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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-Seq II]

ABSTRACT: Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-Seq II]

PROVIDER: PRJNA1049487 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27125082_1.fastq.gz	Fastqsanger.gz
	SRR27125082_2.fastq.gz	Fastqsanger.gz
	SRR27125083_1.fastq.gz	Fastqsanger.gz
	SRR27125083_2.fastq.gz	Fastqsanger.gz
	SRR27125097_1.fastq.gz	Fastqsanger.gz

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming

Project description:Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-seq]

Project description:Epigenetic alterations are among the prominent drivers of cellular senescence and/or aging, intricately orchestrating gene expression programs during these processes. Many studies have investigated the histone modification mechanisms that regulate cellular senescence and aging. In this study, we show that histone lactylation, an identified histone modification that integrates metabolic processes, epigenetic regulation of gene expression and cellular activities in response to internal and external cues, plays a pivotal role in counteracting senescence and mitigating dysfunctions of skeletal muscle in aged mice. Mechanistically, histone lactylation levels markedly decrease during cellular senescence but are restored under hypoxic conditions primarily due to elevated glycolytic activity. The enrichment of histone lactylation at promoters is essential for sustaining the expression of genes involved in the cell cycle and DNA repair pathways, thereby inhibiting cellular senescence. Furthermore, the modulation of enzymes crucial for histone lactylation, including p300 and HDAC1, leads to reduced histone lactylation and accelerated cellular senescence. Consistently, the suppression of glycolysis and the depletion of histone lactylation are also observed during skeletal muscle aging. Running exercise increases the levels of glycolysis and histone lactylation, which in turn upregulate key genes in the DNA repair and proteostasis pathways, thereby helping to preserve the proper function of skeletal muscle. Our study highlights the significant roles of histone lactylation in modulating cellular senescence as well as aging-related tissue function, suggesting that this modification may serve as an innovative biomarker for senescence and provides a promising avenue for antiaging intervention via metabolic manipulation.

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [snRNA-seq]

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [CUT&Tag]

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-Seq II]

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [CUT&Tag]

Project description:Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [CUT&Tag]

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-seq]

Project description:Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-seq]

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [snRNA-seq]

Project description:Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [snRNA-seq]

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming

Project description:This SuperSeries is composed of the SubSeries listed below.

2024-05-01 | GSE226008 | GEO

Ikzf1 lactylation regulates CD4 T cell differentiation

Project description:Dysregulation of Th17 differentiation was implicated in multiple inflammatory and autoimmune diseases including autoimmune uveitis. In the current study, we have provided evidence indicating that lactate-derived lactylation plays important roles in regulating Th17 differentiation. The lactylation level of CD4+ T cells was upregulated in EAU mice and inhibiting lactylation resulted in impaired EAU progression. We characterized the global lactylome of CD4+ T cells of normal and EAU mice. We found that the differentially lactylated proteins were enriched in pathways related to immune responses including leukocyte differentiation. Importantly, our results show that the lactylation level of Ikzf1 (K164) functions in regulating Th17 differentiation by differentially modulating gene expression patterns which are related to CD4+ T cell differentiation by CUT& Tag analysis. In view of the above mentioned well-documented evidence, Ikzf1 lactylation might represent an important regulator for Th17 differentiation in autoimmune uveitis.

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