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Neutrophil extracellular trap induction by alcohol generates unique low-density neutrophils with defective functions and impaired clearance contributing to liver damage in alcoholic hepatitis

ABSTRACT: Neutrophil extracellular trap induction by alcohol generates unique low-density neutrophils with defective functions and impaired clearance contributing to liver damage in alcoholic hepatitis

PROVIDER: PRJNA720943 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14200228_1.fastq.gz	Fastqsanger.gz
	SRR14200228_2.fastq.gz	Fastqsanger.gz
	SRR14200229_1.fastq.gz	Fastqsanger.gz
	SRR14200229_2.fastq.gz	Fastqsanger.gz
	SRR14200230_1.fastq.gz	Fastqsanger.gz

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Neutrophil extracellular trap induction by alcohol generates unique low-density neutrophils with defective functions and impaired clearance contributing to liver damage in alcoholic hepatitis

Project description:Alcoholic hepatitis (AH) is characterized by severe liver and systemic inflammation and high mortality. Although numerous studies correlated neutrophil counts with poor clinical outcomes, the role of neutrophils in AH is poorly understood. Here, we report that neutrophils contribute to liver damage through increased neutrophils extracellular traps (NET) production in AH patients and mouse models with a concordant significant increase of low-density neutrophils (LDNs) in AH patients. Transcriptome analysis revealed that high-density neutrophils (HDNs) are activated and more prone to release NET, whereas LDNs exhibit exhausted phenotype. We show that alcohol-induced NET release in HDNs induces a unique LDN subset with decreased functionality and reduced clearance. Elimination of both defective HDNs and LDNs through in vivo neutrophil depletion or prevention of NET production with granulocyte colony stimulating factor (G-CSF) treatment ameliorate alcohol-induced liver damage. Our findings uncover alcohol-induced neutrophil phenotypic changes and provide mechanistic insights for therapeutic interventions in AH.

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ApoM binds endotoxin contributing to neutralization and clearance by High Density Lipoprotein.

Project description:BackgroundHDL possesses anti-inflammatory properties, however, the exact mechanism is not fully understood. Endotoxin is a potent inducers of TLR4 signaling, leading to inflammatory mediators' release. It has been estimated that TLR4 recognizes about 5% of circulating lipopolysaccharide whereas 95% is cleared by plasma lipoproteins, mainly HDL. ApoM is required for HDL biogenesis and 95% of plasma ApoM is found associated with HDL, both are significantly reduced during sepsis.AimThe aim of this study is to investigate whether ApoM binds endotoxin and contributes to anti-inflammatory activity of HDL.MethodsIsothermal Titration Calorimetry (ITC) was used to determine the binding of ultrapure E. coli LPS to the recombinant ApoM protein. Purified human HDL and recombinant ApoM was used to investigate LPS neutralization using human and murine macrophages and computational simulation was performed.ResultApoM shows high affinity for E. coli LPS, forming 1:1 complexes with Kd values below 1 μΜ, as revealed by ITC. The binding process is strongly exothermic and enthalpy-driven (ΔrH = -36.5 kJ/mol), implying the formation of an extensive network of interactions between ApoM and LPS in the bound state. Computational simulation also predicted high-affinity binding between ApoM and E. coli LPS and the best scoring models showed E. coli LPS docking near the calyx of ApoM without blocking the pocket. The biological significance of this interaction was further demonstrated in macrophages where purified HDL neutralized an E. coli LPS effect and significantly reduced TNFα release from human THP-1 cells.ConclusionApoM binds LPS to facilitate endotoxin neutralization and clearance by HDL.

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Trap-80-dependence of TNF-alpha-induced genes

Project description:In fibroblasts, p65-dependent genes can be sub-divided, depending on whether they are Trap-80-dependent or -independent. To examine the generality of this grouping, we performed a microarray analysis of wild-type and Trap-80 knock-down fibroblasts, before and after stimulation of NF-kappaB activity using TNF-alpha. RNA was extracted from three independent cultures of wild-type and Trap-80 knock-down fibroblasts, before and after stimulation for 1 hour with 5ng/ml TNF-alpha. The unstimulated and stimulated wild-type samples, and the stimulated Trap-80 knock-down samples, were used for microarray analysis.

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TRAP-seq following Pdx1 depletion

Project description:TRAP performed in GFP-RPL10A Min6 cells transfected with siRNA targeting Pdx1 or a non-targeting (NT) control. IP RNA was isolated by TRAP protocol and input lysate was used to isolate Total RNA. RNA-seq was performed on both IP and Total RNA.

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