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Comparison of expression profiles of WT and Nrf2AY/AY mutant macrophages under electrophilic stress agent

ABSTRACT: Comparison of expression profiles of WT and Nrf2AY/AY mutant macrophages under electrophilic stress agent

PROVIDER: PRJNA302712 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR2924990.fastq.gz	Fastqsanger.gz
	SRR2925000.fastq.gz	Fastqsanger.gz
	SRR2924991.fastq.gz	Fastqsanger.gz
	SRR2925001.fastq.gz	Fastqsanger.gz
	SRR2924992.fastq.gz	Fastqsanger.gz

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Comparison of expression profiles of WT and Nrf2AY/AY mutant macrophages under electrophilic stress agent [RNA-Seq]

Project description:Nrf2(A502Y) mutant failed to recognize cis-element required for induction of Nrf2 target genes.To examine whether Nrf2(A502Y) supports expression of a distinct gene set from that supported by Nrf2, RNA-Seq analysis was performed. We compared gene expression profiles in peritoneal macrophages from Nrf2+/+ and Nrf2AY/AY mice between basal and DEM (which is an electorophilic stress agent promoting Nrf2 induction)-treated conditions. mRNA profiles of wild type (WT) and Nrf2AY/AY (AY) mutant macrophages under basal and DEM-treated condition were generated by deep sequencing, in triplicate.

2016-01-04 | E-GEOD-75176 | biostudies-arrayexpress

Comparison of expression profiles of WT and Nrf2AY/AY mutant macrophages under electrophilic stress agent [RNA-Seq]

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Comparison of expression profiles of WT and Nrf2AY/AY mutant macrophages under electrophilic stress agent [ChIP-Seq]

Project description:Nrf2(A502Y) mutant macrophages Nrf2(AY/AY) macrophages were more susceptible to toxicity of xenobiotics. To confirm preferences of binding sequences of Nrf2 and Nrf2A502Y in vivo, we performed ChIP-Seq analyses using an anti-Nrf2 antibody on the DEM-treated peritoneal macrophages derived from Nrf2+/+ and Nrf2AY/AY mice.

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Comparison of expression profiles of WT and Nrf2AY/AY mutant macrophages under electrophilic stress agent [ChIP-Seq]

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Comparison of expression profiles of WT and Nrf2AY/AY mutant macrophages under electrophilic stress agent

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

2016-01-04 | GSE75177 | GEO

Comparison of expression profiles of WT and Nrf2AY/AY mutant macrophages under electrophilic stress agent

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

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Project description:Electrophilic groups, such as Michael acceptors, expoxides, are common motifs in natural products (NPs). Electrophilic NPs can act through covalent modification of cysteinyl thiols on functional proteins, and exhibit potent cytotoxicity and anti-inflammatory/cancer activities. Here we describe a new chemoproteomic strategy, termed multiplexed thiol reactivity profiling (MTRP), and its use in target discovery of electrophilic NPs. We demonstrate the utility of MTRP by identifying cellular targets of gambogic acid, an electrophilic NP that is currently under evaluation in clinical trials as anticancer agent. Moreover, MTRP enables simultaneous comparison of seven structurally diversified -unsaturated -lactones, which provides insights into the relative proteomic reactivity and target preference of diverse structural scaffolds coupled to a common electrophilic motif and reveals various potential druggable targets with liganded cysteines. We anticipate that this new method for thiol reactivity profiling in a multiplexed manner will find broad application in redox biology and drug discovery.

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Oxidative and electrophilic stress conditions and the sor1 mutant

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Project description:In the KEAP1-NRF2 stress response system, KEAP1 acts as a sensor for oxidative and electrophilic stresses through formation of S-S bond and C-S bond, respectively. Of the many questions left related to the sensor activity, following three appear important; whether these KEAP1 sensor systems are operating in vivo, whether oxidative and electrophilic stresses are sensed by the similar or distinct systems, and how KEAP1 equips highly sensitive mechanisms detecting oxidative and electrophilic stresses in vivo. To address these questions, we conducted a series of analyses utilizing KEAP1-cysteine substitution mutant mice, conditional selenocysteine-tRNA (Trsp) knockout mice, and human cohort whole genome sequence (WGS) data. The Trsp-knockout provokes severe deficiency of selenoproteins and compensatory activation of NRF2. However, mice lacking homozygously a pair of critical oxidative stress sensor cysteine residues of KEAP1 fail to activate NRF2 in the Trsp-knockout livers. Secondly, this study provides evidence for the differential utilization of KEAP1 sensors for oxidative and electrophilic stresses in vivo. Thirdly, theoretical calculations show that the KEAP1 dimer equips quite sensitive sensor machinery in which modification of a single molecule of KEAP1 within the dimer is sufficient to affect the activity. WGS examinations of rare variants identified seven non-synonymous variants in the oxidative stress sensors in human KEAP1, while no variant was found in electrophilic sensor cysteine residues, supporting the fail-safe nature of the KEAP1 oxidative stress sensor activity. These results provide valuable information for our understanding how mammals respond to oxidative and electrophilic stresses efficiently.

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