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)

Prostaglandin synthetase activity in high-speed particulate fractions of chick epiphyseal cartilage has been characterized with respect to cofactor requirements, pH optimum, buffer-ion effects, types of prostaglandins formed, and the distribution of prostaglandin synthetase activity in zones of the epiphyseal plate. Direct homogenization of cartilage was found to be more efficacious than releasing chondrocytes by enzymatic digestion for preparation of prostaglandin synthetase, a homogenization time of 4 min yielding maximal activity. The optimal incubation medium contained 50 mM Tris buffer (pH 7.5), 2.5 mM epinephrine, 1 micronM hemoglobin, 3.25 mM glutathione, 200 microgram/ml enzyme protein, and 5 micronM substrate. Glutathione was effective only if present during homogenization. Rates of PGE2 biosynthesis were linear up to 15 min and then rapidly declined, indicative of self-deactivation. The low levels of PGF2alpha formed, and their decrease after 20 min incubation, suggests the possible presence of degradative enzymes. Prostaglandin synthetase was inhibited by aspirin, indomethacin, and vitamin E, but not vitamin K1. Cation concentrations in the physiological range had only modest effects on prostaglandin biosynthesis, and then only if present during tissue homogenization. In the presence of phosphate buffer, Ca2+ was somewhat inhibitory. Since in the absence of phosphate Ca2+ had no deleterious effect, it is probably that the inhibitory effect was caused by precipitation of calcium phosphate. Hypertrophic and calcified cartilage exhibited significantly higher prostaglandin synthetase activity than the proliferating and maturing zones. The increased synthesis of prostaglandins in the low layers of the growth plate may indicate a role of these factors in chondrocyte differentiation and/or calcification.
Calcif Tissue Res 1978 Dec 08
PMID:Localization of prostaglandin synthetase in chicken epiphyseal cartilage. 10 4

Erythrocyte amino acid levels were determined, by gas chromatography, in a group of 34 normal human adults. No significant sex or age correlations were noted. A method for the quantitative gas chromatographic analysis of free amino acids in erythrocytes is described. Following hemolysis and deproteinization the amino acids were isolated on a cation-exchange resin. Glutathione was removed from the amino acid mixture by adsorption on an anion-exchange resin. Following conversion to their N-acetyl-n-propyl esters, 19 amino acids were separated and quantitated by gas chromatography on a single column in 18 min. Typical reproducibility data indicate that a coefficient of variation of 2-5% is attainable.
J Chromatogr 1979 Dec 01
PMID:Determination of erythrocyte amino acids by gas chromatography. 54 19

Glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49) and 6-phosphogluconate dehydrogenase (E.C. 1.1.1.44) activities measured in tissue extracts from sea mussel exhibit a potential unbalance which could cause an accumulation of 6-phosphogluconate. Nevertheless elevated levels of this metabolite are not detected in mussel tissues. The Entner-Doudoroff pathway has not been found in hepatopancreas, adductor muscle and gill tissues. Hepatopancreas glucose-6-phosphate-dehydrogenase and 6-phosphogluconate dehydrogenase apparent kinetic parameters at 25 degrees C, were determined. The enzymes are competitively inhibited by NADPH with respect to NADP+. Oxidized Glutathione at nearly physiological concentrations counteracts NADPH inhibition.
Rev Esp Fisiol 1977 Dec
PMID:[Oxidative phase of pentose-phosphate cycle in sea mussel (mytilus edulis l.) (author's transl)]. 59 83

This study deals with investigations in diabetic disorders. Experiments were carried out on alloxan-induced diabetes in albino rats. Blood glucose, keto acids, and glutathione were determined before and after induction of alloxan diabetes. Blood glucose and keto acids showed an increase after administration of alloxan. Glutathione showed a drop after 1/2 hour, then began to increase till it reached its normal level after 48 hours from the beginning of the diabetic state. The results are discussed.
Z Ernahrungswiss 1977 Dec
PMID:Blood glucose, glutathione, and total keto-acids levels in alloxan-diabetic rats. 60 26

The fundamental reactivity or stability of the chloroethylene molecules affects their hepatotoxic potential. Extent and symmetry of the chlorine substitution, which alters electron delocalization, charge polarization, and solubility, affect biologic response. The most nonsymmetrically depolarized chloroethylene, 1,1-dichloroethylene (1,1-DCE) is the most hepatotoxic and causes a unique pattern of hepatocellular injury involving mitochondria, plasma membranes, and chromatin. The injury caused by the other chloroethylenes examined appears to profoundly affect the structural integrity of the endoplasmic reticulum with toxic potential in the order: trichloroethylene (TRI) greater than vinyl chloride (VCM) greater than perchloroethylene (PER). Pretreatments which increased cytochrome P-450 contents, thus presumably augmenting metabolic activation to a reactive intermediate such as an epoxide, enhanced or were synergistic to the hepatotoxic potential of TRI, VCM and PER but were protective or antagonistic to 1,1-DCE hepatotoxicity. Biologic response to 1,1-DCE may be expressed by a different metabolic pathway. Glutathione appears to be involved in the biologic response to all nonsymmetric chloroethylenes and toact as an antagonist against injury. Marked differences in the patterns of injury and the biologic responses suggest that more than one mechanism is involved in the production of injury by chloroethylenes.
Environ Health Perspect 1977 Dec
PMID:Damage to hepatic cellular membranes by chlorinated olefins with emphasis on synergism and antagonism. 61 38

Serum albumins of certain animal species (cow, sheep, pig) accelerate the decomposition of prostaglandin endoperoxides, with formation of large amounts of prostaglandin D. The reaction is inhibited by arachidonic acid, which suggests an interaction of the endoperoxide with the fatty acid binding sites of serum albumin. Glutathione-S-transferases, in the presence of glutathione, convert the endoperoxide into a mixture of prostaglandin F2alpha, E2 and D2. The prostaglandin D/E-ratio depends on the transferase used. The known rat liver transferases give mainly prostaglandin F2alpha and E2, but a new transferase in sheep lung was discovered which gives rise to large quantities of prostaglandin F2alpha and D2. The sheep lung transferase was purified to homogeneity. Two iso-enzymes with identical enzymic activity were obtained. The major component (transferase SL 2, an iso-enzyme of glutathione-S-transferase, EC 2.5.1.18) has a molecular weight of 45 000 and consists of two subunits. Its isoelectric point is 9,8-9.9. These properties, as well as the amino acid composition and the substrate specificity for typical transferase substrates, indicate a close resemblance to transferase B (ligandin), a major binding protein of rat liver. Although purified glutathione peroxidase from erythrocytes is very active in catalysing the reduction of the 15-hydroperoxy group of prostaglandins, it does not have any effect on the decomposition of the endoperoxide group.
Biochim Biophys Acta 1976 Dec 20
PMID:Conversions of prostaglandin endoperoxides by glutathione-S-transferases and serum albumins. 100 99

The product of the reaction between sodium selenite and glutathione, designated as selenodiglutathione (GSSeSG), nearly completely inhibits amino acid incorporation from [14C]leucyl-tRNA by free polyribosomes isolated from rat liver. The mechanism of this inhibition was studied on the basis of the following three findings. Glutathione decomposes GSSeSG to harmless products; GSSeSG acts instantaneously on some component of the complete incubation system during preparation of the incubation vessels (at 0 degrees C); once GSSeSG has reacted its inhibitory effect cannot be reversed by glutathione. Accordingly, the effect of GSSeSG on the various steps of the amino acid incorporation process was studied by varying the sequence of additions of the reaction components, GSSeSG and GSH. The results of these and other experiments showed elongation factor 2 to be target of GSSeSG. The GSSeSG-B blocked factor could be regenerated by reduction with glutathione reductase and NADPH.
Biochim Biophys Acta 1975 Dec 19
PMID:Elongation factor 2 as the target of the reaction product between sodium selenite and glutathione (GSSeSG) in the inhibiting of amino acid incorporation in vitro. 120 59

We investigated the level of reduced glutathione in mouse liver after injection of staphylococcal enterotoxin type A (SEA) and Serratia marcescens endotoxin (LPS). It was shown that SEA caused significant glutathione depletion. Glutathione level fell more under the combined treatment by both toxins. The data demonstrate a considerable role of antioxidant potential in the mechanism of enhanced sensitivity of animals to the lethal effect produced by LPS.
Biull Eksp Biol Med 1992 Dec
PMID:[Changes in the content of reduced glutathione in the liver of mice under the action of staphylococcal enterotoxin type A and lipopolysaccharide]. 129 97

Acute single dose administration of lanthanum chloride (250 mg/kg body wt, ip) to chicks have been found to alter the levels of enzymes of the antioxidant defence system of chick renal cortex fractions. Such changes involved significant decrease in activities of glucose-6-phosphate dehydrogenase, glutathione reductase, glutathione peroxidase and catalase of kidney epithelial cells. However glutathione-S-transferase activity was not altered. Glutathione and total thiol contents were decreased while lipoperoxidative reactions in kidney-cortex was significantly enhanced. The data indicate that amelioration of lanthanum toxicity condition by methionine supplementation may be due to the methionine serving as a precursor of glutathione.
Indian J Exp Biol 1992 Dec
PMID:Curative effect of methionine on certain enzymes of chick kidney cortex under lanthanum toxicity situation. 129 80

The activities of Superoxide Dismutase (SOD), Glutathione Peroxidase (GSH-Px) and Catalase (CAT) in the ischemic cerebral tissue following the unilateral middle cerebral artery occlusion of rats were assessed. In comparison with the sham-operated rats, both SOD and GSH-Px activity in the ischemic area (striatum and fronto-parietal cortex) were significantly reduced by 30 min. of ischemia, GSH-Px activity in the peri-ischemic area (parieto-parasagittal) was significantly reduced as well. It was shown that in the striatum the GSH-Px activity was much higher than that in the cortex. According to our data, it was suggested that in the ischemic condition, cerebral Superoxide (O2-) and Hydrogen Peroxide (H2O2) were accumulated, and thus the polyunsaturated fatty acids in the neuronal membrane were trapped by these free radical. And such a process resulted in neuronal damage. It implicated that the oxygen free radical might be involved in the neuronal damage induced by Dopamine, since the O2- and H2O2 were excessively generated during the oxidative deamination of Dopamine and the free radical scavengers, SOD and GSH-Px were decreased concomitantly in the cerebral ischemic tissue.
Zhonghua Shen Jing Jing Shen Ke Za Zhi 1992 Dec
PMID:[A study on the activity of three antioxidant enzymes in the brain of experimental acute cerebral ischemia]. 130 99


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