Bradley, M.; Buecheler, U.S.; Walsh, C.T., 1991: Redox enzyme engineering conversion of human glutathione reductase into a trypanothione reductase
BioAssay record AID 75302 submitted by ChEMBL: Inhibitory activity against human glutathione reductase in presence of 100 uM GSSG; no inhibition up to 100 uM.
1BWC: Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies.
Looking for Glutathione reductase? Find out information about Glutathione reductase. see coenzyme coenzyme , any one of a group of relatively small organic molecules required for the catalytic function of certain enzymes. A coenzyme may... Explanation of Glutathione reductase
Glutathione is the most abundant thiol in the vast majority of organisms and is maintained in its reduced form by the flavoenzyme glutathione reductase. In this work, we describe the genetic and functional analysis of the Caenorhabditis elegans gsr-1 gene that encodes the only glutathione reductase protein in this model organism. By using green fluorescent protein reporters we demonstrate that gsr-1 produces two GSR-1 isoforms, one located in the cytoplasm and one in the mitochondria. gsr-1 loss of function mutants display a fully penetrant embryonic lethal phenotype characterized by a progressive and robust cell division delay accompanied by an aberrant distribution of interphasic chromatin in the periphery of the cell nucleus. Maternally expressed GSR-1 is sufficient to support embryonic development but these animals are short-lived, sensitized to chemical stress and have increased mitochondrial fragmentation and lower mitochondrial DNA content. Furthermore, the embryonic lethality of gsr-1 ...
Glutathione reductase (Gsr) is an enzyme that reduces glutathione disulfide to the sulfhydryl form, a major cellular antioxidant. Oxidative burst plays an important role in pathogen killing and initiation of inflammation. Proper redox regulation is crucial for balancing effective pathogen elimination and host preservation. We tested the hypothesis that Gsr plays a critical role in host defense by comparing wildtype (WT) and Gsr- mice after E. coli infection. Compared to WT mice, Gsr- mice exhibited substantially higher mortality, associated with greater bacterial burden, cytokine storm, and striking histological abnormalities. Surprisingly, Gsr- mice displayed increased resistance to LPS. While Gsr- mice exhibited defects in phagocyte mobilization, there appeared no substantial defects in either cell signaling or cytokine production in Gsr- macrophages. The role of Gsr in phagocytic oxidative burst was assessed by both flow cytometry and bioluminescence imaging. The oxidative burst in WT ...
The isoproturon is a systemic herbicide applied in pre- and post-emergence control of annual grasses and broad-leaved weeds in winter crops that block photosynthesis, being listed by European Union as special substance that threaten the earth surface. Probably, can generate reactive oxygen species blocking the respiratory chain and cause oxidative stress and cell death. So, the main purpose of this study was to evaluate the effect of isoproturon on the antioxidant capacity of the wild-type Saccharomyces cerevisiae UE-ME3 and IGC-4072 strains. The UE-ME3 strain showed an adaptive response to this phenylurea, showing a growth similar to that control cells, an increase of non-protein thiols content, cell viability and glutathione antioxidant capacity, response that depend on glutathione reductase and glucose-6-phosphate dehydrogenase activities. However, the IGC-4072 strain in the presence of isoproturon showed cell death, exhibiting a poorly growth, dry weight and cell viability decrease, as well ...
Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione ...
Glutathione Reductase tagged: signaling, biochemistry, redox systems, nadph, nadp, gssg, gsh, cellular redox systems, cellular reduction and oxidation, glutathione disulfide, powerpoint, slide
Oxford Biomedicals Glutathione Reductase Assay Kit is used to maintain a high GSH/GSSG ratio, which is essential for protection against oxidative stress.
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A cDNA for pea glutathione reductase has been cloned and sequenced. The derived amino acid sequence of 562 residues shows a high degree of homology to the previously published GR sequences from human erythrocytes and from two prokaryotes: Escherichia coli and Pseudomonas aeruginosa. The pea enzyme differs from other GRs in having an M-terminal leader sequence of about 60-70 residues which may be a chloroplast transit peptide and a 20 amino acid C-terminal extension of unknown function.. ...
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Gsr catalyzes the reduction of glutathione disulfide to glutathione, a major cellular antioxidant. Paradoxically, Gsr-deficient neutrophils are impaired in their oxidative burst and produce less ROS (Figs. 6, 7). Although the exact mechanisms involved remain unclear, we can offer some speculations. One might argue that deficiency of Gsr in the germ line of the mutant mice might trigger a compensatory antioxidant response, augmenting the cellular oxidative defense mechanisms, which in turn would decrease the net production of ROS in the Gsr-deficient phagocytes. Although we cannot rule out this possibility, we think this postulate is less likely. First, the pharmacological inhibitor BCNU abolished the oxidative burst in wild-type cells (Fig. 6D). It is unlikely that a short pretreatment of wild-type phagocytes with BCNU would trigger a compensatory antioxidant response. Second, a stronger antioxidant compensatory mechanism cannot explain the decrease in HMPS activity in the Gsr-deficient ...
0164] Holleschau and Rathbun (1994), The effects of age on glutathione peroxidase and glutathione reductase activities in lenses of Old World simians and prosimians (PubMed) ...
The disulfide reducing activities of GSSG-and CoASSG-reductases were measured on partially purified extracts from a variety of prokaryotes and eukaryotes. Glutathione-reductase was found in varying...
1GRF: Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution.
... ,Origami host strains are K-12 derivatives that have mutations in both the thioredoxin reductase (trxB) and glutathione reductase (gor) genes, which greatly enhances disulfide bond formation in the cytoplasm. Studies have shown that expression in Origami(DE3) yielded 10-fold more active protein than,biological,biology supply,biology supplies,biology product
pep:known chromosome:VEGA66:8:33653238:33698163:1 gene:OTTMUSG00000016634 transcript:OTTMUST00000040242 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Gsr description:glutathione reductase 1 ...
SWISS-MODEL Template Library (SMTL) entry for 1gre.1. SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION
SWISS-MODEL Template Library (SMTL) entry for 1grf.1. SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION
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Enzymatic activities of glutathione peroxidase, glutathione-S-transferase, glutathione reductase and catalase, as well as the glutathione content were measured in the brain tissue of regularly cycling rats at dioestrus, proestrus and estrus. The activity of glutathione peroxidase was found to be suppressed at proestrus, whereas that of catalase was increased at dioestrus. Glutathione transferase and glutathione reductase activities, as well as the glutathione content appeared to be stable during the oestrous cycle. These results suggest that, in the female rat, glutathione peroxidase and catalase activities in the brain tissue are influenced by the ovarian hormone status ...
Abstract: In all 5 acute (AVHs) and chronic viral hepatites (CVHs) there was the increase of erythrocyte activities of glutathione peroxidase (GPx) and glutathione reductase (GR), and the decrerase in GSH concentration. In blood plasma there was accumulation of GPx, glutathione S-transferase (GST) and γ-glutamyl transferase (γGT). GSH and GR increased in plasma only in AVHs. In CVH C erythrocyte GST increased. Evidently changes in the erythrocyte glutathione system are reactions to oxidative stress and in blood plasma they are consequences of inflammation and hepatocyte cytolysis. Changes were more pronounced in middle-heavy course than in the heavy one. These changes have pathogenic importance and can be used in addition to complex diagnostics. They are significantly differed from changes in chronic gall-bladder diseases. Necessity of separate investigation of glutathione system in erythrocytes and blood plasma but not in whole blood is argued ...
Glutathione reductase (GR) catalyzes the reduction of glutathione disulfide, which helps to maintain a cellular reducing environment during stress in organisms. However, GR of polar yeast has not...
Glutathione helps protect cells from free radical damage by acting as an antioxidant. Within cells, glutathione exists in reduced (GSH) and oxidized (GSSG) states. In healthy cells and tissue, more than 90% of the pool is in the reduced form (GSH) while less than 10% exists in the disulfide form (GSSG). The GSH form acts as an electron donor and is thereby oxidized itself to the GSSG form. Glutathione reductase is a homodimeric enzyme that is a member of the flavoprotein disulfide oxidoreductases. Glutathione Reductase reduces oxidized glutathione (GSSG) back to reduced glutathione (GSH) in the presence of NADPH.
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The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase.
Nonlinear regression methods in design of experiments and mathematical modelling. Applications to the analysis of the steady-state kinetics of glutathione reductase ...
Riboflavin status of 61 pregnant Chines women was investigated in a longitudinal study by functional assay of the coenzyme activation of erythrocyte glutathione reductase. maternal nonfasting venous blood was collected at 26 and 36 gestational weeks and weeks postpartum. At delivery, 27 pairs of maternal and cord blood samples were also...
The glutathione peroxidase-glutathione reductase system, an alternative pathway for metabolic utilization of H2O2 [Chance, Sies & Boveris (1979) Physiol. Rev. 59, 527-605], was investigated in Trypanosoma cruzi, an organism lacking catalase and deficient in peroxidase [Boveris & Stoppani (1977) Experientia 33, 1306-1308]. The presence of glutathione (4.9 +/- 0.7 nmol of reduced glutathione/10(8) cells) and NADPH-dependent glutathione reductase (5.3 +/- 0.4 munit/10(8) cells) was demonstrated in the cytosolic fraction of the parasite, but with H2O2 as substrate glutathione peroxidase activity could not be demonstrated in the same extracts. With t-butyl hydroperoxide or cumene hydroperoxide as substrate, a very low NADPH-dependent glutathione peroxidase activity was detected (equivalent to 0.3-0.5 munit of peroxidase/10(8) cells, or about 10% of glutathione reductase activity). Blank reactions of the glutathione peroxidase assay (non-enzymic oxidation of glutathione by hydroperoxides and enzymic ...
In the forebrain from male Wistar rats aged 5, 15 and 25 months, age-related putative alterations in the glutathione system (reduced and oxidized glutathione; redox index) were chronically induced by the administration in drinking water of free radical generators (hydrogen peroxide, ferrous chloride) or of inhibitors of endogenous free radical defenses (diethyl-dithio-carbamate, an inhibitor of superoxide dismutase activity). In hydrogen peroxide administered rats, both reduced glutathione and the cerebral glutathione redox index markedly declined as a function of aging, whereas oxidized glutathione consistently increased. In contrast, chronic iron intake failed to modify the reduced glutathione in forebrain from the rats of the different ages tested, whereas the oxidized glutathione was increased in the older brains. The chronic intake of diethyl-dithio-carbamate enhanced the concentrations of reduced glutathione in the forebrains from the rats of the different ages tested, the oxidized ...
Results Hyperzincuria and hypermagnesuria were evident in diabetic subjects compared with control subjects. There were no differences in plasma magnesium or whole-blood manganese between groups. Plasma copper was higher and plasma zinc was lower in diabetic than in control subjects. When data were viewed with respect to specific diabetes-associated complications, diabetic subjects with retinopathy, hypertension, or microvascular disease had higher plasma copper concentrations compared with both diabetic subjects without complications and with control subjects. There were no significant differences between control and diabetic subjects in erythrocyte copper-zinc superoxide dismutase activity or whole-blood glutathione peroxidase or glutathione reductase activities. Plasma peroxide concentrations were higher in diabetic than control subjects.. ...
The effect of endurance training on glutathione (GSH) status and antioxidant enzyme system was investigated in skeletal muscle, heart, and liver of female Sprague-Dawley rats pair fed an isocaloric diet. Ten weeks of treadmill training (25 m/min, 10% grade for 2 h/day, 5 days/wk) increased citrate synthase activity in the deep vastus lateralis (DVL) and soleus muscles by 79 and 39%, respectively (P , 0.01), but not in the heart or liver. In DVL, GSH content was increased 33% (P , 0.05) with training, accompanied by a 64% (P , 0.05) increase in glutamate content but no change in cysteine. Trained rats showed a 62 and 27% higher GSH peroxidase (GPX) and superoxide dismutase (SOD) activity, respectively (P , 0.05), in DVL compared with control rats. In contrast, GSH content and glutathione reductase (GR) activity in soleus declined with training (P , 0.05), whereas activities of GPX and SOD remained unchanged. Training did not alter GSH status in the liver or plasma but significantly decreased the ...
OUTLINE: Participants undergo blood sample collection. Samples are used to measure levels of antioxidant enzymes (i.e., glutathione, glutathione peroxidase, glutathione reductase, superoxide dismutase, and reduced glutathione) and biomarkers of oxidative stress and DNA damage in leukocytes (i.e., thiobarbituric acid reactive substances [TBARS] and 8-hydroxydeoxyguanosine). Samples are analyzed via antioxidant enzyme assay, TBARS assay, and enzyme-linked immunosorbent assay.. PROJECTED ACCRUAL: A total of 40 participants (20 at high risk for developing prostate cancer and 20 healthy controls) will be accrued for this study. ...
This study aims to evaluate the significance of the changes of erythrocyte reduced glutathione (GSH) in the course of diabetes mellitus including the pre-diabet
Rats fed aspartame (1000 mg/kg b.wt.) for 180 days showed significant increase in the activities of alanine aminotransferase (ALT), aspartate aminotransferase (AST), alkaline phosphatase (ALP) and γ-glutamyl transferase (GGT).. The activity of glutathione peroxidase (GPx), and glutathione reductase (GR) were significantly reduced in the liver.[1]. ...
GSH/GSSG Ratio Detection Assay (ab138881). Sensitivity |10 nM. Direct quantification of glutathione (GSH) with a green fluorescent dye. HTP ready.
Hello, Ive read here in several posts that oral glutathione is not recommended as it may cause a methyl-trap. My doc has put me on oral glutathione...
Glutathione Reporter provides extensive information, references to published scientific literature, on glutathione & its relationships with chronic diseases.
Cancer cells and normal cells are known to respond differently to nutrients and drugs that affect glutathione status. Numerous studies have shown that tumor cells have elevated levels of
Benefits of Glutathione is a blog that provides information on Glutathione (GSH) and its importance to the individual. Our main mission is to serve as a resource for people who want to learn more about GSH and its benefits. ...
The Genomics Shared Resource (GSR) is a core laboratory that has been supported in part by the CCSG since 1999. The purpose of the GSR laboratory is to provide...
Three pairs of parental (ρ+) and established mitochondrial DNA depleted (ρ0) cells, derived from bone, lung and muscle were used to verify the influence of the nuclear background and the lack of efficient mitochondrial respiratory chain on antioxidant defences and homeostasis of intracellular reactive oxygen species (ROS). Mitochondrial DNA depletion significantly lowered glutathione reductase activity, glutathione (GSH) content, and consistently altered the GSH2 : oxidized glutathione ratio in all of the ρ0 cell lines, albeit to differing extents, indicating the most oxidized redox state in bone ρ0 cells. Activity, as well as gene expression and protein content, of superoxide dismutase showed a decrease in bone and muscle ρ0 cell lines but not in lung ρ0 cells. GSH peroxidase activity was four times higher in all three ρ0 cell lines in comparison to the parental ρ+, suggesting that this may be a necessary adaptation for survival without a functional respiratory chain. Taken together, ...
Title:Glutathione-Related Factors and Oxidative Stress in Autism, A Review. VOLUME: 19 ISSUE: 23. Author(s):A. Ghanizadeh, S. Akhondzadeh, M. Hormozi, A. Makarem, M. Abotorabi-Zarchi and A. Firoozabadi. Affiliation:Research Center for Psychiatry and Behavioral Sciences, Department of Psychiatry, Hafez Hospital, Shiraz, Iran.. Keywords:Autism, oxidative stress, glutathione, treatment, inflammation, methylation, sulfate, spectrum disorders, neurobiology, therapeutic interventions. Abstract:Autism spectrum disorders are complex neuro-developmental disorders whose neurobiology is proposed to be associated with oxidative stress which is induced by reactive oxygen species. The process of oxidative stress can be a target for therapeutic interventions. In this study, we aimed to review the role of oxidative stress, plasma glutathione (GSH), and related factors as the potential sources of damage to the brain as well as the possible related factors which reduce the oxidative stress. Methylation capacity, ...
Glutathione exists in reduced (GSH) and oxidized (GSSG) states. In the reduced state, the thiol group of cysteine is able to donate a reducing equivalent (H++ e-) to other unstable molecules, such as reactive oxygen species. In donating an electron, glutathione itself becomes reactive, but readily reacts with another reactive glutathione to form glutathione disulfide (GSSG). Such a reaction is possible due to the relatively high concentration of glutathione in cells (up to 5 mM in the liver). GSH can be regenerated from GSSG by the enzyme glutathione reductase.. In healthy cells and tissue, more than 90% of the total glutathione pool is in the reduced form (GSH) and less than 10% exists in the disulfide form (GSSG). An increased GSSG-to-GSH ratio is considered indicative of oxidative stress.. GSH is known as a substrate in both conjugation reactions and reduction reactions, catalyzed by glutathione S-transferase enzymes in cytosol, microsomes, and mitochondria. However, it is also capable of ...
Glutathione peroxidase 4, also known as GPX4, is an enzyme that in humans is encoded by the GPX4 gene. GPX4 is a phospholipid hydroperoxidase that protects cells against membrane lipid peroxidation. The antioxidant enzyme glutathione peroxidase 4 (GPx4) belongs to the family of glutathione peroxidases, which consists of 8 known mammalian isoenzymes (GPx1-8). Gpx4 catalyzes the reduction of hydrogen peroxide, organic hydroperoxides, and lipid peroxides at the expense of reduced glutathione and functions in the protection of cells against oxidative stress. The oxidized form of glutathione (glutathione disulfide), which is generated during the reduction of hydroperoxides by GPx4, is recycled by glutathione reductase and NADPH/H+. GPx4 differs from the other GPx family members in terms of its monomeric structure, a less restricted dependence on glutathione as reducing substrate, and the ability to reduce lipid-hydroperoxides inside biological membranes. Inactivation of GPX4 leads to an accumulation ...
Aging is often associated with accumulation of oxidative damage in proteins and lipids. However, some studies do not support this view, raising the question of whether high levels of oxidative damage are associated with lifespan. In the current investigation, Drosophila melanogaster flies were kept on diets with 2 or 10% of either glucose or fructose. The lifespan, fecundity, and feeding as well as amounts of protein carbonyls (PC) and lipid peroxides (LOOH), activities of superoxide dismutase (SOD), catalase, glutathione-S-transferase (GST), and glutathione reductase activity of thioredoxin reductase (TrxR) were measured in "young" (10-day old) and "aged" (50-day old) flies. Flies maintained on diets with 10% carbohydrate lived longer than those on the 2% diets. However, neither lifespan nor fecundity was affected by the type of carbohydrate. The amount of PC was unaffected by diet and age, whereas flies fed on diets with 10% carbohydrate had about fivefold higher amounts of LOOH compared to ...
Glutathione exists in reduced (GSH) and oxidized (GSSG) states. In the reduced state, the thiol group of cysteine is able to donate a reducing equivalent (H++ e-) to other unstable molecules, such as reactive oxygen species. In donating an electron, glutathione itself becomes reactive, but readily reacts with another reactive glutathione to form glutathione disulfide (GSSG). Such a reaction is possible due to the relatively high concentration of glutathione in cells (up to 5 mM in the liver). GSH can be regenerated from GSSG by the enzyme glutathione reductase.. In healthy cells and tissue, more than 90% of the total glutathione pool is in the reduced form (GSH) and less than 10% exists in the disulfide form (GSSG). An increased GSSG-to-GSH ratio is considered indicative of oxidative stress.. GSH is known as a substrate in both conjugation reactions and reduction reactions, catalyzed by glutathione S-transferase enzymes in cytosol, microsomes, and mitochondria. However, it is also capable of ...