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Gene expression profiles under oxidative stress conditions in human HaCaT keratinocytes and the derivative cells expressing shRNA against NRF2, MLL1, or UTX.

ABSTRACT: Gene expression profiles under oxidative stress conditions in human HaCaT keratinocytes and the derivative cells expressing shRNA against NRF2, MLL1, or UTX.

PROVIDER: PRJNA1052078 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27200460_1.fastq.gz	Fastqsanger.gz
	SRR27200460_2.fastq.gz	Fastqsanger.gz
	SRR27200461_1.fastq.gz	Fastqsanger.gz
	SRR27200461_2.fastq.gz	Fastqsanger.gz
	SRR27200462_1.fastq.gz	Fastqsanger.gz

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Gene expression profiles under oxidative stress conditions in human HaCaT keratinocytes and the derivative cells expressing shRNA against NRF2, MLL1, or UTX.

Project description:To determine how transcriptome is altered by knockdown of NRF2, MLL1, or UTX, we performed RNA-sequencing (RNA-seq) analysis of HaCaT cells and its shRNA-expressing derivatives before and after exposure to hydrogen peroxide (H2O2) or cerium oxide nanoparticles (CeO2 NPs).

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Genomic occupancies of MLL1 and UTX, and H3K4me3/K3K27me3 histone modifications upon hydrogen peroxide treatment in human HaCaT keratinocytes.

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Genomic occupancies of MLL1 and UTX, and H3K4me3/K3K27me3 histone modifications upon hydrogen peroxide treatment in human HaCaT keratinocytes.

Project description:Genomic occupancies of MLL1 and UTX, and H3K4me3/K3K27me3 histone modifications upon hydrogen peroxide treatment in human HaCaT keratinocytes.

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HaCaT keratinocytes day3 vs HaCaT keratinocytes day10

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2003-03-10 | E-GEOD-336 | biostudies-arrayexpress

Protein dataset of immortalized HaCaT cells p53 knock down HaCaT keratinocytes

Project description:The p53 protein is encoded by TP53 gene and plays the key role in significant number of cellular processes including proliferation, apoptosis and regulation of many stress response pathways. P53 acts like a direct transcription activator of numerous genes regulating cell cycle arrest, DNA repair, growth inhibition and many others (Mollereau and Ma, 2014). The canonical biological function of p53 is maintaining genome integrity via elimination of damaged or exposed to genotoxic stress cells. Immortalized HaCaT cells are widely used for keratinocyte research, since they maintain stable keratinocyte phenotype, have nearly unlimited proliferative potential, do not require specific growth and differentiation factors (Colombo et al., 2017). Also, HaCaT cells produce typical differentiation markers such as cytokeratins K14 and K10, involucrin (Colombo et al., 2017) and respond to keratinocyte differentiation stimuli. Taking together, HaCaT cells have similar to normal human keratinocytes (NHK) properties, however, as many of spontaneously immortalized cell lines HaCaT cells bear two mutant p53 alleles - R282Q and H179Y (Lehman et al., 1993). Mutp53 in HaCaT has an increased affinity to other p53 family members (p63, p73), which significantly expands p53 properties. Moreover, mutp53 indirectly affects specific target genes via protein-protein interactions with other transcription factors (NF-Y, E2F1, NF-KB) or by tethering p63 to new promotor locations. For more detailed investigation of mutp53 impact on various processes in HaCaT cells we performed a shRNA mediated knockdown of mutp53. For generation of stable TP53 knockdown we employed plasmid vector pLKO-p53-shRNA-941 (Addgene # #25637) followed by puromycin selection of transduced cells. Here we present proteomic dataset obtained from wild type HaCaT cells and p53 knock down HaCaT keratinocytes.

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Project description:We employed human HaCaT cells as a model system to identify cellular proteins that accompany SDS-induced toxicity based on a proteomic approach. HaCaT human keratinocyte cell line were treated with a non-cytotoxic dose of SDS (25 µg/ml, as determined by the MTT assay and microscopically examination) for 48 h. The altered abundance of proteins from HaCaT keratinocytes exposed to SDS was analyzed by LC-MS/MS approach and quantified using Progenesis LC software. The abundance of 217 proteins (which were identified by multiple peptides, ≥ 2) was altered in keratinocytes exposed to SDS; in which 131 proteins had increased abundance while 86 proteins was down regulated. The Pathview map of 131 up-regulated proteins was built and enhancement of glycolysis/gluconeogenesis was found.

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2017-11-03 | PXD007776 | Pride

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Project description:An important step in the proteomic analysis is the optimal extraction and the processing of protein material in order to ensure the highest sensitivity in downstream protein detection. Cell lysis is important for proteomic profiling with an eventual aim to discover differently expressed proteins (DEPs). Herein for cell lysis, two sample preparation protocols were compared: 0.2% SDS-based solubilization combined with the 1DE-gel concentration (Protocol 1) and osmotic shock (Protocol 2). HaCaT keratinocytes were cultured with/without sodium dodecyl sulfate (SDS) and used to test the hypothesis that SDS might be associated with the initiation and development of malignancies. Protocol 1 increased sensitivity and coverage of HaCaT proteome, it permitted us to reveal the provided new insights into the skin impact of SDS (widely used and rather non-toxic component of household chemicals, cosmetic products, shampoos and so on). Our results suggest the possible role of SDS in skin cancerogenesis.

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