neurons in primary cultures, astrocytes and C6 glioma cells has two steps: ATP loss-induced nuclear release and the Ca2+-mediated formation of a multiple protein complex and its extracellular release. Under the serum-starving condition, ProTα is diffused from the nucleus throughout the cell due to the ATP loss-induced impairment of importin α–mediated nuclear transport. Subsequent mechanisms are all Ca2+-dependent. They include the formation of a protein complex with ProTα, S100A13, p40 Syt-1 and Annexin A2 (ANXA2); the fusion of the protein complex to the plasma membrane via p40 Syt-1–Stx-1 interaction; and TMEM16F scramblase-mediated ANXA2 flop-out. Subsequently, the protein complex is extracellularly released, leaving ANXA2 on the outer cell surface. The ANXA2 is then flipped in by a force of ATP8A2 activity, and the non-vesicular release of protein complex is repeated. Thus, the ANXA2 flop-out could play key roles in a new type of non-vesicular and non-classical release for DAMPs/alarmins, which is distinct from the modes conducted via gasdermin D or mixed-lineage kinase domain-like pseudokinase pores.

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Pharmacological targets at the lysosomal autophagy–NLRP3 inflammasome crossroads

Bonam,

Mastrippolito,

Georgel

et al. 2024

Trends in Pharmacological Sciences

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Gasdermin D as a cellular switch to orientate immune responses via IL-33 or IL-1β

Cited by 3 publications

References 13 publications

Emodin alleviates lung ischemia–reperfusion injury by suppressing gasdermin D‐mediated pyroptosis in rats

Emodin alleviates lung ischemia–reperfusion injury by suppressing gasdermin D‐mediated pyroptosis in rats

Non-Vesicular Release of Alarmin Prothymosin α Complex Associated with Annexin-2 Flop-Out

Pharmacological targets at the lysosomal autophagy–NLRP3 inflammasome crossroads

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