Gene expression data from HepG2 cell treated with glutathione (GSH)
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ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: GSE242415 | GEO | 2024/03/20
REPOSITORIES: GEO
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Project description:Gene expression data from HepG2 cell treated with glutathione (GSH)
| PRJNA1013183 | ENA
Project description:An excess of reactive oxygen species (ROS) can cause severe oxidative damage to cellular components in photosynthetic cells. Antioxidant systems, such as the ascorbate-glutathione cycle, regulate redox status in cells to guard against such damage. Dehydroascorbate reductase (DHAR, EC 1.8.5.1) catalyzes the glutathione-dependent reduction of oxidized ascorbate (dehydroascorbate) and contains a redox active site and glutathione binding-site. The DHAR gene is important in biological and abiotic stress responses involving reduction of the oxidative damage caused by ROS. In this study, a transgenic microalgae (TA) strain was constructed by cloning the Oryza sativa L. japonica DHAR (OsDHAR) gene controlled by an isopropyl β-D-1-thiogalactopyranoside (IPTG)-inducible promoter (Ptrc) into the Synechococcus elongatus PCC 7942 strain of cyanobacteria to study the functional activities of OsDHAR under oxidative stress caused by hydrogen peroxide exposure. OsDHAR expression increased the growth of S. elongatus PCC 7942 under oxidative stress by reducing the levels of hydroperoxides and malondialdehyde (MDA) and mitigating the loss of chlorophyll. DHAR and glutathione S-transferase activity were higher than in the wild-type (WT) strain. Additionally, overexpression of OsDHAR in S. elongatus PCC 7942 greatly increased the glutathione (GSH)/glutathione disulfide (GSSG) ratio compared to ascorbic acid (AsA)/dehydroascorbate (DHA) ratio in the presence or absence of hydrogen peroxide. These results strongly suggest that DHAR attenuates deleterious oxidative effects via the glutathione (GSH)-dependent antioxidant system in cyanobacterial cells. The expression of heterologous OsDHAR in S. elongatus PCC 7942 protected cells from oxidative damage through a GSH-dependent antioxidant system via GSH-dependent reactions at the redox active site and GSH binding site residues during oxidative stress.
2019-11-25 | GSE140121 | GEO
Project description:Oxidative stress caused by Menadione or Hydrogen peroxide in synchronized Saccharomyces cerevisiae cultures. Alpha factor synchronized cultures (0.2-0.4 OD), treated at the beginning of S phase (25 min after release from G1 arrest) with either 2 mM Menadione (MD) or 0.24 mM Hydrogen peroxide (HP), show cell cycle effects. Cells treated with MD arrested at G1. Cells treated with HP delayed at S and then, after removal of HP at 135 minutes , continued the cell cycle, only to arrest at G2/M. Growth was carried out in 30C with shaking (295 rpm). Two time course experiments were performed with each oxidative stress agent, designated as H2O2 and H2O2_II, MD and MD_II. Keywords = oxidative stress Keywords = menadione Keywords = hydrogen peroxide Keywords = time course Keywords = cell cycle Keywords = yeast Keywords: other
2005-02-04 | GSE2239 | GEO
Project description:Oxidative stress caused by Menadione or Hydrogen peroxide in synchronized Saccharomyces cerevisiae cultures. Alpha factor synchronized cultures (0.2-0.4 OD), treated at the beginning of S phase (25 min after release from G1 arrest) with either 2 mM Menadione (MD) or 0.24 mM Hydrogen peroxide (HP), show cell cycle effects. Cells treated with MD arrested at G1. Cells treated with HP delayed at S and then, after removal of HP at 135 minutes , continued the cell cycle, only to arrest at G2/M. Growth was carried out in 30C with shaking (295 rpm). Two time course experiments were performed with each oxidative stress agent, designated as H2O2 and H2O2_II, MD and MD_II. Keywords = oxidative stress Keywords = menadione Keywords = hydrogen peroxide Keywords = time course Keywords = cell cycle Keywords = yeast
2005-02-04 | E-GEOD-2239 | biostudies-arrayexpress
Project description:Oxidative stress is harmful for organism and occurs when the cells exposed to superoxid, hydrogen peroxide and alkylhydroperoxides. In microorganism, the glutathione- and thioredoxin-dependent reduction systems are universal and play an important role in response to defending oxidative stress. The _-glutamylcysteine synthetase (_-GCS) is an essential enzyme to biosynthesize the tripeptide glutathione (GSH) in organism. Similarly, thioredoxin reductase is an important enzyme in thioredoxin-dependent reduction system. In Clostridium acetobutylicum, the _-glutamylcysteine synthetase (encoded by CAC1539, gcs) and thioredoxin reductase (encoded by CAC1548, trxB) were inactivated using ClosTron technology. The gcs mutant grew insufficiently and consumed less glucose in the phosphate-limited continuous culture and exhibited more sensitive to oxidative stress. The trxB mutant just exhibited lower growth rate and less glucose uptake in the solventogenic phase, compared to wild type. The DNA microarrays were performed to investigate the transcripome difference between wild type and the mutants. In gcs mutant, the genes related to chemotaxis and flagella biosynthesis proteins were induced significantly and in the trxB mutant, the sporulation genes were induced largely. Based on the phenotypes and transcriptome comparison results, the relationship between GSH- and Trx-dependent induction systems was discussed in Clostridium acetobutylicum.
2015-04-13 | E-MTAB-2747 | biostudies-arrayexpress
Project description:Expression profiling of wild type E. coli K-12 strain MG1655 with exogenous glutathione (GSH) supplementation, sub-inhibitory ciprofloxacin concentration and GSH with inhibitory ciprofloxacin concentration. We used microarrays to detail the global gene expression program underlying ciprofloxacin exposure and glutathione mediated abrogation of ciprofloxacin's anti-bacterial action.
2018-01-29 | GSE93896 | GEO
Project description:Glutathione (GSH) is a tripeptide involved in controlling heavy metal movement in plants. Our previous study demonstrated that GSH, applied to plant roots site-specifically, inhibited Cd translocation from roots to shoots in oilseed rape plants (Brassica napus) cultured hydroponically. One of the factors of this inhibitory effect was due to activation of Cd efflux from root cells. To investigate the molecular mechanism triggered by root applied GSH in more detail, the Cd movement was monitored non-invasively using a positron-emitting tracer imaging system (PETIS). The Cd absorption and efflux process in roots were visualized successfully. The effects of GSH on Cd efflux from root cells were estimated by analyzing obtained imaging data. Another image analysis suggested that Cd return was activated by GSH, applied to roots, at the shoot base. Cutting the shoot base of oilseed rape plants significantly inhibited Cd efflux from root cells. These experimental results demonstrated the shoot base is playing important roles in distributing Cd in the plant bodies. Furthermore, DNA microarray analysis revealed that over 300 genes in the roots of oilseed rape plants responded to root applied GSH. Among them, transporter proteins, related to heavy metal movement in plants, and proteins related to changing the structure of cell walls were involved.
2021-03-11 | GSE144768 | GEO
Project description:Regulatory T cells (Tregs) maintain immune homeostasis and prevent autoimmunity. Serine can stimulate glutathione (GSH) synthesis and feeds into the one-carbon metabolic cycle essential for effector T cell (Teff) responses. However, serine’s functions, linkage to GSH, and role in stress responses in Tregs are unknown. Here we show, using mice with Treg-specific ablation of the catalytic subunit of glutamate cysteine ligase (Gclc), that GSH loss in Tregs alters serine import and synthesis, and that the integrity of this feedback loop is critical for Treg suppressive capacity. Although Gclc-ablation does not impair Treg differentiation, the mutant mice develop severe spontaneous autoimmunity and show enhanced anti-tumor responses. Gclc-deficient Tregs exhibit increased serine metabolism, mTOR activation and proliferation but FoxP3 was downregulated. Limitation of cellular serine in vitro and in vivo restores FoxP3 expression and suppressive capacity to Gclc-deficient Tregs. Our work reveals an unexpected role for GSH in restricting serine availability to preserve Treg functionality.
2020-04-01 | GSE145311 | GEO
Project description:The essential thiol antioxidant, glutathione (GSH) is recruited into the nucleus of mammalian cells early in cell proliferation, suggesting a key role of the nuclear thiol pool in cell cycle regulation. However, the functions of nuclear GSH (GSHn) and its integration with the cytoplasmic GSH (GSHc) pools in whole cell redox homeostasis and signaling are unknown. Here we show that GSH is recruited into the nucleus early in cell proliferation in Arabidopsis thaliana, confirming the requirement for localization of GSH in the nucleus as a universal feature of cell cycle regulation. GSH accumulation in the nucleus was triggered by treatments that synchronize cells at G1/S as identified by flow cytometry and marker transcripts. Significant decreases in transcripts associated with oxidative signaling and stress tolerance occurred when GSH was localized in the nucleus. Increases in GSH1 and GSH2 transcripts accompanied the large increase in total cellular GSH observed during cell proliferation, but only GSH2 was differentially expressed in cells with high GSHn relative to those with an even intracellular distribution of GSH. Of the 7 Bcl-2 associated (BAG) genes in A. thaliana, only the nuclear-localized BAG 6 was differentially expressed in cells with high GSHn compared to GSHc. We conclude that GSHn is associated with decreased oxidative signaling and stress responses and that whole cell redox homeostasis is restored as the cell cycle progresses by enhanced GSH synthesis and accumulation in the cytoplasm. Arabidopsis cells were harvested at points during cell proliferation where GSH was localized either in the nucleus (GSHn) or where GSH was distributed throughout the cytoplasm (GSHc) for RNA extraction and hybridization on Affymetrix microarrays. We selected three stages where the GSH was into the nucleus and three stages where the GSH was distributed throughout the cells.
2010-02-27 | E-GEOD-20454 | biostudies-arrayexpress
Project description:Investigated protein glutathionylation in HL-1 cardiomyocyte cells in response to hydrogen peroxide using a clickable glutathione approach. After exposure, or not, to hydrogen peroxide the glutathionylated proteins with heavy or light azido glutathione were enriched and subjected to LC-MS/MS analysis followed by quantification.
2021-09-08 | PXD014937 | Pride