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Selective Extracellular Signal-Regulated Kinase 1/2 (ERK1/2) Inhibition by the SCH772984 Compound Attenuates In Vitro and In Vivo Inflammatory Responses and Prolongs Survival in Murine Sepsis Models

ABSTRACT: Selective Extracellular Signal-Regulated Kinase 1/2 (ERK1/2) Inhibition by the SCH772984 Compound Attenuates In Vitro and In Vivo Inflammatory Responses and Prolongs Survival in Murine Sepsis Models

PROVIDER: PRJNA746487 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15130751_1.fastq.gz	Fastqsanger.gz
	SRR15130751_2.fastq.gz	Fastqsanger.gz
	SRR15130752_1.fastq.gz	Fastqsanger.gz
	SRR15130752_2.fastq.gz	Fastqsanger.gz
	SRR15130753_1.fastq.gz	Fastqsanger.gz

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Selective Extracellular Signal-Regulated Kinase 1/2 (ERK1/2) Inhibition by the SCH772984 Compound Attenuates In Vitro and In Vivo Inflammatory Responses and Prolongs Survival in Murine Sepsis Models

Project description:This is an accompanying ATAC-seq data to the transcriptomic survey of RAW264.7 cells treated with ERK1/2 inhibitor SCH772984 upon 1hr, 4hrs and 24 hrs LPS challenge. The transcriptomic data are deposited in GEO under GSE179554.

2021-09-24 | GSE180085 | GEO

Selective extracellular signSelective Extracellular Signal-Regulated Kinase 1/2 (ERK1/2) Inhibition by the SCH772984 Compound Attenuates In Vitro and In Vivo Inflammatory Responses and Prolongs Survival in Murine Sepsis Models

Project description:Selective extracellular signSelective Extracellular Signal-Regulated Kinase 1/2 (ERK1/2) Inhibition by the SCH772984 Compound Attenuates In Vitro and In Vivo Inflammatory Responses and Prolongs Survival in Murine Sepsis Models

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Project description:Sepsis is the leading cause of death in intensive care units worldwide. Current treatments of sepsis are largely supportive and clinical trials using specific pharmacotherapy for sepsis have failed to improve outcomes. Here, we used the lipopolysaccharide (LPS)-stimulated mouse RAW264.7 cell line and AlphaLisa assay for TNFa as a readout to perform a supervised drug repurposing screen for sepsis treatment with compounds targeting epigenetic enzymes, including kinases. We identified the SCH772984 compound, an extracellular signal-regulated kinase (ERK) 1/2 inhibitor, as an effective blocker of TNFa production in vitro. RNA-Seq of the SCH772984-treated RAW264.7 cells at 1, 4, and 24 h time points of LPS challenge followed by functional annotation of differentially expressed genes highlighted the suppression of cellular pathways related to the immune system. SCH772984 treatment improved survival in the LPS-induced lethal endotoxemia and cecal ligation and puncture (CLP) mouse models of sepsis, and reduced plasma levels of Ccl2/Mcp1. Functional analyses of RNA-seq datasets for kidney, lung, liver, and heart tissues from SCH772984-treated animals collected at 6 h and 12 h post-CLP revealed a significant downregulation of pathways related to the immune response and platelets activation but upregulation of the extracellular matrix organization and retinoic acid signaling pathways. Thus, this study defined transcriptome signatures of SCH772984 action in vitro and in vivo, an agent that has the potential to improve sepsis outcome

2021-09-24 | GSE179554 | GEO

Selective Extracellular Signal-Regulated Kinase 1/2 (ERK1/2) Inhibition by the SCH772984 Compound Attenuates In Vitro and In Vivo Inflammatory Responses and Prolongs Survival in Murine Sepsis Models.

| S-EPMC8508766 | biostudies-literature

Vasopressin V2 Receptor, Tolvaptan, and ERK1/2 Phosphorylation in the Renal Collecting Duct

Project description:Activation of ERK1 and ERK2 is essential in regulation of a wide variety of cellular and physiological processes. In native inner medullary collecting ducts, vasopressin (AVP) working through the V2 subtype vasopressin receptor (V2R)-mediated activation of Gαs, inhibits ERK1 and ERK2 activity. However, it has been reported that V2R can signal independently of Gαs through the activation of β-arrestin, which activates ERK1 and ERK2. Vaptans, V2R antagonists that function as so-called “inverse agonists”, have the potential of promoting cell proliferation via β-arrestin-dependent ERK activation. Here we use the mpkCCD cell line which natively expresses V2R to investigate the effects of AVP, the V2-selective analog dDAVP, and tolvaptan on ERK1 and ERK2 phosphorylation and activation. We demonstrated that ERK1 and ERK2 phosphorylation in mpkCCD cells was significantly reduced by either AVP or dDAVP, in contrast to the increases seen in non-collecting duct cells overexpressing V2R. We also found that tolvaptan has a strong effect to increase ERK1 and ERK2 phosphorylation in the presence of dDAVP and that the tolvaptan effect to increase ERK1 and ERK2 phosphorylation is absent in PKA-null mpkCCD cells. Thus, it appears that the tolvaptan effect to increase ERK activation is PKA-dependent and, therefore, not mediated by the β-arrestin pathway. Overall, the studies show that AVP decreases and that tolvaptan increases ERK1 and ERK2 activation in cells expressing V2R at endogenous levels, and provide no evidence for a role for β-arrestin in the regulation of ERK1 and ERK2 activity.

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Vasopressin V2 Receptor, Tolvaptan, and ERK1/2 Phosphorylation in the Renal Collecting Duct II

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2021-08-13 | GSE181803 | GEO

Expression data from ERK1/2 null endothelial cells

Project description:Angiogenesis is a complex process orchestrated by both growth factors and cell adhesion to the extracellular matrix and is initiated by focal degradation of the vascular basement membrane with subsequent migration and proliferation of endothelial cells (EC). The Ras/Raf/MEK/ERK pathway is critical for EC function during angiogensis. Although in vitro studies implicate ERK1 and ERK2 in EC survival, their precise role in EC function in vivo remains poorly defined. Cre/loxP technology was used to inactivate Erk1 and Erk2 in EC during murine development, resulting in embryonic lethality due to a drastic reduction in angiogenesis. The angiogenic defect was linked to diminished EC proliferation and migration, but not to increased cell apoptosis. Expression of key cell cycle regulators was diminished in the double knockout cells. In addition, both Paxillin and Focal Adhesion Kinase were expressed at lower levels and failed to correctly localize to the cell membrane in EC lacking Erk1 and Erk2, leading to defects in the organization of the cytoskeleton and in cell motility. The results demonstrate that ERK1 and ERK2 coordinate cell proliferation and migration during angiogenesis. Lentivirus infected cells to generate ERK1/2 WT and ERK1/2 DKO endothelial cells were cultured, RNA was extracted and Affymetrix gene expression arrays were performed.

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Identification of ERK1 direct substrates using stable isotope labeled kinase assay linked phosphoproteomics

Project description:Following the kinase assay linked phosphoproteomics strategy (KALIP) (Xue, L et al., 2012), we used extracellular signal-regulated kinases 1 (ERK1) to phosphorylate the HEK293 cell lysate under the in vitro kinase assay condition. The phosphorylated proteins were then isolated and identified by mass spectrometry. The in vitro phosphorylated proteins with new phosphates were further overlapped with reported in vivo ERK1-dependent phosphoproteomics data for the identification of bona fide direct substrates of ERK1. In total, we identified 27 direct substrates of ERK1. Data analysis procedure: Raw MS files from the LTQ-Orbitrap-Velos were analyzed by Proteome Discoverer 1.3. MS/MS spectra were searched against the IPI-human database (version 3.83) containing both forward and reverse protein sequences by the SEQUEST search engine. The false discovery rate (FDR) was set to 0.01 on the peptide level. Ingenuity Pathway Analysis (IPA) was applied for the functional annotation.

2014-07-17 | PXD000357 | Pride

Biosynthesis of the antifungal compound fragin is controlled by a novel quorum sensing signal

Project description:Members of the diazeniumdiolate class of natural compounds show great potential for drug development. Yet, their biosynthesis has remained elusive to date. Here, we identify a gene cluster directing the biosynthesis of the diazeniumdiolate compound fragin in Burkholderia cenocepacia H111. We provide evidence that fragin is a metallophore and that metal chelation is the molecular basis of its antifungal activity. We also show that a subset of the fragin biosynthetic genes is involved in the synthesis of a novel cell-to-cell signaling molecule, valdiazen. RNA-Seq analyses revealed that valdiazen not only controls fragin biosynthesis but affects expression of more than 100 genes. Homologs of the valdiazen biosynthesis genes are found in various bacteria, suggesting that valdiazen is the first representative of a new signal molecule class. Using structural information, in silico prediction of enzymatic functions and biochemical data we propose a biosynthesis route for fragin and valdiazen.

2018-04-05 | GSE97171 | GEO

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