NLRP3 regulates macrophage M2 polarization through up-regulation of IL-4 in asthma

2018 ◽  
Vol 475 (12) ◽  
pp. 1995-2008 ◽  
Author(s):  
Ying Liu ◽  
Xin Gao ◽  
Yi Miao ◽  
Yuanyuan Wang ◽  
Huan Wang ◽  
...  
Keyword(s):  
Nlrp3 Inflammasome ◽  
Inflammatory Diseases ◽  
Allergic Inflammation ◽  
Lavage Fluid ◽  
Interferon Γ ◽  
Receptor Protein ◽  
Loss Of Function ◽  
Caspase 1 ◽  
M2 Polarization ◽  
Factor Α

Activation of nucleotide-binding oligomerization domain-like receptor protein 3 (NLRP3) inflammasome received substantial attention recently in inflammatory diseases. Macrophages contribute to allergic inflammation in asthma. The present study was aimed to investigate the effect of NLRP3 inflammasome on the polarization of macrophages. We utilized human primary monocytes and monocyte-derived macrophages to study the expression of NLRP3 inflammasome components (NLRP3, apoptosis-associated specklike protein, and caspase-1) and its downstream cytokine interleukin-1β (IL-1β). By gain- or loss-of-function assays, we next explored the effects of NLRP3 inflammasome on M1/M2 polarization and secretion of IL-4, interferon-γ, tumor necrosis factor-α, and IL-1β. The results showed increased numbers of M2 cells in asthma. And NLRP3 inflammasome was activated and involved in the inflammation of asthma. Furthermore, silence of NLRP3 down-regulated IL-4 secretion and up-regulated M1/M2. In contrast, overexpression of NLRP3 increased IL-4 and decreased M1/M2. As expected, IL-4 was involved in NLRP3-mediated down-regulation of Ml/M2 ratio. Moreover, NLRP3 interacted with IRF4 and was required for optimal IRF4-dependent IL-4 transcription. Subsequently, deficiency of NLRP3 in ovalbumin-induced allergic asthmatic mice impaired lung inflammation and up-regulated M1/M2, and diminished IL-4 in bronchoalveolar lavage fluid. Collectively, we demonstrated here that activation of NLRP3 was engaged in the promotion of asthma. NLRP3, but not the inflammasome adaptor ASC or caspase-1, promoted the polarization of M2 macrophages through up-regulating the expression of IL-4, thereby contributing to its regulation of asthma.

scholarly journals Distinct expression profile and histological distribution of NLRP3 inflammasome components in the tissues of Hainan black goat suggest a site-specific role in the inflammatory response

2017 ◽  
Vol 65 (3) ◽  
pp. 402-416 ◽  
Author(s):  
Kaizhao Zhang ◽  
Pan Tao ◽  
Jianxin Liu ◽  
Qingnan Wang ◽  
Shikun Ge ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Nlrp3 Inflammasome ◽  
Cortical Neurons ◽  
Inflammatory Diseases ◽  
Polyclonal Antibodies ◽  
Receptor Protein ◽  
Mesenteric Lymph Nodes ◽  
Specific Expression ◽  
Caspase 1 ◽  
Black Goat

The NOD-like receptor protein 3 (NLRP3) inflammasome comprised of NLRP3, ASC and caspase-1 plays an important role in the inflammatory and innate immune response. However, little is known about the expression pattern and histological distribution of these genes in goat. Here, we first cloned the fulllength cDNAs of the NLRP3, ASC and caspase-1 genes of Hainan black goat and produced their polyclonal antibodies. Tissue-specific expression and histological distribution of these genes were analysed. Phylogenetic analysis revealed that these three goat genes had high homology with Bos taurus genes and low homology with avian or fish genes. After immunisations with these recombinant Histagged proteins, the titres of antiserum were higher than 1:1024 and purified IgG was obtained. These three genes were expressed in all examined tissues, the mRNA expression level of NLRP3 and caspase-1 was most abundant in the spleen and mesenteric lymph nodes (MLNs), while ASC was primary expressed in the liver, spleen and kidney. The histological distribution of NLRP3, ASC and caspase-1 was detected in myocardial cells, hepatocytes, focal lymphocytes, bronchiolar epithelial cells, renal tubular epithelial cells, cortical neurons and endothelial cells of the germinal centres in the MLNs. These results will be helpful in further investigations into the function of the NLRP3 inflammasome and in elucidating its role in caprine inflammatory diseases.

scholarly journals Structural Moieties Required for Cinnamaldehyde-Related Compounds to Inhibit Canonical IL-1β Secretion

Molecules ◽  
2018 ◽  
Vol 23 (12) ◽  
pp. 3241 ◽  
Author(s):  
Su-Chen Ho ◽  
Yi-Huang Chang ◽  
Ku-Shang Chang
Keyword(s):  
Nlrp3 Inflammasome ◽  
Functional Group ◽  
Inflammatory Diseases ◽  
Receptor Protein ◽  
Side Chain ◽  
Activated Macrophages ◽  
Inhibitory Effects ◽  
Chronic Inflammatory Diseases ◽  
Caspase 1 ◽  
Related Compounds

Suppressing canonical NOD-like receptor protein 3 (NLRP3) inflammasome-mediated interleukin (IL)-1β secretion is a reliable strategy for the development of nutraceutical to prevent chronic inflammatory diseases. This study aimed to find out the functional group responsible for the inhibitory effects of cinnamaldehyde-related compounds on the canonical IL-1β secretion. To address this, the suppressing capacities of six cinnamaldehyde-related compounds were evaluated and compared by using the lipopolysaccharide (LPS)-primed and adenosine 5′-triphosphate (ATP)-activated macrophages. At concentrations of 25~100 μM, cinnamaldehyde and 2-methoxy cinnamaldehyde dose-dependently inhibited IL-1β secretion. In contrast, cinnamic acid, cinnamyl acetate, cinnamyl alcohol and α-methyl cinnamaldehyde did not exert any inhibition. Furthermore, cinnamaldehyde and 2-methoxy cinnamaldehyde diminished expressions of NLRP3 and pro-IL-1β. Meanwhile, cinnamaldehyde and 2-methoxy cinnamaldehyde prevented the ATP-induced reduction of cytosolic pro-caspase-1 and increase of secreted caspase-1. In conclusion, for cinnamaldehyde-related compounds to suppress NLRP3 inflammasome-mediated IL-1β secretion, the propenal group of the side chain was essential, while the substituted group of the aromatic ring played a modifying role. Cinnamaldehyde and 2-methoxy cinnamaldehyde exerted dual abilities to inhibit canonical IL-1β secretion at both stages of priming and activation. Therefore, there might be potential to serve as complementary supplements for the prevention of chronic inflammatory diseases.

scholarly journals Inflammasomes and Fibrosis

2021 ◽  
Vol 12 ◽  
Author(s):  
Wen-Juan Zhang ◽  
Shu-Juan Chen ◽  
Shun-Chang Zhou ◽  
Su-Zhen Wu ◽  
Hui Wang
Keyword(s):  
Nlrp3 Inflammasome ◽  
Inflammatory Diseases ◽  
Innate Immune ◽  
Receptor Protein ◽  
Activation Process ◽  
Common Pathway ◽  
Classical Activation ◽  
Activation Pathway ◽  
Caspase 1

Fibrosis is the final common pathway of inflammatory diseases in various organs. The inflammasomes play an important role in the progression of fibrosis as innate immune receptors. There are four main members of the inflammasomes, such as NOD-like receptor protein 1 (NLRP1), NOD-like receptor protein 3 (NLRP3), NOD-like receptor C4 (NLRC4), and absent in melanoma 2 (AIM2), among which NLRP3 inflammasome is the most studied. NLRP3 inflammasome is typically composed of NLRP3, ASC and pro-caspase-1. The activation of inflammasome involves both “classical” and “non-classical” pathways and the former pathway is better understood. The “classical” activation pathway of inflammasome is that the backbone protein is activated by endogenous/exogenous stimulation, leading to inflammasome assembly. After the formation of “classic” inflammasome, pro-caspase-1 could self-activate. Caspase-1 cleaves cytokine precursors into mature cytokines, which are secreted extracellularly. At present, the “non-classical” activation pathway of inflammasome has not formed a unified model for activation process. This article reviews the role of NLRP1, NLRP3, NLRC4, AIM2 inflammasome, Caspase-1, IL-1β, IL-18 and IL-33 in the fibrogenesis.

scholarly journals Hispidulin Inhibits Mast Cell-Mediated Allergic Inflammation through Down-Regulation of Histamine Release and Inflammatory Cytokines

Molecules ◽  
2019 ◽  
Vol 24 (11) ◽  
pp. 2131 ◽  
Author(s):  
Dong Eun Kim ◽  
Kyoung-jin Min ◽  
Min-Jong Kim ◽  
Sang-Hyun Kim ◽  
Taeg Kyu Kwon
Keyword(s):  
Mast Cells ◽  
Inflammatory Cytokines ◽  
Immunoglobulin E ◽  
Inflammatory Diseases ◽  
Allergic Inflammation ◽  
Interleukin 4 ◽  
Type I ◽  
Ige Mediated ◽  
Factor Α ◽  
Jnk Activation

Hispidulin (4′,5,7-trihydroxy-6-methoxyflavone) is a natural compound derived from traditional Chinese medicinal herbs, and it is known to have an anti-inflammatory effect. Here, we investigated the effect of hispidulin on the immunoglobulin E (IgE)-mediated allergic responses in rat basophilic leukemia (RBL)-2H3 mast cells. When RBL-2H3 cells were sensitized with anti-dinitrophenyl (anti-DNP) IgE and subsequently stimulated with DNP-human serum albumin (HSA), histamine and β-hexosaminidase were released from the cells by degranulation of activated mast cells. However, pretreatment with hispidulin before the stimulation of DNP-HSA markedly attenuated release of both in anti-DNP IgE-sensitized cells. Furthermore, we investigated whether hispidulin inhibits anti-DNP IgE and DNP-HSA-induced passive cutaneous anaphylaxis (PCA), as an animal model for Type I allergies. Hispidulin markedly decreased the PCA reaction and allergic edema of ears in mice. In addition, activated RBL-2H3 cells induced the expression of inflammatory cytokines (tumor necrosis factor-α and interleukin-4), which are critical for the pathogenesis of allergic disease, through the activation of c-Jun N-terminal kinase (JNK). Inhibition of JNK activation by hispidulin treatment reduced the induction of cytokine expression in the activated mast cells. Our results indicate that hispidulin might be a possible therapeutic candidate for allergic inflammatory diseases through the suppression of degranulation and inflammatory cytokines expression.

scholarly journals Inhibitory Effects of the Two Novel TSPO Ligands 2-Cl-MGV-1 and MGV-1 on LPS-induced Microglial Activation

Cells ◽  
2019 ◽  
Vol 8 (5) ◽  
pp. 486 ◽  
Author(s):  
Sheelu Monga ◽  
Rafi Nagler ◽  
Rula Amara ◽  
Abraham Weizman ◽  
Moshe Gavish
Keyword(s):  
Inflammatory Responses ◽  
Inflammatory Diseases ◽  
Cell Metabolism ◽  
Interferon Γ ◽  
Translocator Protein ◽  
Ros Generation ◽  
Protective Effects ◽  
Neuronal Progenitor ◽  
Cytokines And Chemokines ◽  
Factor Α

The 18 kDa translocator protein (TSPO) ligands 2-Cl-MGV-1 and MGV-1 can attenuate cell death of astrocyte-like cells (U118MG) and induce differentiation of neuronal progenitor cells (PC-12). Lipopolysaccharide (LPS) is a bacterial membrane endotoxin that activates cellular inflammatory pathways by releasing pro-inflammatory molecules, including cytokines and chemokines. The aim of the present study was to assess the immuno-modulatory effect of TSPO ligands in activated microglial cells. We demonstrated that the TSPO ligands 2-Cl-MGV-1 and MGV-1 can prevent LPS-induced activation of microglia (BV-2 cell line). Co-treatment of LPS (100 ng/mL) with these TSPO ligands (final concentration- 25 µM) reduces significantly the LPS-induced release of interleukin-6 (IL-6) from 16.9-fold to 2.5-fold, IL-β from 8.3-fold to 1.6-fold, interferon-γ from 16.0-fold to 2.2-fold, and tumor necrosis factor-α from 16.4-fold to 1.8-fold. This anti-inflammatory activity seems to be achieved by inhibition of NF-κB p65 activation. Assessment of initiation of ROS generation and cell metabolism shows significant protective effects of these two novel TSPO ligands. The IL-10 and IL-13 levels were not affected by any of the TSPO ligands. Thus, it appears that the ligands suppress the LPS-induced activation of some inflammatory responses of microglia. Such immunomodulatory effects may be relevant to the pharmacotherapy of neuro-inflammatory diseases.

scholarly journals OLT1177, a β-sulfonyl nitrile compound, safe in humans, inhibits the NLRP3 inflammasome and reverses the metabolic cost of inflammation

2018 ◽  
Vol 115 (7) ◽  
pp. E1530-E1539 ◽  
Author(s):  
Carlo Marchetti ◽  
Benjamin Swartzwelter ◽  
Fabia Gamboni ◽  
Charles P. Neff ◽  
Katrin Richter ◽  
...  
Keyword(s):  
Human Blood ◽  
Nlrp3 Inflammasome ◽  
Inflammatory Diseases ◽  
Plasma Concentrations ◽  
Metabolic Cost ◽  
Inflammasome Activation ◽  
Potassium Efflux ◽  
Caspase 1 ◽  
Healthy Humans

Activation of the NLRP3 inflammasome induces maturation of IL-1β and IL-18, both validated targets for treating acute and chronic inflammatory diseases. Here, we demonstrate that OLT1177, an orally active β-sulfonyl nitrile molecule, inhibits activation of the NLRP3 inflammasome. In vitro, nanomolar concentrations of OLT1177 reduced IL-1β and IL-18 release following canonical and noncanonical NLRP3 inflammasome activation. The molecule showed no effect on the NLRC4 and AIM2 inflammasomes, suggesting specificity for NLRP3. In LPS-stimulated human blood-derived macrophages, OLT1177 decreased IL-1β levels by 60% and IL-18 by 70% at concentrations 100-fold lower in vitro than plasma concentrations safely reached in humans. OLT1177 also reduced IL-1β release and caspase-1 activity in freshly obtained human blood neutrophils. In monocytes isolated from patients with cryopyrin-associated periodic syndrome (CAPS), OLT1177 inhibited LPS-induced IL-1β release by 84% and 36%. Immunoprecipitation and FRET analysis demonstrated that OLT1177 prevented NLRP3-ASC, as well as NLRP3-caspase-1 interaction, thus inhibiting NLRP3 inflammasome oligomerization. In a cell-free assay, OLT1177 reduced ATPase activity of recombinant NLRP3, suggesting direct targeting of NLRP3. Mechanistically, OLT1177 did not affect potassium efflux, gene expression, or synthesis of the IL-1β precursor. Steady-state levels of phosphorylated NF-κB and IkB kinase were significantly lowered in spleen cells from OLT1177-treated mice. We observed reduced IL-1β content in tissue homogenates, limited oxidative stress, and increased muscle oxidative metabolism in OLT1177-treated mice challenged with LPS. Healthy humans receiving 1,000 mg of OLT1177 daily for 8 d exhibited neither adverse effects nor biochemical or hematological changes.

scholarly journals NLRP3 inflammasome activation contributes to remifentanil-induced postoperative hyperalgesia via regulation of NMDA receptor NR1 subunit phosphorylation and GLT-1

2020 ◽  
Author(s):  
Yuan Yuan ◽  
Chenxu Wang ◽  
Beibei Dong ◽  
Keliang Xie ◽  
Yonghao Yu
Keyword(s):  
Spinal Cord ◽  
Nmda Receptor ◽  
Nlrp3 Inflammasome ◽  
Receptor Protein ◽  
Inflammasome Activation ◽  
Remifentanil Infusion ◽  
Caspase 1 ◽  
Nlrp3 Inflammasome Activation ◽  
Behavioural Tests ◽  
Inflammasome Inhibitors

Abstract Background Although remifentanil provides perfect analgesia during operations, postoperative remifentanil-induced hyperalgesia (RIH) might be a challenge to anaesthetists. Increasingly, the NOD-like receptor protein 3 (NLRP3) signalling pathway are being implicated in the initiation and maintenance of these conditions. In the present work, we examined the hypothesis that NLRP3 inflammasome activation contributes to RIH via regulation of NMDA receptor NR1 subunit phosphorylation and glutamate transporter-1 (GLT-1) by interleukin-1β (IL-1β). Methods We first tested the changes in thermal and mechanical hyperalgesia at baseline (24 h before remifentanil infusion) and 2 h, 6 h, 24 h, and 48 h after remifentanil infusion in a rat model of incisional pain. Then, the expression of IL-1β and GLT-1 and phosphorylation of NMDA receptor NR1 subunits (Phospho-NR1) in the L4–L6 spinal cord segments were measured. Furthermore, we investigated the effects of IL-1ra, a selective IL-1β inhibitor, on behavioural tests of RIH and on the expression of GLT-1 and Phospho-NR1. In addition, we measured the expression of TLR4, P2X7R, NLRP3 and caspase-1, which are indicators of NLRP3 inflammasome activation. Finally, we investigated the effects of (+)-naloxone (a TLR4 inhibitor), A438079 (a P2X7R inhibitor) and ac-YVADcmk (a caspase-1 inhibitor), which are all selective NLRP3 inflammasome inhibitors, on behavioural tests of RIH and on the expression of IL-1β, GLT-1 and Phospho-NR1. Results The initiation and maintenance of RIH was mediated by a previously unidentified mechanism--namely, remifentanil-induced spinal NLRP3 inflammasome activation and the associated release of IL-1β. Remifentanil induced significant postoperative hyperalgesia, as indicated by behavioural tests, which were markedly improved by pretreatment with IL-1ra and NLRP3 inflammasome inhibitors. Moreover, remifentanil infusion decreased the expression of GLT-1 and increased Phospho-NR1 in the spinal cord, which were reversed by pretreatment with IL-1ra and NLRP3 inflammasome inhibitors. More importantly, remifentanil infusion increased IL-1β expression and activated NLRP3 inflammasomes, which were significantly attenuated by NLRP3 inflammasome inhibitors. Conclusion The above results suggest that NLRP3 inflammasome activation contributes to RIH via regulation of Phospho-NR1 and GLT-1 by IL-1β. Inhibition of NLRP3 inflammasome activation or IL-1β may be an effective and novel option for the treatment of RIH.

scholarly journals Koumine Suppresses IL-1β Secretion and Attenuates Inflammation Associated With Blocking ROS/NF-κB/NLRP3 Axis in Macrophages

2021 ◽  
Vol 11 ◽  
Author(s):  
Yufei Luo ◽  
Bojun Xiong ◽  
Haiping Liu ◽  
Zehong Chen ◽  
Huihui Huang ◽  
...  
Keyword(s):  
Nlrp3 Inflammasome ◽  
Inflammatory Diseases ◽  
Inhibitory Effect ◽  
Receptor Protein ◽  
Mechanistic Study ◽  
Inflammasome Activation ◽  
Nlrp3 Inflammasome Activation ◽  
Underlying Mechanisms

Koumine (KM), one of the primary constituents of Gelsemium elegans, has been used for the treatment of inflammatory diseases such as rheumatoid arthritis, but whether KM impacts the activation of the NOD-like receptor protein 3 (NLRP3) inflammasome remains unknown. This study aimed to explore the inhibitory effect of KM on NLRP3 inflammasome activation and the underlying mechanisms both in vitro using macrophages stimulated with LPS plus ATP, nigericin or monosodium urate (MSU) crystals and in vivo using an MSU-induced peritonitis model. We found that KM dose-dependently inhibited IL-1β secretion in macrophages after NLRP3 inflammasome activators stimulation. Furthermore, KM treatment efficiently attenuated the infiltration of neutrophils and suppressed IL-1β production in mice with MSU-induced peritonitis. These results indicated that KM inhibited NLRP3 inflammasome activation, and consistent with this finding, KM effectively inhibited caspase-1 activation, mature IL-1β secretion, NLRP3 formation and pro-IL-1β expression in LPS-primed macrophages treated with ATP, nigericin or MSU. The mechanistic study showed that, KM exerted a potent inhibitory effect on the NLRP3 priming step, which decreased the phosphorylation of IκBα and p65, the nuclear localization of p65, and the secretion of TNF-α and IL-6. Moreover, the assembly of NLRP3 was also interrupted by KM. KM blocked apoptosis-associated speck-like protein containing a CARD (ASC) speck formation and its oligomerization and hampered the NLRP3-ASC interaction. This suppression was attributed to the ability of KM to inhibit the production of reactive oxygen species (ROS). In support of this finding, the inhibitory effect of KM on ROS production was completely counteracted by H2O2, an ROS promoter. Our results provide the first indication that KM exerts an inhibitory effect on NLRP3 inflammasome activation associated with blocking the ROS/NF-κB/NLRP3 signal axis. KM might have potential clinical application in the treatment of NLRP3 inflammasome-related diseases.

scholarly journals The Role of the Effects of Autophagy on NLRP3 Inflammasome in Inflammatory Nervous System Diseases

2021 ◽  
Vol 9 ◽  
Author(s):  
Shizhen Zhao ◽  
Xiaotian Li ◽  
jie Wang ◽  
Honggang Wang
Keyword(s):  
Nervous System ◽  
Nlrp3 Inflammasome ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Cerebral Hypoperfusion ◽  
Receptor Protein ◽  
Future Research ◽  
Nervous System Diseases ◽  
Caspase 1

Autophagy is a stable self-sustaining process in eukaryotic cells. In this process, pathogens, abnormal proteins, and organelles are encapsulated by a bilayer membrane to form autophagosomes, which are then transferred to lysosomes for degradation. Autophagy is involved in many physiological and pathological processes. Nucleotide-binding oligomerization domain-like receptor protein 3 (NLRP3) inflammasome, containing NLRP3, apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) and pro-caspase-1, can activate caspase-1 to induce pyroptosis and lead to the maturation and secretion of interleukin-1 β (IL-1 β) and IL-18. NLRP3 inflammasome is related to many diseases. In recent years, autophagy has been reported to play a vital role by regulating the NLRP3 inflammasome in inflammatory nervous system diseases. However, the related mechanisms are not completely clarified. In this review, we sum up recent research about the role of the effects of autophagy on NLRP3 inflammasome in Alzheimer’s disease, chronic cerebral hypoperfusion, Parkinson’s disease, depression, cerebral ischemia/reperfusion injury, early brain injury after subarachnoid hemorrhage, and experimental autoimmune encephalomyelitis and analyzed the related mechanism to provide theoretical reference for the future research of inflammatory neurological diseases.

scholarly journals Glycine Attenuates Lipopolysaccharide-Induced Acute Lung Injury by Regulating NLRP3 Inflammasome and NRF2 Signaling

Nutrients ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 611 ◽  
Author(s):  
Yunchang Zhang ◽  
Xiaoshi Ma ◽  
Da Jiang ◽  
Jingqing Chen ◽  
Hai Jia ◽  
...  
Keyword(s):  
Lung Injury ◽  
Nlrp3 Inflammasome ◽  
Nuclear Factor Κb ◽  
Receptor Protein ◽  
Mrna Levels ◽  
Gm Csf ◽  
Lps Challenge ◽  
Induce Lung Injury ◽  
Underlying Mechanisms ◽  
Factor Α

Glycine supplementation has been reported to alleviate lipopolysaccharide (LPS)-induced lung injury in mice. However, the underlying mechanisms responsible for this beneficial effect remain unknown. In the present study, male C57BL/6 mice were treated with aerosolized glycine (1000 mg in 5 mL of 0.9% saline) or vehicle (0.9% saline) once daily for 7 continuous days, and then were exposed to aerosolized LPS (5 mg in 5 mL of 0.9% saline) for 30 min to induce lung injury. Sera and lung tissues were collected 24 h post LPS challenge. Results showed that glycine pretreatment attenuated LPS-induced decreases of mucin at both protein and mRNA levels, reduced LPS-triggered upregulation of pro-inflammatory cytokines, such as tumor necrosis factor-α (TNF-α), interferons, granulocyte-macrophage colony-stimulating factor (GM-CSF), and interleukins. Further study showed that glycine-reduced LPS challenge resulted in the upregulation of nuclear factor κB (NF-κB), nucleotide binding domain (NOD)-like receptor protein 3 (NLRP3) inflammasome. In addition, LPS exposure led to the downregulation of NRF2 and downstream targets, which were significantly improved by glycine administration in the lung tissues. Our findings indicated that glycine pretreatment prevented LPS-induced lung injury by regulating both NLRP3 inflammasome and NRF2 signaling.

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