diethyl-maleate and gamma-glutamylcysteine

diethyl-maleate has been researched along with gamma-glutamylcysteine* in 2 studies

Other Studies

2 other study(ies) available for diethyl-maleate and gamma-glutamylcysteine

ArticleYear
Non-linear impact of glutathione depletion on C. elegans life span and stress resistance.
    Redox biology, 2017, Volume: 11

    The redox environment in cells and organisms is set by low-molecular mass and protein-bound thiols, with glutathione (GSH) representing a major intracellular redox buffer. Subtle thiol oxidation elicits signal transduction processes and adaptive responses to cope with stressors, whereas highly oxidizing conditions may provoke cell death. We here tested how thiol depletion affects life span, stress resistance and stress signaling in the model organism Caenorhabditis elegans. Diethyl maleate (DEM), an α,β-unsaturated carbonyl compound that conjugates to GSH and other thiols, decreased C. elegans life span at a concentration of 1mM. In contrast, low and moderate doses of DEM (10-100µM) increased mean and maximum life span and improved resistance against oxidative stress. DEM-induced life span extension was not detectable in worms deficient in either the FoxO orthologue, DAF-16, or the Nrf2 orthologue, SKN-1, pointing to a collaborative role of the two transcription factors in life span extension induced by thiol depletion. Cytoprotective target genes of DAF-16 and SKN-1 were upregulated after at least 3 days of exposure to 100µM DEM, but not 1mM DEM, whereas only 1mM DEM caused upregulation of egl-1, a gene controlled by a p53-orthologue, CEP-1. In order to test whether depletion of GSH may elicit effects similar to DEM, we suppressed GSH biosynthesis in worms by attenuating γ-glutamylcysteine synthetase (gcs-1) expression through RNAi. The decline in GSH levels elicited by gcs-1 knockdown starting at young adult stage did not impair viability, but increased both stress resistance and life expectancy of the worms. In contrast, gcs-1 knockdown commencing right after hatching impaired nematode stress resistance and rendered young adult worms prone to vulval ruptures during egg-laying. Thus, modest decrease in GSH levels in young adult worms may promote stress resistance and life span, whereas depletion of GSH is detrimental to freshly hatched and developing worms.

    Topics: Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Cell Death; Dipeptides; DNA-Binding Proteins; Forkhead Transcription Factors; Gene Expression Regulation, Developmental; Gene Knockdown Techniques; Glutamate-Cysteine Ligase; Glutathione; Maleates; Oxidation-Reduction; Oxidative Stress; Repressor Proteins; Sulfhydryl Compounds; Transcription Factors; Tumor Suppressor Protein p53

2017
Effect of oxygen on induction of the cystine transporter by bacterial lipopolysaccharide in mouse peritoneal macrophages.
    The Journal of biological chemistry, 2001, Mar-30, Volume: 276, Issue:13

    Amino acid transport in mouse peritoneal macrophages is mediated by several membrane carriers with different substrate specificity and sensitivity to environmental stimuli. We reported previously that transport activities of cystine and arginine in the macrophages were induced markedly by low concentrations of bacterial lipopolysaccharide (LPS). It is known that a variety of macrophage functions are affected by ambient oxygen tension. In this study, we have investigated the effects of oxygen on the induction of amino acid transport activity by LPS and found that the induction of cystine, but not arginine, transport activity was dependent on the ambient oxygen tension. When the macrophages were cultured with 2% O(2) in the presence of 1 ng/ml LPS, induction of cystine transport activity was reduced by approximately 70% compared with cells cultured under normoxic conditions. In macrophages, transport of cystine is mediated by a Na(+)-independent anionic amino acid transporter named system x(c)(-). System x(c)(-) is composed of two protein components, xCT and 4F2hc, and the expression of xCT was closely correlated with system x(c)(-) activity. A putative NF-kappaB binding site was found in the 5'-flanking region of the xCT gene, but the enhanced expression of xCT by LPS and oxygen was not mediated by NF-kappaB binding. An increase in intracellular GSH in macrophages paralleled induction of xCT, but not gamma-glutamylcysteine synthetase. These results suggest the importance of system x(c)(-) in antioxidant defense in macrophages exposed to LPS and oxidative stress.

    Topics: Amino Acids; Animals; Antioxidants; Base Sequence; Binding Sites; Biological Transport; Blotting, Northern; Cell Nucleus; Cystine; Dipeptides; Dose-Response Relationship, Drug; Female; Glutamate-Cysteine Ligase; Glutathione; Hypoxia; Lipopolysaccharides; Macrophages; Macrophages, Peritoneal; Maleates; Mice; Mice, Inbred C57BL; Mice, Knockout; Molecular Sequence Data; NF-kappa B; Oxidative Stress; Oxygen; RNA, Messenger; Signal Transduction; Time Factors

2001
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