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

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

PROVIDER: PRJNA1074731 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27919000_1.fastq.gz	Fastqsanger.gz
	SRR27919000_2.fastq.gz	Fastqsanger.gz
	SRR27919001_1.fastq.gz	Fastqsanger.gz
	SRR27919001_2.fastq.gz	Fastqsanger.gz
	SRR27919002_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

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

Project description:Hypoxia promotes tumorigenesis and lactate accumulation in esophageal squamous cell carcinoma (ESCC). Lactate can induce histone lysine lactylation (Kla, a recently-identified histone marks) to regulate transcription. However, the functional consequence of histone Kla under hypoxia in ESCC remains to be explored. Here, we reveal that hypoxia facilitates histone H3K9la to enhance LAMC2 transcription for proliferation of ESCC. We found that global level of Kla was elevated under hypoxia, and thus identified the landscape of histone Kla in ESCC by quantitative proteomics. Furthermore, we show a significant increase of H3K9la level induced by hypoxia. Next, MNseq ChIP-seq and RNA-seq analysis suggest that H3K9la is enriched at the promoter of cell junction genes. Finally, we demonstrate that the histone H3K9la facilitates the expression of LAMC2 for ESCC invasion by in vivo and in vitro experiments. Briefly, our study reveal a vital role of histone Kla triggered by hypoxia in cancer.

2024-05-22 | GSE255352 | GEO

Hypoxia promotes histone H3K9 lactylation to enhance <i>LAMC2</i> transcription in esophageal squamous cell carcinoma.

Project description:Hypoxia promotes tumorigenesis and lactate accumulation in esophageal squamous cell carcinoma (ESCC). Lactate can induce histone lysine lactylation (Kla, a recently identified histone marks) to regulate transcription. However, the functional consequence of histone Kla under hypoxia in ESCC remains to be explored. Here, we reveal that hypoxia facilitates histone H3K9la to enhance LAMC2 transcription for proliferation of ESCC. We found that global level of Kla was elevated under hypoxia, and thus identified the landscape of histone Kla in ESCC by quantitative proteomics. Furthermore, we show a significant increase of H3K9la level induced by hypoxia. Next, MNase ChIP-seq and RNA-seq analysis suggest that H3K9la is enriched at the promoter of cell junction genes. Finally, we demonstrate that the histone H3K9la facilitates the expression of LAMC2 for ESCC invasion by in vivo and in vitro experiments. Briefly, our study reveals a vital role of histone Kla triggered by hypoxia in cancer.

| S-EPMC11233973 | biostudies-literature

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

Project description:To identify potential histone Kla sites trigged by hypoxia in ESCC, we performed a stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomic analysis coupled with Kla affinity enrichment to characterize the landscape of histone Kla in the KYSE30 cells

2024-01-29 | PXD048995 |

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

Project description:As a novel post-translational modification of histone derived from lactate, lysine lactylation (Kla) links lactate metabolism to epigenetic regulation, playing a role in modulation of gene expression in tumor and immune microenvironment. Evidence so far indicates that HDAC1-3 can catalyze the removal of Kla. However, the regulated targets of HDACs for Kla and functional consequence remain elusive. Herein, we used an antibody-based proximity labeling approach to identify SIRT3 binding to histone H3K9la and catalytic removal of the lactylationoup. The molecular docking results further revealed the mechanism of the binding of Kla peptide to SIRT3. More importantly, SIRT3 can specifically modulate the gene transcription by regulating H3K9la, inhibiting the progression of esophageal cancer cells (ESCC). In conclusion, our work identifies the delactylase of H3K9la and reveal an H3K9la-mediated molecular mechanism catalyzed by SIRT3 for gene transcription regulation in ESCC, and our findings provide an opportunity to investigate the physiological significance of Kla and shed light on the unknown cellular mechanisms controlled by SIRT3.

2024-08-18 | GSE274648 | GEO

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

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

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

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

| PRJNA1138673 | ENA

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.

2023-08-28 | GSE226678 | GEO

PTBP1 Lactylation Promotes Glioma Stem Cell Maintenance through PFKFB4-Driven Glycolysis

Project description:Longstanding evidence implicates glioma stem cells (GSCs) as the major driver for glioma propagation and recurrence. GSCs have a distinctive metabolic landscape characterized by elevated glycolysis. Lactate accumulation resulting from enhanced glycolytic activity can drive lysine lactylation to regulate protein functions, suggesting that elucidating the lactylation landscape in GSCs could provide insights into glioma biology. Herein, we demonstrated that global lactylation was significantly elevated in GSCs compared to differentiated glioma cells (DGCs). PTBP1, a central regulator of RNA processing, was hyperlactylated in GSCs, and SIRT1 induced PTBP1 delactylation. PTBP1-K436 lactylation supported glioma progression and GSC maintenance. Mechanistically, K436 lactylation inhibited PTBP1 proteasomal degradation by attenuating the interaction with TRIM21. Moreover, PTBP1 lactylation enhanced its RNA-binding capacity and facilitated PFKFB4 mRNA stabilization, which further increased glycolysis. Together, these findings uncovered a lactylation-mediated mechanism in GSCs driven by metabolic reprogramming that induces aberrant epigenetic modifications to further stimulate glycolysis, resulting in a vicious cycle to exacerbate tumorigenesis.

2024-11-05 | GSE262995 | GEO

Expression data from hypoxia exposed normal human esophageal epithelial cells

Project description:To delineate the role of hypoxia in esophageal epithelial biology, we carried out gene array experiments using a non-transformed immortalized diploid human esophageal cell line, EPC2-hTERT (Mol Cancer Res. 2003;1:729-38). Unlike cancer cell lines, EPC2-hTERT has no genetic alterations at early passages that may affect the cellular response to hypoxia.

2009-09-01 | GSE17353 | GEO

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