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RRBS of TET2-mutant human neutrophils

ABSTRACT: RRBS of TET2-mutant human neutrophils

PROVIDER: PRJNA882416 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21640121.fastq.gz	Fastqsanger.gz
	SRR21640122.fastq.gz	Fastqsanger.gz
	SRR21640123.fastq.gz	Fastqsanger.gz
	SRR21640124.fastq.gz	Fastqsanger.gz

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ATAC-seq, RNA-seq and RRBS of TET2-mutant human neutrophils

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RRBS of TET2-mutant human neutrophils

Project description:Somatic mutations acquired by hematopoietic stem cells (HSCs) are commonly found over the course of a lifespan. Some of these clones will outgrow through a process known as clonal hematopoiesis (CH) and produce mutated immune cell progeny, which will shape host immunity. Individuals with CH are asymptomatic but have increased risk of developing leukemia, cardiovascular and pulmonary inflammatory diseases, and severe infections. Despite the key role that neutrophils play in the development of such diseases, little is known about how these prevalent somatic mutations affect neutrophil functionality. In this work, we describe how mutations in TET2, one of the most common mutated genes in individuals with CH, affect human neutrophil biology.

2023-12-01 | GSE213770 | GEO

ATACSeq of TET2-mutant human neutrophils

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RNASeq of TET2-mutant human neutrophils

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ATAC-seq, RNA-seq and RRBS of TET2-mutant human neutrophils

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

2023-12-01 | GSE213771 | GEO

Context Dependent Effects of Ascorbic Acid Treatment in TET2 Mutant Myeloid Neoplasia

Project description:Loss-of-function TET2 mutations (TET2MT) are common in myeloid neoplasia. TET2, a DNA dioxygenase, requires 2-oxoglutarate and Fe(II) to oxidize 5-methylcytosine. TET2MT thus result in hypermethylation and transcriptional repression. Ascorbic acid (AA) increases dioxygenase activity by facilitating Fe(III)/Fe(II) redox reaction and may alleviate some biological consequences of TET2MT by restoring dioxygenase activity. Here, we report the utility of AA in the prevention of TET2MT MN, clarify the mechanistic underpinning of the TET2-AA interactions, and demonstrate that the ability of AA to restore TET2 activity in cells depends on N- and C-terminal lysine acetylation and nature of TET2MT. Consequently, pharmacologic modulation of acetyltransferases and histone deacetylases may regulate TET dioxygenase-dependent AA effects. Thus, our study highlights the contribution of factors that may enhance or attenuate AA effects on TET2 and provides a rationale for novel therapeutic approaches including combinations of AA with class I/II HDAC inhibitor or sirtuin activators in TET2MT leukemia.

2020-09-09 | PXD020550 | Pride

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