Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: KEGG:D00031 (Glutathione)
 5,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A chemically defined liquid medium has been developed for the study of the physiology and antigen production of the Legionnaires disease bacterium. The medium contains basal salts, vitamins, alpha-ketoglutaric acid, pyruvate, 0.05% l-cysteine, 0.05% glutathione, and a mixture of 20 additional amino acids, each of 0.01% final concentration, except serine, which was at 0.1%. The medium in shake culture at 37 degrees C with increased CO2 at pH 6.5, supports the maximum rate of growth, the highest cell yields, and the maximum cell surface antigen as distinguished by specific fluorescein isothiocyanate-conjugated antibody. Studies during the development of this medium showed that CO2, pyruvate, and alpha-ketoglutarate strongly stimulated growth; that cysteine and methionine were required for growth; and that serine, threonine, histidine, tyrosine, and tryptophane were energy sources. Glutathione substituted for cysteine, but cystine did not. The organisms did not use glucose and polysaccharides, as judged by cell yields when these carbohydrates were present or absent. The chelators malate, citrate, and ethylenediaminetetraacetic acid totally inhibited growth. Beta-mercaptoethanol, thioglycolate, dithiothreitol, and Tween 80 (0.05%) inhibited growth strongly or completely. Catalase activity was extremely weak or absent. Morphology varied, depending upon conditions and phases of growth. In general, filamentous forms became chains of cigar-shaped bacilli fragmenting to pairs and becoming coccoidal in the late stationary pha-e of growth. The organism grew at 25, 30, and 37 degrees C. Although they varied in their growth characteristics, 10 isolates were passed for five transfers in the chemically defined broth, giving maximum rates of growth, cell yields, and antigen production.
J Clin Microbiol 1979 May
PMID:Development of a chemically defined liquid medium for growth of Legionella pneumophila. 3 86

Glutathione reductase plays an important role in protecting hemoglobin, red cell enzymes, and biological cell membranes against oxidative damage by increasing the level of reduced glutathone (GSSGR) in the process of aerobic glycolysis. The enzyme deficiency may result in mild to moderately severe hemolytic anemia upon exposure to certain drugs or chemicals. However, hereditary deficiency of the enzyme is extremely rare. Recent studies on glutathione reductase in the red cell have shown more insight in the understanding of red cell metabolism and interactions with other enzymes, especially glucose-6-phosphate dehydrogenase (G-6-PD). Glutathione reducatase in serum may be a source of error in any clinical laboratory test in which an enzyme activity is determined indirectly by measuring the change in reduced nicotinamide-adenine dinucleotide (NADH) or reduced nicotinamide adenine dinucleotide phosphate (NADPH) absorbance. Glutathione reductase levels are reduced in banked blood when citrate-phosphate-dextrose (CPD) is used as a preservative. Reviewed is the role of glutathione reductase in the metabolism of the red cell and its clinical implication and usefulness.
Ann Clin Lab Sci
PMID:Glutathione reductase in the red blood cells. 62 27

The effects of reduced glutathione (GSH) administration (1.2 g/day and 2.4 g/day intravenously) on erythrocyte glutathione levels, serum gamma-glutamyl transpeptidase activity (GGTP) and urinary glucaric acid elimination were studied in a population of 24 chronic alcoholics voluntarily admitted to a 30 day detoxification protocol in comparison to a 12 patient control group treated only with chlordiazepoxide (initial dose 75-100 mg/day). Glutathione treatment increases dose-dependently and in a significant way erythrocyte glutathione levels and hastens the recovery of serum GGTP and urinary glucaric acid elimination. The relationship between glutathione, GGTP and glucaric acid is discussed, suggesting the possible role of GSH against the oxidative damage of alcohol.
Clin Ter 1992 May
PMID:[Contribution of glutathione to detoxification in alcoholism. Biochemical-clinical studies]. 135 98

Glutathione (GSH) and cysteine were determined in the plasma and the erythrocytes of alcoholic and non-alcoholic cirrhotics as fluorescent monobromobimane derivatives by high-performance liquid chromatography (HPLC). Cirrhotic patients displayed a significant decrease of plasma GSH, as well as of plasma cysteine, that was related to the degree of liver disease but not to the nutritional conditions. On the contrary, erythrocyte cysteine was found to increase significantly in all cirrhotics, particularly in alcoholics, regardless of the severity of disease. In an attempt to find a possible explanation of these alterations, the GSH synthesizing enzymes, gamma-glutamylcysteine synthetase (GC-s) and GSH synthetase (GSH-s) activities were determined in the erythrocytes. GSH-s activity was significantly lower in cirrhotic patients, whereas GC-s activity did not differ in the three groups.
Scand J Clin Lab Invest 1992 May
PMID:Alteration of erythrocyte glutathione, cysteine and glutathione synthetase in alcoholic and non-alcoholic cirrhosis. 141 Dec 53

Glutathione is one of the endogenous protective chemicals, like prostaglandins, in the gastric mucosa. Depletion of these agents aggravate the chemical- or stress-induced gastric erosions and ulcers. However, gastroprotection can be achieved even in the presence of low mucosal concentration of glutathione and prostaglandins, indicating the presence of other protective chemicals (e.g. polyamines, growth factors, neurotransmitters, steroids) in the stomach. Protein sulfhydryls were also implicated in the mechanism of action of gastroprotective drugs. We recently tested the hypothesis that cysteine proteases might be a target of gastroprotective and antiulcer agents, and decided to look for the presence of proteases and protease inhibitors (PI) in the gastric mucosa and juice. Protease activity and PI were measured with general substrates hemoglobin, azocasein and albumin at optimal pH (2.0, 5.6, 7.4) of aspartic, cysteine and serine proteases. Homogenates of glandular stomach mucosa and gastric juice from fasted rats were incubated in the presence or absence of specific inhibitors and gastroprotective SH alkylators such as NEM or iodoacetate. PI was measured after acid and heat inactivation of endogenous proteinases and addition of pepsin, cysteine proteinase papain, or trypsin. Our results indicate that of the proteases found in the stomach 98% was pepsin at pH 2.0, and up to 56% or 24% was SH-sensitive at pH 5.6 or 7.4, respectively. Intragastric administration of SH alkylators such as NEM or iodoacetate exerted a dose- and time-dependent gastroprotection against chemically induced acute erosions and ulcers. Thus, in addition to glutathione, proteinases and their specific endogenous inhibitors may also be involved in gastric mucosal injury and protection.
Clin Chim Acta 1992 Mar 13
PMID:Glutathione, protein sulfhydryls and cysteine proteases in gastric mucosal injury and protection. 157 83

Glutathione was measured in doxorubicin-sensitive cells from small cell carcinoma of lung (GLC4 210), and the levels compared with those of cells with acquired resistance and a line of resistant non-small-cell adenocarcinoma A549 (Alveolar type 2). The effect of different doxorubicin concentrations on glutathione were measured by HPLC. The effect of doxorubicin on the viability of the cell lines was studied using thiazole blue dye reduction. An increase in A549 sensitivity to doxorubicin was produced using buthionine-S,R-sulfoximine at a non-toxic dose.
Clin Chim Acta 1990 Dec 24
PMID:The effect of doxorubicin on the glutathione content and viability of cultured human lung cancer cell lines A549 and GLC4 210. 196 36

Reactive oxygen species occur in tissues and can damage DNA, proteins, carbohydrates, and lipids. These potentially deleterious reactions are controlled by a system of enzymatic and nonenzymatic antioxidants which eliminate prooxidants and scavenge free radicals. The ability of the lipid-soluble carotenoids to quench singlet molecular oxygen may explain some anticancer properties of the carotenoids, independent of their provitamin A activity. Tocopherols are the most abundant and efficient scavengers of hydroperoxyl radicals in biological membranes. Water-soluble antioxidants include ascorbate and cellular thiols. Glutathione is an important substrate for enzymatic antioxidant functions and is capable of nonenzymatic radical scavenging. Thiols associated with membrane proteins may also be important to the antioxidant systems. Interactions between the thiols, tocopherols, and other compounds enhance the effectiveness of cellular antioxidant defense.
Am J Clin Nutr 1991 Jan
PMID:Antioxidant defense systems: the role of carotenoids, tocopherols, and thiols. 198 87

Exposure of cultured human melanoma cells from three different cell lines to Adriamycin and carmustine at non-cytotoxic (micromolar) concentrations results in a rapid, reversible depletion of cellular glutathione; maximal depletion is achieved within 1 h, and glutathione levels recover within 2-3 h. Glutathione depletion is accompanied by an enhancement of the cytotoxic effects of the alkylating agent melphalan, which ranges from 15- to 55-fold. These results suggest that the combination of Adriamycin and carmustine may provide a rational drug combination for the rapid depletion of glutathione from malignant melanoma, thereby sensitizing these tumor cells to alkylating agent cytotoxicity.
J Cancer Res Clin Oncol 1991
PMID:Sensitization of human melanoma cells to melphalan cytotoxicity by adriamycin and carmustine. 206 51

The effect of chronic ethanol administration on pulmonary antioxidant protection systems was investigated in male Sprague-Dawley rats exposed to room air or room air containing ethanol vapors for 5 weeks. Blood ethanol concentrations in ethanol-exposed rats were usually between 200 and 300 mg/dl. Glutathione, vitamin E, and malondialdehyde concentrations were measured in lung homogenates, and antioxidant enzyme activities (catalase, glutathione peroxidase, Cu/Zn-superoxide dismutase, glutathione reductase) were determined in the supernatant fractions. For comparison, the measurements were also made using liver fractions. Ethanol treatment increased the activities of catalase (117%) and Cu/Zn-superoxide dismutase (25%) in lung but not in liver. Although chronic ethanol inhalation lowered hepatic glutathione (19%) and hepatic vitamin E (33%), there was no increase in malondialdehyde content in either liver or lung of ethanol-exposed rats. The elevation of pulmonary antioxidant enzyme activities could be interpreted to mean that lung is a target for ethanol-induced oxidative stress. However, as there was no loss of pulmonary GSH or vitamin E and no increase in malondialdehyde formation, it appears that long-term ethanol exposure did not produce a significant degree of oxidative stress in rat lung.
Alcohol Clin Exp Res 1990 Dec
PMID:Antioxidant protection systems of rat lung after chronic ethanol inhalation. 208 23

3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase catalyses the rate-limiting step in cholesterol synthesis. Glutathione (GSH) has been postulated to be an important activator of HMG-CoA reductase in vivo. HMG-CoA reductase activity was assayed in cultured fibroblasts from healthy children. Solubilized enzyme preparations were prepared by ultracentrifugation after freezing and thawing of fibroblasts. Such treatment increased the relative enzyme activity markedly. Enzymological assay conditions were established. Addition of GSH stimulated the reaction, whereas there was inhibition after addition of glutathione disulphide (GSSG). The inhibitory effect of GSSG could be reversed by the addition of excess GSH. Fibroblast preparations, deficient in GSH, were obtained from children with glutathione synthetase deficiency or from normal subjects after the growth of fibroblasts in the presence of buthionine sulphoximine. Solubilized enzyme preparations from GSH-deficient fibroblasts had HMG-CoA reductase activities lower than or comparable with those of control preparations. The results indicate only some reduction in the capacity for cholesterol synthesis in subjects with glutathione deficiency. The existence of additional activation mechanisms in vivo, alternative to GSH, for thiol-dependent modulation of HMG-CoA reductase activity seems likely.
Eur J Clin Invest 1990 Aug
PMID:Cholesterol synthesis in patients with glutathione deficiency. 212 8


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