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OGD-Induced Lactylation of H3K9 Contributes to M1 polarization and Inflammation of microglia Through TNF pathway

ABSTRACT: OGD-Induced Lactylation of H3K9 Contributes to M1 polarization and Inflammation of microglia Through TNF pathway

PROVIDER: PRJNA1138673 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29913364_1.fastq.gz	Fastqsanger.gz
	SRR29913364_2.fastq.gz	Fastqsanger.gz
	SRR29913365_1.fastq.gz	Fastqsanger.gz
	SRR29913365_2.fastq.gz	Fastqsanger.gz
	SRR29913366_1.fastq.gz	Fastqsanger.gz

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OGD-Induced Lactylation of H3K9 Contributes to M1 polarization and Inflammation of microglia Through TNF pathway

Project description:Hypoxia-induced M1 polarization of microglia and the resultant inflammatory response are pivotal mechanisms in the development of hypoxic-ischemic encephalopathy (HIE). Recent studies have identified lactylation of histones as a novel epigenetic modification, in which lactate groups are added to lysine residues on histones. Lactate, a product of cellular respiration, accumulates in the cytoplasm when cells experience hypoxia due to the conversion of pyruvate by lactate dehydrogenase. Therefore, histone lactylation may be involved in the pathogenesis of HIE. This study aims to investigate the role and mechanism of histone lactylation in hypoxia-induced M1 polarization of microglia and the associated inflammation, with the goal of providing new insights for the research and treatment of HIE.

2024-10-30 | GSE272754 | GEO

Metabolic regulation of gene expression by histone lactylation

Project description:Cancer-augmented lactogenesis has been described by the Warburg effect, and is associated with several major hallmarks of neoplasia. However, the non-metabolic functions of elevated lactate in physiology and disease remain unknown. Here we report histone lysine lactylation as a new type of epigenetic mechanism and as a functional destination for lactate. Histone lactylation is induced under glycolytic conditions such as hypoxia and M1 macrophage polarization. In the late phase of M1 macrophage polarization, increases in histone lactylation but not acetylation mark M2-like genes for activation. Our findings suggest a feedback mechanism of the innate immune system to switch from proinflammation to resolution through histone Kla-associated gene expression. This mechanism is implemented by the coopted function of lactate and histone lactylation in metabolism and epigenetics. Together, our study opens a new avenue for understanding function of lactate and glycolysis underlined diverse pathophysiological conditions.

2019-08-06 | GSE115354 | GEO

PHD inhibition upregulates glycolytic pathway in OGD

Project description:To elucidate the mechanism of enarodustat pretreatment-induced protection against oxygen-glucose deprivation (OGD), we have we have employed whole genome microarray expression profiling as a discovery platform to identify genes upregulated by enarodustat exposure. HK2 cells were pretreated with either vehicle (DMSO) or enarodustat for 24 hours prior to OGD for 16 hours. Pathway analysis revealed upregulated glysolysis pathway.

2020-04-14 | GSE130144 | GEO

Therapeutic potential of microglial SMEK1 via regulation of H3 lysine 9 lactylation in cerebral ischemia-reperfusion injury

Project description:Immune responses and neuroinflammation occurring after acute ischemic stroke (AIS) are closely related to brain injury. Histone lactylation is a metabolic stress-related histone modification that participates in the pathogenesis of various diseases. However, the role of histone regulation in cerebral ischemic stroke remains unknown. In this study, a transient middle cerebral artery occlusion (tMCAO/R) model and an oxygen–glucose deprivation and reoxygenation (OGD/R) model were used to simulate in vivo/in vitro ischemia–reperfusion injury. The underlying mechanism of microglial histone lactylation was investigated using microglia-specific SMEK1-overexpressing mice and BV2 cells. The results showed that lactate overload resulted in elevated histone lactylation after AIS. Decreased SMEK1 expression in microglia after ischemic stroke was associated with increased lactate levels and subsequent neuroinflammation. Microglia-specific SMEK1 deficiency in microglia after ischemia can promote lactate production by inhibiting the pyruvate dehydrogenase kinase 3-pyruvate dehydrogenase (PDK3-PDH) pathway. Specifically, H3 lysine 9 lactylation (H3K9la) activated Ldha and Hif-1α transcription in microglia and promoted glycolysis. SMEK1-overexpressing mice exhibited better neurologic recovery after ischemic stroke than control mice. Mechanistically, we provided new evidence that microglial histone lactylation promoted glycolysis in ischemia‒reperfusion injury and elucidated the potential role of SMEK1 as an upstream regulatory molecule in histone lactylation after cerebral ischemia. According to our results, microglial SMEK1 may be potential therapeutic targets for AIS.

2025-01-02 | GSE283233 | GEO

Hypoxia promotes histone H3K9 lactylation to enhance LAMC2 transcription in esophageal squamous cell carcinoma

Project description:Hypoxia promotes histone H3K9 lactylation to enhance LAMC2 transcription in esophageal squamous cell carcinoma

| PRJNA1074731 | ENA

Identification of SIRT3 as an eraser for H3K9 lactylation by antibody-mediated proximity labeling strategy

Project description:Identification of SIRT3 as an eraser for H3K9 lactylation by antibody-mediated proximity labeling strategy

| PRJNA1147570 | ENA

Global transcriptomic profiling of oxygen-glucose deprivation (OGD)-mediated neuronal injury

Project description:Oxygen-glucose deprivation (OGD) is a cellular phenomenon consistently observed upon occurrence of ischemic stroke which eventually results in neuronal death. Neuronal cell death after ischemia takes place via two distinct processes, necrosis and apoptosis. Apoptosis, programmed cell death, is denoted by chromatin condensation, nuclear blebbing, cellular shrinkage, and DNA fragmentation. Unlike apoptosis, cellular swelling and lysis is suggestive of necrosis. However, these two processes are related not only to the severity but also to the duration of ischemia. Microarray analysis was carried out using 20 Illumina mouse Ref8V1.1 genechip arrays. The assignment of the arrays was as follows: Controls (n=5); exposure to OGD for 10min, 5h, 8h, 15h and 24 h (n=3 respectively).

2013-12-31 | E-GEOD-23158 | biostudies-arrayexpress

Global Profiling of Protein Lactylation Across Subcellular Fractionation Methods in HCT-116

Project description:Protein lactylation is a novel post-translational modification (PTM) involved in many important physiological processes such as macrophage polarization, immune regulation and tumour cell growth. However, most studies to date have focused on the function of lactylation on histones, and little is known about the distribution of lactylation on subcellular proteins. Here, we utilized subcellular fractionation methods to perform the global profiling of lactylation in human colon carcinoma HCT116 cells. This approach detected more unique lactylated proteins compared to the standard method when the amount of antibody and cells was equal. In total, 899 lysine lactylation sites were detected on 441 proteins, including 291 newly discovered lactylation sites and 63 newly lactylated proteins reported under the DDA and DIA acquisition modes. Functional enrichment analysis revealed that the majority of these proteins are involved in nucleosome assembly and slicesome function. For each subcellular fraction, the newly discovered lactylated proteins account for 10% to 20%. Notably, XPC not only has four new lactylation modification sites, but also one of which has been shown to be essential for the nucleotide excision repair process. Additionally, one of the newly discovered lactylation sites in scaffold attachment factor B1 (SAFB1) was found to be very important for the negative regulation of transcriptional activity. In conclusion, we describe a novel method that provides for understanding the characterization of subcellular lactylated proteins.

2024-12-15 | PXD053474 | Pride

Differential lipid partitioning between adipocytes and tissue macrophages modulates macrophage lipotoxicity and M2/M1 polarization in obese mice.

Project description:Obesity-associated insulin resistance is characterized by a state of chronic, low-grade inflammation that is associated with the accumulation of M1 proinflammatory macrophages in adipose tissue. Although different evidence explains the mechanisms linking the expansion of adipose tissue and adipose tissue macrophage (ATM) polarization, in the current study we investigated the concept of lipid-induced toxicity as the pathogenic link that could explain the trigger of this response. We addressed this question using isolated ATMs and adipocytes from genetic and diet-induced murine models of obesity. Through transcriptomic and lipidomic analysis, we created a model integrating transcript and lipid species networks simultaneously occurring in adipocytes and ATMs and their reversibility by thiazolidinedione treatment. We show that polarization of ATMs is associated with lipid accumulation and the consequent formation of foam cell–like cells in adipose tissue. Our study reveals that early stages of adipose tissue expansion are characterized by M2-polarized ATMs and that progressive lipid accumulation within ATMs heralds the M1 polarization, a macrophage phenotype associated with severe obesity and insulin resistance. Furthermore, rosiglitazone treatment, which promotes redistribution of lipids toward adipocytes and extends the M2 ATM polarization state, prevents the lipid alterations associated with M1 ATM polarization. Our data indicate that the M1 ATM polarization in obesity might be a macrophage-specific manifestation of a more general lipotoxic pathogenic mechanism. This indicates that strategies to optimize fat deposition and repartitioning toward adipocytes might improve insulin sensitivity by preventing ATM lipotoxicity and M1 polarization. 15 samples; 2 genotypes and 2 time points

2012-03-22 | E-GEOD-36669 | biostudies-arrayexpress

PHD inhibition upregulates glycolytic pathway in OGD

Project description:PHD inhibition upregulates glycolytic pathway in OGD

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