Mechanism of RNAm6A methylation modification regulating NLRP3 inflammasome activation for hand, foot and mouth disease progression
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA981706 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR24881513_1.fastq.gz | Fastqsanger.gz | |||
| SRR24881513_2.fastq.gz | Fastqsanger.gz | |||
| SRR24881514_1.fastq.gz | Fastqsanger.gz | |||
| SRR24881514_2.fastq.gz | Fastqsanger.gz | |||
| SRR24881515_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 24 |
Similar Datasets
Project description:The some biomarkers can be found by pairwise comparison. They can distinguish between extremely severe Hand,foot and mouth disease and mild Hand,foot and mouth disease,moreover,they can applied to diagnose extremely severe Hand,foot and mouth disease mild Hand,foot and mouth disease vs.control; extremely severe Hand,foot and mouth disease vs.control; extremely severe Hand,foot and mouth disease vs.mild Hand,foot and mouth disease,verification by qRT-PCR
2013-11-27 | E-GEOD-52780 | biostudies-arrayexpress
Project description:The some biomarkers can be found by pairwise comparison. They can distinguish between extremely severe Hand,foot and mouth disease and mild Hand,foot and mouth disease,moreover,they can applied to diagnose extremely severe Hand,foot and mouth disease
2013-11-27 | GSE52780 | GEO
Project description:During the life cycle of Enterovirus 71 (EV71), N6-methyladenosine (m6A) modification has an important impact on viral replication and the cellular response to viral infection, but the effect of m6A modification on cellular RNAs and pathways during infection is still unknown. The purpose of this research was to investigate the role of m6A in regulating host cell inflammatory response and disease progression during EV71 infection. Methylation RNA immunoprecipitation sequencing (MeRIP-seq) and RNA sequencing (RNA-seq) results show the m6A methylation modification map of control and EV71-infected groups of RD cells. And multilevel validation showed that decreased expression of demethylase FTO (fat mass and obesity-associated protein) was responsible for the elevated total m6A levels in EV71-infected RD cells and that TXNIP may be a target gene for demethylase FTO action. Further functional experiments showed that demethylase FTO silencing promoted TXNIP expression, activation of NLRP3 inflammasome and promoted the release of pro-inflammatory factors in vitro, and demethylase FTO overexpression showed the opposite result. Further tested in an animal model of severe EV71 infection, with results consistent with in vitro. In conclusion, our findings suggested that depletion of demethylase FTO in the presence of EV71 infection increased the m6A level of TXNIP mRNA 3ʹ UTR, increased mRNA stability, and promoted TXNIP expression, which activated the NLRP3 inflammasome and led to the release of pro-inflammatory factors, ultimately promoted HFMD progression. This could help with the development and prevention of m6A modification inhibitor-based drugs for viral-related inflammation and disease.
2023-06-13 | GSE234534 | GEO
Project description:To elucidate alterations in immune cells during enterovirus 71 (EV-A71) infection and explore potential interaction mechanisms.Single-cell sequencing technology was used to sequence peripheral blood monocytes (PBMCs) obtained from a severe hand, foot and mouth disease (HFMD) patient due to EV-A71 and a healthy control.
2024-06-20 | GSE269965 | GEO
Project description:Large-scale outbreak of hand-foot and mouth disease, France, 2021
| PRJEB48181 | ENA
Project description:Inflammasome, activated by pathogen-derived and host-derived danger signals, constitutes a multimolecular signaling complex that serves as a platform for caspase-1 (CASP1) activation and interleukin-1beta (IL1B) maturation. The activation of NLRP3 inflammasome requires two-step signals. The first “priming” signal (Signal 1) enhances gene expression of inflammasome components. The second “activation” signal (Signal 2) promotes the assembly of inflammasome components. Deregulated activation of NLRP3 inflammasome contributes to the pathological processes of Alzheimer’s disease (AD) and multiple sclerosis (MS). However, at present, the precise mechanism regulating NLRP3 inflammasome activation and deactivation remains largely unknown. By genome-wide gene expression profiling, we studied the molecular network of NLRP3 inflammasome activation-responsive genes in a human monocyte cell line THP-1 sequentially given two-step signals. We identified the set of 83 NLRP3 inflammasome activation-responsive genes. Among them, we found the NR4A nuclear receptor family NR4A1, NR4A2, and NR4A3, the EGR family EGR1, EGR2, and EGR3, the IkappaB family NFKBIZ, NFKBID, and NFKBIA as a key group of the genes that possibly constitute a negative feedback loop for shutting down inflammation following NLRP3 inflammasome activation. By molecular network analysis, we identified a complex network of NLRP3 inflammasome activation-responsive genes involved in cellular development and death, and immune and inflammatory responses, where transcription factors AP-1, NR4A, and EGR serve as a hub. Thus, NLRP3 inflammasome activation-responsive genes constitute the molecular network composed of a set of negative feedback regulators for prompt resolution of inflammation. To load the Signal 1 (S1), THP-1 cells were incubated for 3 hours in the culture medium with or without inclusion of 0.2 microgram/ml lipopolysaccharide (LPS). To load the Signal 2 (S2), they were incubated further for 2 hours in the culture medium with inclusion of 10 microM nigericin sodium salt dissolved in ethanol or the equal v/v% concentration of ethanol (vehicle), followed by processing for microarray analysis on Human Gene 1.0 ST Array (Affymetrix).
2014-07-01 | E-GEOD-58959 | biostudies-arrayexpress
Project description:The NLRP3 inflammasome is dysregulated in autoinflammatory disorders caused by inherited mutations and contributes to the pathogenesis of several chronic inflammatory diseases. In this study, we discovered that disulfiram, a safe FDA-approved drug, specifically inhibits the NLRP3 inflammasome, but not the NLRC4 or AIM2 inflammasomes. Disulfiram suppresses caspase-1 activation, ASC speck formation, and pyroptosis induced by several stimuli that activate NLRP3. Mechanistically, NLRP3 is palmitoylated at cysteine 126, a modification required for its localization to the trans-Golgi network and inflammasome activation which was inhibited by disulfiram. Administration of disulfiram to animals inhibited the NLRP3, but not the NLRC4 inflammasome in vivo. Our study uncovers a mechanism by which disulfiram targets NLRP3 and provides a rationale for using a safe FDA-approved drug for the treatment of NLRP3-associated inflammatory diseases.
2024-07-25 | PXD054126 | Pride
Project description:This experiment was performed to analyze the contribution of NLRP3 inflammasome activation to age-related changes in hippocampal RNA. The hypothesis was that decreased inflammasome activation would reduce hippocampal inflammation. Results indicate that inflammasome knockout animals are protected from age-related changes in hippocampal gene expression Gene expression profiles of young (1 month) and old (21-23 month) wild type, CIAS -/- and ASC -/- mouse hippocampal tissue were compared. Total mRNA was extracted using Trizol.
2013-09-05 | E-GEOD-43034 | biostudies-arrayexpress
Project description:The immune system may respond to engineered nanomaterials (ENM) through inflammatory reactions. The NLRP3 inflammasome responds to a wide range of ENM, and its activation is associated with various inflammatory diseases. The objective of the study was to compare the effects of gold ENM of different shapes on NLRP3 inflammasome activation and related signalling pathways. Differentiated THP-1 cells (wildtype, ASC- or NLRP3-deficient), were exposed to PEGylated gold nanorods, nanostars, and nanospheres. Exposed cells were subjected to gene expression analysis. Nanorods, but not nanostars or nanospheres, showed NLRP3 inflammasome activation. ASC- or NLRP3-deficient cells did not show this effect. Gold nanorod-induced NLRP3 inflammasome activation was accompanied by downregulated sterol/cholesterol biosynthesis, oxidative phosphorylation, and purinergic receptor signalling. In conclusion, the shape and surface chemistry of gold nanoparticles determine NLRP3 inflammasome activation.
2023-05-29 | GSE233641 | GEO
Project description:The NLRP3 inflammasome is linked to sterile and pathogen-dependent inflammation, and its dysregulation underlies many chronic diseases. Mitochondria have been implicated as regulators of NLRP3 inflammasome through multiple mechanisms including generation of mitochondrial ROS. Here we report that mitochondrial electron transport chain (ETC) complexes I, II, III and V inhibitors all prevent NLRP3 inflammasome activation. Ectopic expression of Saccharomyces cerevisiae NADH dehydrogenase (NDI1) or Ciona intestinalis alternative oxidase (AOX), which can respectively complement the functional loss of mitochondrial complex I or III, without generation of ROS, rescued NLRP3 inflammasome activation in the absence of endogenous mitochondrial complex I or complex III function. Metabolomics revealed phosphocreatine (PCr), which can sustain ATP levels, as a common metabolite that is diminished by mitochondrial ETC inhibitors. PCr depletion decreased ATP levels and NLRP3 inflammasome activation. Thus, mitochondrial ETC sustains NLRP3 inflammasome activation through PCr-dependent generation of ATP but a ROS independent mechanism.
2022-03-09 | GSE197606 | GEO