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Dynamic investigation of hypoxia-induced L-lactylation

ABSTRACT: Dynamic investigation of hypoxia-induced L-lactylation

PROVIDER: PRJNA1205663 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31870706_1.fastq.gz	Fastqsanger.gz
	SRR31870706_2.fastq.gz	Fastqsanger.gz
	SRR31870707_1.fastq.gz	Fastqsanger.gz
	SRR31870707_2.fastq.gz	Fastqsanger.gz
	SRR31870708_1.fastq.gz	Fastqsanger.gz

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Dynamic investigation of hypoxia-induced L-lactylation

Project description:The recently identified histone modification lysine lactylation can be stimulated by L-lactate and glycolysis. Although the chemical group added upon lysine lactylation was originally proposed to be the L-enantiomer of lactate (KL-la), two isomeric modifications, lysine D-lactylation (KD-la), and N-ε-(carboxyethyl) lysine (Kce), also exist in cells, with their precursors being metabolites of glycolysis. The dynamic regulation and differences among these three modifications in response to hypoxia have not been investigated previously. In this study, we demonstrate that intracellular KL-la, but not KD-la or Kce, is upregulated in response to hypoxia. Depletion of glyoxalase enzymes, GLO1 and GLO2, had minimal impact on KD_x001E_la, Kce, or hypoxia-induced KL-la. Conversely, blocking glycolytic flux to L-lactate under hypoxic conditions by knocking out LDHA/B completely abolished the induction of KL-la, but increased KD-la and Kce. We further observed a correlation between the level of KL-la and HIF-1α expression under hypoxic conditions and when small molecules were used to stabilize HIF-1α in the normoxia condition. Our result demonstrated that there is a strong correlation between HIF-1α and KL-la in lung cancer tissues, and that patient samples with higher grade tend to have higher KL-la levels. Using a proteomics approach, we quantified 66 KL-la sites that were upregulated by hypoxia and demonstrated that p300/CBP contributes to hypoxia-induced KL-la. Collectively, our study demonstrates that KL-la, rather than KD-la or Kce, is the prevailing lysine lactylation in response to hypoxia. Our results therefore demonstrate a link between KL-la and the hypoxia-induced adaptation of tumor cells.

2025-02-10 | GSE285693 | GEO

Hypoxia-inducible Factor 1α Mediated Lactylation to Enhance Inflammatory Response during Hypoxia induced lung dysfunction

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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.

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Hypoxia-inducible Factor 1α Mediated Lactylation to Enhance Inflammatory Response during Hypoxia induced lung dysfunction [RNA-seq]

Project description:Hypoxia-inducible Factor 1α Mediated Lactylation to Enhance Inflammatory Response during Hypoxia induced lung dysfunction [RNA-seq]

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

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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.

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