| Glutathione (GSH, ) is an antioxidant in plants, animals, fungi, and some bacteria and archaea. Glutathione is capable of preventing damage to important cellular components caused by reactive oxygen species such as free radicals, peroxides, lipid peroxides, and heavy metals. It is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine. The carboxyl group of the cysteine residue is attached by normal peptide linkage to glycine. |
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InChI=1S/C10H17N3O6S/c11- 5(10(18) 19) 1- 2- 7(14) 13- 6(4- 20) 9(17) 12- 3- 8(15) 16/h5- 6,20H,1- 4,11H2,(H,12,17) (H,13,14) (H,15,16) (H,18,19) /t5- ,6- /m0/s1 |
| RWSXRVCMGQZWBV-WDSKDSINSA-N |
| N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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See:
PubMed
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antioxidant
A substance that opposes oxidation or inhibits reactions brought about by dioxygen or peroxides.
Bronsted base
A molecular entity capable of accepting a hydron from a donor (Bronsted acid).
(via organic amino compound )
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Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
cofactor
An organic molecule or ion (usually a metal ion) that is required by an enzyme for its activity. It may be attached either loosely (coenzyme) or tightly (prosthetic group).
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geroprotector
Any compound that supports healthy aging, slows the biological aging process, or extends lifespan.
skin lightening agent
Any cosmetic used to lighten the colour of skin by reducing the concentration of melanin.
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View more via ChEBI Ontology
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L-γ-glutamyl-L-cysteinylglycine
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5-L-Glutamyl-L-cysteinylglycine
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KEGG COMPOUND
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gamma-L-Glutamyl-L-cysteinyl-glycine
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KEGG COMPOUND
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Glutathione
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KEGG COMPOUND
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Glutathione-SH
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HMDB
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GSH
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KEGG COMPOUND
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N-(N-gamma-L-Glutamyl-L-cysteinyl)glycine
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KEGG COMPOUND
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Reduced glutathione
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KEGG COMPOUND
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111188
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ChemSpider
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1312
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DrugCentral
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C00001518
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KNApSAcK
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C00051
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KEGG COMPOUND
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D00014
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KEGG DRUG
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DB00143
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DrugBank
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FDB001498
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FooDB
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Glutathione
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Wikipedia
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GLUTATHIONE
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MetaCyc
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GSH
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PDBeChem
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HMDB0000125
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HMDB
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| View more database links |
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1729812
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Reaxys Registry Number
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Reaxys
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70-18-8
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CAS Registry Number
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KEGG COMPOUND
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70-18-8
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CAS Registry Number
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ChemIDplus
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Shibamura A, Ikeda T, Nishikawa Y (2009) A method for oral administration of hydrophilic substances to Caenorhabditis elegans: Effects of oral supplementation with antioxidants on the nematode lifespan. Mechanisms of ageing and development 130, 652-655 [PubMed:19580823] [show Abstract] Numerous studies using Caenorhabditis elegans have used a protocol in which chemicals are orally delivered by incorporating them into the nematode growth media or mixing them with the food bacteria. However, actual exposure levels are difficult to estimate as they are influenced by both the rates of ingestion into the intestine as well as absorption from the intestinal lumen. We used liposomes loaded with the hydrophilic fluorescent reagent uranin to test oral administration of water-soluble substances to C. elegans. Ingestion of liposomes loaded with fluorescent dye resulted in successful oral delivery of chemicals into the intestines of C. elegans. Using liposomes, oral administration of hydrophilic antioxidants (ascorbic acid, N-acetyl-cysteine, reduced glutathione, and thioproline) prolonged the lifespan of the nematodes, whereas the conventional method of delivery showed neither fluorescence nor longevity effects. Our method efficiently and quantitatively delivers solutes to nematodes. | Castrillo JI, Zeef LA, Hoyle DC, Zhang N, Hayes A, Gardner DC, Cornell MJ, Petty J, Hakes L, Wardleworth L, Rash B, Brown M, Dunn WB, Broadhurst D, O'Donoghue K, Hester SS, Dunkley TP, Hart SR, Swainston N, Li P, Gaskell SJ, Paton NW, Lilley KS, Kell DB, Oliver SG (2007) Growth control of the eukaryote cell: a systems biology study in yeast. Journal of biology 6, 4 [PubMed:17439666] [show Abstract]
BackgroundCell growth underlies many key cellular and developmental processes, yet a limited number of studies have been carried out on cell-growth regulation. Comprehensive studies at the transcriptional, proteomic and metabolic levels under defined controlled conditions are currently lacking.ResultsMetabolic control analysis is being exploited in a systems biology study of the eukaryotic cell. Using chemostat culture, we have measured the impact of changes in flux (growth rate) on the transcriptome, proteome, endometabolome and exometabolome of the yeast Saccharomyces cerevisiae. Each functional genomic level shows clear growth-rate-associated trends and discriminates between carbon-sufficient and carbon-limited conditions. Genes consistently and significantly upregulated with increasing growth rate are frequently essential and encode evolutionarily conserved proteins of known function that participate in many protein-protein interactions. In contrast, more unknown, and fewer essential, genes are downregulated with increasing growth rate; their protein products rarely interact with one another. A large proportion of yeast genes under positive growth-rate control share orthologs with other eukaryotes, including humans. Significantly, transcription of genes encoding components of the TOR complex (a major controller of eukaryotic cell growth) is not subject to growth-rate regulation. Moreover, integrative studies reveal the extent and importance of post-transcriptional control, patterns of control of metabolic fluxes at the level of enzyme synthesis, and the relevance of specific enzymatic reactions in the control of metabolic fluxes during cell growth.ConclusionThis work constitutes a first comprehensive systems biology study on growth-rate control in the eukaryotic cell. The results have direct implications for advanced studies on cell growth, in vivo regulation of metabolic fluxes for comprehensive metabolic engineering, and for the design of genome-scale systems biology models of the eukaryotic cell. | Czeczot H, Scibior D, Skrzycki M, Podsiad M (2006) Glutathione and GSH-dependent enzymes in patients with liver cirrhosis and hepatocellular carcinoma. Acta biochimica Polonica 53, 237-242 [PubMed:16404476] [show Abstract] We investigated glutathione level, activities of selenium independent GSH peroxidase, selenium dependent GSH peroxidase, GSH S-transferase, GSH reductase and the rate of lipid peroxidation expressed as the level of malondialdehyde in liver tissues obtained from patients diagnosed with cirrhosis or hepatocellular carcinoma. GSH level was found to be lower in malignant tissues compared to adjacent normal tissues and it was higher in cancer than in cirrhotic tissue. Non-Se-GSH-Px activity was lower in cancer tissue compared with adjacent normal liver or cirrhotic tissue, while Se-GSH-Px activity in cancer was found to be similar to its activity in cirrhotic tissue and lower compared to control tissue. An increase in GST activity was observed in cirrhotic tissue compared with cancer tissue, whereas the GST activity in cancer was lower than in adjacent normal tissue. The activity of GSH-R was similar in cirrhotic and cancer tissues, but higher in cancer tissue compared to control liver tissue. An increased level of MDA was found in cancer tissue in comparison with control tissue, besides its level was higher in cancer tissue than in cirrhotic tissue. Our results show that the antioxidant system of cirrhosis and hepatocellular carcinoma is severely impaired. This is associated with changes of glutathione level and activities of GSH-dependent enzymes in liver tissue. GSH and enzymes cooperating with it are important factors in the process of liver diseases development. | Djurhuus R, Segadal K, Svardal AM (2006) Glutathione in blood cells decreases without DNA breaks after a simulated saturation dive to 250 msw. Aviation, space, and environmental medicine 77, 597-604 [PubMed:16780237] [show Abstract]
IntroductionSaturation diving involves exposure to high pressure and elevated oxygen level. The impact of cellular defense systems like glutathione in protecting cells against oxidative DNA damage seems unclear. The aim of the present study was, therefore, to investigate whether diving conditions would affect blood cell glutathione and thus alter the mononuclear cells' (MNC) susceptibility to oxidative DNA damage.MethodsEight subjects participated in a simulated saturation dive to 2.6 MPa (250 msw) lasting 19.3 d (0.8 d compression, 6.6 d bottom phase, 11.9 d decompression) breathing helium-oxygen with PO2 ranging from 35 to 70 kPa (3.5-7.0 msw). Blood samples collected before compression and after decompression were analyzed for glutathione content and single-stranded DNA breaks.ResultsThe results demonstrate for the first time that a simulated saturation dive decreased glutathione content in peripheral blood cells (32% decrease in MNC), and that the decrease was most pronounced in the erythrocytes (45%). Remarkably, no single-stranded DNA breaks could be detected in the MNC despite the low glutathione level.DiscussionThe results suggest that glutathione is a useful indicator of oxidative stress and that a low glutathione level represents no significant harm to the blood cells in the absence of other toxic agents. The lack of DNA strand breaks suggests that protection against oxidative DNA damage was mainly provided by mechanisms other than the glutathione system. Although previous investigations point to hyperoxia as the most plausible explanation for the present observations, the effect of high pressure cannot be excluded. | Calvo-Marzal P, Chumbimuni-Torres KY, Höehr NF, Kubota LT (2006) Determination of glutathione in hemolysed erythrocyte with amperometric sensor based on TTF-TCNQ. Clinica chimica acta; international journal of clinical chemistry 371, 152-158 [PubMed:16650398] [show Abstract]
BackgroundGSH has a relevant role in human metabolism as an indicator of disease risks. An amperometric sensor for glutathione (GSH) determination is described as an alternative method featuring simple construction procedure and short time analysis.MethodThe developed sensor was used to determine glutathione at low potential using a TTF-TCNQ complex.ResultsThe sensor exhibits a linear response range from 5 to 340 micromol/l under applied potential of 200 mV vs. SCE. The sensitivity and detection limit were 90.1 microA l/mmol cm(2) and 0.3 micromol/l, respectively.ConclusionWhen the sensor was tested in hemolysed erythrocyte samples for GSH determination, a good correlation in results was observed between the sensor and the spectrophotometric method. The sensor showed recovery values between 98% and 102%. | Schulpis KH, Papassotiriou I, Parthimos T, Tsakiris T, Tsakiris S (2006) The effect of L-cysteine and glutathione on inhibition of Na+, K+-ATPase activity by aspartame metabolites in human erythrocyte membrane. European journal of clinical nutrition 60, 593-597 [PubMed:16391576] [show Abstract]
BackgroundReports have implicated Aspartame (N-L-a-aspartyl-L-phenylalanine methyl ester, ASP) in neurological problems.AimTo evaluate Na(+), K(+)-ATPase activities in human erythrocyte membranes after incubation with the ASP metabolites, phenylalanine (Phe), methanol (MeOH) and aspartic acid (Asp).MethodsErythrocyte membranes were obtained from 12 healthy individuals and were incubated at 37 degrees C for 1 h with the sum or each of the ASP metabolites separately, which are commonly measured in blood after ASP ingestion. Na(+), K(+)-ATPase and Mg(2+)-ATPase activities were measured spectrophotometrically.ResultsMembrane Mg(2+)-ATPase activity was not altered. The sum of ASP metabolite concentrations corresponding to 34, 150 or 200 mg/kg of the sweetener ingestion resulted in an inhibition of the membrane Na(+), K(+)-ATPase by -30, -40, -48%, respectively. MeOH concentrations of 0.14, 0.60 or 0.80 mM decreased the enzyme activity by -25, -38, -43%, respectively. Asp concentrations of 2.80, 7.60 or 10.0 mM inhibited membrane Na(+), K(+)-ATPase by -26, -40, -46%, respectively. Phe concentrations of 0.14, 0.35 or 0.50 mM reduced the enzyme activity by -24, -44, -48%, respectively. Preincubation with L-cysteine or reduced glutathione (GSH) completely or partially restored the inhibited membrane Na(+), K(+)-ATPase activity by high or toxic ASP metabolite concentrations.ConclusionsLow concentrations of ASP metabolites had no effect on Na(+), K(+)-ATPase activity. High or abuse concentrations of ASP hydrolysis products significantly decreased the membrane enzyme activity, which was completely or partially prevented by L-cysteine or reduced GSH. | Iwasaki Y, Hoshi M, Ito R, Saito K, Nakazawa H (2006) Analysis of glutathione and glutathione disulfide in human saliva using hydrophilic interaction chromatography with mass spectrometry. Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 839, 74-79 [PubMed:16621738] [show Abstract] A sensitive method for the determination of glutathione (GSH) and glutathione disulfide (GSSG) in human saliva was developed and validated. GSH was captured and stabilized by the addition of N-ethylmaleimide (NEM). Solid-phase extraction (SPE) using an Oasis MAX extraction cartridge was employed for sample preparation and analysis was performed on a Shimadzu LCMS-2010 A that was operated in the single ion monitoring mode using positive ion electrospray ionization (ESI) as the interface. The monitored ion for GSH-NEM was m/z 433 and that for GSSG was m/z 613. Chromatography was carried out on an Atlantis HILIC silica column (150 mm x 2.1 mm, 5 microm) with acetonitrile and formate buffer as the mobile phase at the flow rate of 0.2 ml/min. The calibration curve was linear over the range of 0.1-100 microM for GSH-NEM. The extraction recoveries of GSH-NEM spiked at concentrations of 25 and 50 microM were 97.1 and 104.4%, respectively. Similar results were obtained for GSSG. The newly developed hydrophilic interaction chromatography with mass spectrometry (HILIC/MS) method showed superior sensitivity for the determination of GSH and GSSG in human saliva samples. | Briz O, Romero MR, Martinez-Becerra P, Macias RI, Perez MJ, Jimenez F, San Martin FG, Marin JJ (2006) OATP8/1B3-mediated cotransport of bile acids and glutathione: an export pathway for organic anions from hepatocytes? The Journal of biological chemistry 281, 30326-30335 [PubMed:16877380] [show Abstract] In cholestasis, the accumulation of organic anions in hepatocytes is reduced by transporters (multidrug resistance-associated proteins and OSTalpha-OSTbeta) able to extrude them across the basolateral membrane. Here we investigated whether organic anion-transporting polypeptides (OATPs) may contribute to this function. Xenopus laevis oocytes expressing human carboxylesterase-1 efficiently loaded cholic acid (CA) methyl ester, which was cleaved to CA and exported. Expression of OATP8/1B3 enhanced CA efflux, which was trans-activated by taurocholate but trans-inhibited by reduced (GSH) and oxidized (GSSG) glutathione. Moreover, taurocholate and estradiol 17beta-D-glucuronide, but not bicarbonate and glutamate, cis-inhibited OATP8/1B3-mediated bile acid transport, whereas glutathione cis-stimulated this process, which involved the transport of glutathione itself with a stoichiometry of 2:1 (GSH/bile acid). No cis-activation by glutathione of OATP-C/1B1 was found. Using real time quantitative reverse transcription-PCR, the absolute abundance of OATP-A/1A2, OATP-C/1B1, and OATP8/1B3 mRNA in human liver biopsies was measured. In healthy liver, expression levels of OATP-C/1B1 were approximately 5-fold those of OATP8/1B3 and >100-fold those of OATP-A/1A2. This situation was not substantially modified in several cholestatic liver diseases studied here. In conclusion, although both OATP-C/1B1 and OATP8/1B3 are highly expressed, and able to transport bile acids, their mechanisms of action are different. OATP-C/1B1 may be involved in uptake processes, whereas OATP8/1B3 may mediate the extrusion of organic anions by symporting with glutathione as a normal route of exporting metabolites produced by hepatocytes or preventing their intracellular accumulation when their vectorial traffic toward the bile is impaired. | Kaynar H, Meral M, Turhan H, Keles M, Celik G, Akcay F (2005) Glutathione peroxidase, glutathione-S-transferase, catalase, xanthine oxidase, Cu-Zn superoxide dismutase activities, total glutathione, nitric oxide, and malondialdehyde levels in erythrocytes of patients with small cell and non-small cell lung cancer. Cancer letters 227, 133-139 [PubMed:16112416] [show Abstract] Lung cancer is a common pathology with high mortality due to late diagnosis. Glutathione peroxidase (GSH-Px), glutathione-S-transferase (GST), catalase (CAT), xanthine oxidase (XO), Cu-Zn superoxide dismutase (Cu-Zn SOD) activities, total glutathione (TGSH), nitric oxide (NO*), and malondialdehyde (MDA) levels were investigated in erythrocytes of patients with non-small-cell lung cancer (NSCLC) and small-cell lung cancer (SCLC), and healthy control group. We aimed to investigate serum GSH, GSH-dependent enzymes activities (GSH-Px and GST), XO, CAT, Cu-Zn SOD activity, and NO*, and MDA levels in patients with NSCLC and with SCLC and correlate with the cancer stage. Erythrocyte MDA, NO*, TGSH levels and erythrocyte SOD, CAT and XO activities were significantly higher in patients with NSCLC and SCLC than in controls. Slightly increased erythrocyte GSH-Px and GST activities were not significantly different from the controls. Erythrocyte MDA level positively correlated with erythrocyte NO* levels in patients with early stage (I+II) in NSCLC groups. Erythrocyte MDA level positively correlated with erythrocyte XO activity in patients with advanced stage (III+IV) in NSCLC groups. However, no other correlation could be found among the parameters in healthy controls and patients with NSCLC and with SCLC. Results obtained in this study indicate significant changes in antioxidant defence system in NSCLC and SCLC patients, which may lead to enhanced action of oxygen radical, resulting in lipid peroxidation. | Sohlenius-Sternbeck AK, Schmidt S (2005) Impaired glutathione-conjugating capacity by cryopreserved human and rat hepatocytes. Xenobiotica; the fate of foreign compounds in biological systems 35, 727-736 [PubMed:16316931] [show Abstract] The activity of glutathione transferase was measured in sonicates of fresh rat hepatocytes and of cryopreserved rat, human and dog hepatocytes in the presence of added glutathione and by using 1-chloro-2,4-dinitrobenzene (CDNB) as non-selective substrate. The glutathione-conjugating capacity was also investigated in the presence of CDNB alone (without glutathione) with intact fresh rat hepatocytes and cryopreserved rat and human hepatocytes. Finally, the intracellular level of glutathione was measured in these hepatocytes. The specific activity of glutathione transferase in sonicates of fresh rat hepatocytes (in the presence of added GSH and CDNB) was about 415 nmol/min/10(6) cells. The corresponding activities in cryopreserved rat, human and dog hepatocytes were approximately 320, 440 and 540 nmol/min/10(6) cells, respectively. In contrast, glutathione conjugation by the intact cryopreserved human and rat hepatocytes in the presence of CDNB alone was less than 10% of the corresponding conjugation by fresh rat hepatocytes, indicating that glutathione was depleted in these cryopreserved hepatocytes. Glutathione depletion was confirmed after analytical measurement of the glutathione levels in fresh and cryopreserved hepatocytes. In fresh rat hepatocytes the level of glutathione was 44 nmol/10(6) cells, whereas it was 2.5 and 4.4 nmol/10(6) cells in cryopreserved rat and human hepatocytes, respectively. In summary, glutathione transferase was active in these cryopreserved hepatocytes but the cryopreservation procedure likely causes depletion in the intracellular level of glutathione, resulting in an overall reduced glutathione conjugating capacity. | Wu G, Fang YZ, Yang S, Lupton JR, Turner ND (2004) Glutathione metabolism and its implications for health. The Journal of nutrition 134, 489-492 [PubMed:14988435] [show Abstract] Glutathione (gamma-glutamyl-cysteinyl-glycine; GSH) is the most abundant low-molecular-weight thiol, and GSH/glutathione disulfide is the major redox couple in animal cells. The synthesis of GSH from glutamate, cysteine, and glycine is catalyzed sequentially by two cytosolic enzymes, gamma-glutamylcysteine synthetase and GSH synthetase. Compelling evidence shows that GSH synthesis is regulated primarily by gamma-glutamylcysteine synthetase activity, cysteine availability, and GSH feedback inhibition. Animal and human studies demonstrate that adequate protein nutrition is crucial for the maintenance of GSH homeostasis. In addition, enteral or parenteral cystine, methionine, N-acetyl-cysteine, and L-2-oxothiazolidine-4-carboxylate are effective precursors of cysteine for tissue GSH synthesis. Glutathione plays important roles in antioxidant defense, nutrient metabolism, and regulation of cellular events (including gene expression, DNA and protein synthesis, cell proliferation and apoptosis, signal transduction, cytokine production and immune response, and protein glutathionylation). Glutathione deficiency contributes to oxidative stress, which plays a key role in aging and the pathogenesis of many diseases (including kwashiorkor, seizure, Alzheimer's disease, Parkinson's disease, liver disease, cystic fibrosis, sickle cell anemia, HIV, AIDS, cancer, heart attack, stroke, and diabetes). New knowledge of the nutritional regulation of GSH metabolism is critical for the development of effective strategies to improve health and to treat these diseases. | Morrison JA, Jacobsen DW, Sprecher DL, Robinson K, Khoury P, Daniels SR (1999) Serum glutathione in adolescent males predicts parental coronary heart disease. Circulation 100, 2244-2247 [PubMed:10577998] [show Abstract]
BackgroundTraditional risk factors account for only half of the morbidity and mortality from coronary heart disease (CHD). There is substantial evidence that oxidative injury plays a major role in the atherosclerotic process. Thus, antioxidants may protect against development of atherosclerosis. Glutathione, an intracellular tripeptide with antioxidant properties, may be protective.Methods and resultsThis case-control study compared total serum glutathione (tGSH) in 81 adolescent male offspring of parents with premature CHD (ie, before 56 years of age) and 78 control male offspring of parents without known or suspected CHD. Case offspring had significantly lower tGSH than control offspring. In multiple logistic regression with parental CHD status as the dependent variable, age entered as a covariate, and other CHD risk factors competing to enter the model as significant independent predictor variables, LDL cholesterol (odds ratio [OR], 2.15 [units=1.5 SD]; 95% CI, 1.21 to 3.82), tGSH (OR, 0.40; 95% CI, 0.22 to 0.71), HDL cholesterol (OR, 0.42; 95% CI, 0.22 to 0.78), and total serum homocysteine (OR, 2.6; 95% CI, 1.35 to 5.02) entered the model as significant predictors of parental CHD status.ConclusionsLow tGSH in adolescent boys is a significant independent predictor of parental CHD, in addition to elevated LDL cholesterol, low HDL cholesterol, and elevated total serum homocysteine concentrations. | Yim CY, Hibbs JB, McGregor JR, Galinsky RE, Samlowski WE (1994) Use of N-acetyl cysteine to increase intracellular glutathione during the induction of antitumor responses by IL-2. Journal of immunology (Baltimore, Md. : 1950) 152, 5796-5805 [PubMed:8207209] [show Abstract] IL-2 therapy can induce marked oxidative stress via reactive oxygen and nitrogen intermediates. Glutathione, the major intracellular reductant, may become rate limiting to cytotoxic lymphocyte activation and proliferation under these circumstances. N-Acetyl cysteine (NAc-cys) was used to increase intracellular glutathione levels during lymphokine-activated killer (LAK) cell activation by IL-2. Incubation of splenocytes with NAc-cys (0.6 to 1.0 mM) resulted in significant changes in intracellular reduced and total glutathione (92% and 58% increase, respectively) at 96 h. These levels correlated with markedly enhanced cell proliferation (threefold) and cytolytic effector cell generation (> fivefold increase in LU/10(6) cells) induced by the combination of NAc-cys with IL-2. IL-2 exposure by itself unexpectedly increased intracellular reduced glutathione by 43%. IL-2 and NAc-cys were synergistic in increasing glutathione levels (reduced glutathione: 292% increase; total: 251% increase). Inhibition of glutathione synthesis, using L-buthionine-(S,R)-sulfoximine reversed the effects of NAc-cys on intracellular glutathione, as well as cellular proliferation and cytotoxicity. This experiment established that the effects of NAc-cys required de novo glutathione synthesis. In conjunction with IL-2/LAK treatment, oral NAc-cys administration (260 to 900 mg/kg/day for 7 days) significantly decreased tumor progression in a refractory s.c. tumor model. A small fraction of mice (11 to 17%) had complete tumor regressions. NAc-cys may be useful as an adjunct to increase the antitumor activity of IL-2/LAK therapy. | Witschi A, Reddy S, Stofer B, Lauterburg BH (1992) The systemic availability of oral glutathione. European journal of clinical pharmacology 43, 667-669 [PubMed:1362956] [show Abstract] When the plasma glutathione concentration is low, such as in patients with HIV infection, alcoholics, and patients with cirrhosis, increasing the availability of circulating glutathione by oral administration might be of therapeutic benefit. To assess the feasibility of supplementing oral glutathione we have determined the systemic availability of glutathione in 7 healthy volunteers. The basal concentrations of glutathione, cysteine, and glutamate in plasma were 6.2, 8.3, and 54 mumol.l-1 respectively. During the 270 min after the administration of glutathione in a dose of 0.15 mmol.kg-1 the concentrations of glutathione, cysteine, and glutamate in plasma did not increase significantly, suggesting that the systemic availability of glutathione is negligible in man. Because of hydrolysis of glutathione by intestinal and hepatic gamma-glutamyltransferase, dietary glutathione is not a major determinant of circulating glutathione, and it is not possible to increase circulating glutathione to a clinically beneficial extent by the oral administration of a single dose of 3 g of glutathione. | Uotila L (1973) Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver. Biochemistry 12, 3944-3951 [PubMed:4745654] | Uotila L (1973) Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. Biochemistry 12, 3938-3943 [PubMed:4200890] |
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