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ChIP-seq analysis of changes in H3K27ac by endoplasmic reticulum stress (ERS) in mouse primary hepatocytes.

ABSTRACT: ChIP-seq analysis of changes in H3K27ac by endoplasmic reticulum stress (ERS) in mouse primary hepatocytes.

PROVIDER: PRJNA505776 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8197280.fastq.gz	Fastqsanger.gz
	SRR8197281.fastq.gz	Fastqsanger.gz
	SRR8197282.fastq.gz	Fastqsanger.gz
	SRR8197283.fastq.gz	Fastqsanger.gz
	SRR8197276.fastq.gz	Fastqsanger.gz

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ChIP-seq analysis of changes in H3K27ac by endoplasmic reticulum stress (ERS) in mouse primary hepatocytes.

Project description:Mouse primary hepatocytes (MPH) prepared from C57Bl6 male adult mice were treated with the ERS-drug thapsigargin and ChIP-seq was performed using an H3K27ac antibody (Active Motif ref 39685).

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Transcriptomic analysis of endoplasmic reticulum stress (ERS) regulated genes in mouse primary hepatocytes.

Project description:Transcriptomic analysis of endoplasmic reticulum stress (ERS) regulated genes in mouse primary hepatocytes.

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Transcriptomic analysis of endoplasmic reticulum stress (ERS) regulated genes in mouse primary hepatocytes.

Project description:Mouse primary hepatocytes (MPH) prepared from C57Bl6 male adult mice were treated with the ERS-drug thapsigargin and used to prepare RNA.

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Project description:Primary retroperitoneal liposarcoma (RLPS) is a rare heterogeneous tumor occurring within retroperitoneal space, and its overall survival did not improve much in the past few decades. Based on a small-sample clinical practice at our center, patients with RLPS can greatly benefit from combination of anlotinib and eribulin. In this study, we investigated combinational effect of anlotinib and eribulin on RLPS. Through transcriptome analysis, we uncovered and validated that synergistic effect mainly induced by endoplasmic reticulum stress (ERS) pathway both in vitro and in vivo.

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Project description:In eukaryotic cells, the spatial regulation of protein expression is frequently conferred through the coupling of mRNA localization and the local control of translation. mRNA localization to the endoplasmic reticulum (ER) is a prominent example of such regulation and serves a ubiquitous role in segregating the synthesis of secretory and integral membrane proteins to the ER. Recent genomic and biochemical studies have now expanded this view to suggest a role for the ER in global protein synthesis. We have utilized cell fractionation and ribosome profiling to obtain a genomic survey of the subcellular organization of mRNA translation and report that ribosomal loading of mRNAs, a proxy for mRNA translation, is biased to the ER. Notably, ER-associated mRNAs encoding both cytosolic and topogenic signal-encoding proteins display similar ribosome loading densities, suggesting that ER-associated ribosomes serve a global role in mRNA translation. We propose that the partitioning of mRNAs and their translation between the cytosol and ER compartments may represent a novel mechanism for the post-transcriptional regulation of gene expression. HEK293 cells were fractionated between the cytosol and endoplasmic reticulum. Within each fraction, ribosome footprints were generated and sequenced. In parallel, total mRNA was sequenced.

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