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Functional reprogramming of neutrophils within tumors by hypoxia-driven histone lactylation [RNA-seq]

ABSTRACT: Functional reprogramming of neutrophils within tumors by hypoxia-driven histone lactylation [RNA-seq]

PROVIDER: PRJNA1204117 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31848344_1.fastq.gz	Fastqsanger.gz
	SRR31848344_2.fastq.gz	Fastqsanger.gz
	SRR31848345_1.fastq.gz	Fastqsanger.gz
	SRR31848345_2.fastq.gz	Fastqsanger.gz
	SRR31848346_1.fastq.gz	Fastqsanger.gz

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Functional reprogramming of neutrophils within tumors by hypoxia-driven histone lactylation [scRNA-seq]

Project description:Functional reprogramming of neutrophils within tumors by hypoxia-driven histone lactylation [scRNA-seq]

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Functional reprogramming of neutrophils within tumors by hypoxia-driven histone lactylation [scRNA-seq]

Project description:We used scRNAseq to study the mechanism underlying the functional reprogramming in brain tumors. scRNA-seq of FACS-sorted neutrophils was performed on mice with brain tumors (SB28). We showd that the immunosuppressive ability of brain-tumor infiltrating neutrophils was exclusively mediated by a population of highly glycolytic neutrophils expressing the transferrin receptor CD71.

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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.

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Dynamic investigation of hypoxia-induced L-lactylation

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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.

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