Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Guinea pig glomeruli were grown for 22 days in a serum-free medium composed of Waymouth's MB 752/1 supplemented with sodium pyruvate, nonessential amino acids, and antibiotics. To this basic medium was added insulin, transferrin, selenium (Se), tri-iodothyronine, or fibronectin (FN) - either singly, or in various combinations - and sequential quantitative studies of the glomerular outgrowths were performed. Total cells in glomerular outgrowths, mitotic index, and glomerular attachment rate were determined and compared with values for glomerular outgrowths in media containing either no additions or all of the above components. FN was required for whole glomerular attachment, while transferrin plus FN was required for mitosis in glomerular cell outgrowths. Insulin and tri-iodothyronine slightly increased glomerular cell outgrowth by slightly increasing whole glomerular attachment, but had little effect on mitosis in glomerular outgrowths. The effect of Se was complex. Se did not affect whole glomerular attachment or mitosis in the presence of transferrin plus FN. However, in a medium containing transferrin, FN, and 3-amino-1,2,4-triazole (AT) (an inhibitor of catalase and glutathione peroxidase), Se increased total cell number but had little effect on the glomerular attachment rate or the mitotic index. Morphologic analysis of glomeruli early in culture suggested that Se may act by decreasing the amount of or delaying the time of cell death. In all of the media tested, total DNA was relatively constant over the course of 22 days, suggesting the possibility that glomerular cells cultured in a serum-free medium are part of a cell renewal system.
Virchows Arch B Cell Pathol Incl Mol Pathol 1986
PMID:Kidney glomerular explants in serum-free media: role of individual medium components in cell outgrowth. 287 79

Rats were exposed to 12% O2 (1 atm) for 48 hr, then 10% O2 for the duration of the exposures. Significant elevations in enzymes of the glutathione peroxidase system were found in the lungs of rats killed 3.5, 7.5, and 12.5 days of exposure compared to air-breathing controls. Superoxide dismutase was also elevated after hypoxia but nonsignificantly. Animals killed 12.5 days after exposures exhibited 75% (P less than 0.05) more thiobarbituric acid reactive products in their lungs compared to controls. These results along with significant increases of lung lipid peroxidation and in an augmentation of protective antiperoxidative lung defense capabilities. Hypoxia also resulted in enzyme elevations of lung phosphofructokinase and pyruvate kinase, which may indicate an adaptive increase in lung glycolytic capabilities which would be helpful in maintaining lung tissue energy requirements during hypoxia. In addition, it was confirmed that red blood cell count, hemoglobin and hematocrit values increased after prolonged hypoxia. The results of this study might also reflect enzyme elevation/induction due to cellular reparative-proliferative processes following hypoxia.
Exp Mol Pathol 1986 Dec
PMID:Selected pulmonary biochemical and hematological changes produced by prolonged hypoxia in the rat. 294 10

A 40% reduction of the diameter of the ascending aorta maintained for 60 days induced the formation of a compensate cardiac hypertrophy in rabbits without changing the value of the azide insensitive Ca2+-ATPase activity in comparison to control hearts. The cardiac mitochondria isolated from constricted animals assayed in presence of glutamate and succinate did not show a change in the R.C.I. and ADP/O values in comparison to the controls, whilst the QO2 value enhanced or decreased respectively when determined with glutamate or succinate. The intramuscular injections of CoQ10 (12 mg/kg body weight/48 h) enhanced the mitochondrial CoQ10 concentrations both in the control and in the constricted animals and further increased the QO2 value determined in both groups of animals when glutamate was used as the substrate. The production of O2.- radicals by the level of the complexes I and III of the respiratory chain, did not change in the constricted animals, nor in the animals administered with CoQ10 in comparison to the control. CoQ10 augmented the rate of oxygen consumption by the submitochondrial particles only in the constricted animals. Moreover, the treatment with the coenzyme or the constriction of the aorta, did not modify the cardiac superoxide dismutase activity, but increased the glutathione peroxidase activity only in the banded animals. In addition, in the CoQ10 treated animals there was a reduction of NADH-diaphorase activity both in the control and constricted animals, while the malondialdehyde, generated during the thiobarbituric acid test, and the cardiac content of lipofuscin were decreased.
J Mol Cell Cardiol 1987 Jan
PMID:The effect of treatment with coenzyme Q10 on the mitochondrial function and superoxide radical formation in cardiac muscle hypertrophied by mild aortic stenosis. 303 17

We have measured and characterized three oxidant defense enzymes in early and late intraerythrocytic stages of the human malarial parasite, Plasmodium falciparum. Isolated early intraerythrocytic stages contain catalase (24.1 mumol min-1 (mg protein)-1) and superoxide dismutase (SOD; 6.3 units (mg protein)-1) but little or no glutathione peroxidase (GPX; less than 2 mumol min-1 (mg protein)-1). Isolated late intraerythrocytic stages of P. falciparum contain slightly less catalase (17.0 mumol min-1 (mg protein)-1) but significantly more GPX (7.7 mumol min-1 (mg protein)-1) and SOD (25.1 units (mg protein)-1). P. falciparum, like P. berghei, probably acquires most of its SOD from its host, since parasite-associated SOD is predominantly cyanide-sensitive, and has the same pI as host SOD. Unlike P. berghei, however, late stages of P. falciparum contain an additional SOD isozyme which is not cyanide-sensitive and may represent an endogenous enzyme. Parasites grown in red cells that have been partially depleted of SOD are more sensitive to exogenously generated superoxide, suggesting some dependence of the parasite on host SOD.
Mol Biochem Parasitol 1988 Jul
PMID:Oxidant defense enzymes of Plasmodium falciparum. 304 Dec 78

Oxidative damage produced by oxygen free radicals has been investigated in various mammalian cells in culture. Incubation of these cells with redox cycling quinones resulted in a stimulation of superoxide anion and hydrogen peroxide formation. Further metabolism of H2O2 by glutathione peroxidase caused oxidation and depletion of cellular glutathione followed by oxidation of protein sulfhydryl groups and cytotoxicity. Several targets susceptible to oxidative modification have been identified, including the mitochondrial, endoplasmic reticular, and plasma membrane Ca2+-translocases. As result, a marked and sustained increase in cytosolic free Ca2+ concentration occurred, followed by the activation of some catabolic Ca2+-dependent processes, namely phospholipases, proteases, and endonucleases. In addition, an impairment of the transmembranal signal-transducing system(s) was found. Recent investigations demonstrated that several modifications occur also in the cytoskeleton of oxidative stress-challenged cells. They mainly consist of oxidative actin cross-linking and dissociation of the cytoskeleton from the plasma membrane. All these alterations appear to contribute to the multifactorial process underlying the irreversible cell injury caused by oxidative stress.
Mol Toxicol
PMID:Oxidative stress injury studied in isolated intact cells. 333 5

We used isolated, buffer-perfused rabbit hearts to evaluate whether global, normothermic ischemia altered mitochondrial hydrogen peroxide (H2O2) generation and mitochondrial activities of the major enzymes responsible for degrading H2O2 and superoxide anion (O2-.): glutathione peroxidase (GPD) and superoxide dismutase (SOD), respectively. This preparation lacks exogenous neutrophils and endogenous xanthine oxidase, which are other potential sources of oxygen metabolites. Ischemia depressed mitochondrial oxidative phosphorylation parameters, State 4 succinate-supported H2O2 generation rates, and the relative flux of State 4 oxygen consumption that was diverted to H2O2 formation. The production of H2O2 was not abolished. Ischemia and reperfusion significantly reduced the activities of SOD (by 43%) and GPD (by 39%) in the mitochondrial fraction. Cytosolic GPD activity was also depressed. The results suggest that the myocardial cell's ability to enzymatically degrade H2O2 and O2-. is compromised, particularly in the mitochondrion. Although mitochondrial H2O2 production is decreased, the mitochondria may persist as a source of this oxygen metabolite following ischemia. Collectively, the data may help explain why mitochondria are vulnerable targets of free radical-mediated damage due to ischemia.
J Mol Cell Cardiol 1987 Dec
PMID:Mitochondrial hydrogen peroxide generation and activities of glutathione peroxidase and superoxide dismutase following global ischemia. 344 86

Contrary to previous reports in the literature, bloodstream forms of the haemoflagellate protozoan Trypanosoma brucei brucei are not deficient in their ability to metabolize hydrogen peroxide, although they either lack or only possess the normal enzymes for H2O2 detoxification, catalase (EC 1.11.1.6) and glutathione peroxidase (EC 1.11.1.9), at extremely low levels. The hydrogen peroxide which is consumed appears to be reduced by NADPH derived from glucose via the pentose phosphate pathway. This process requires the newly discovered cofactor trypanothione.
Mol Biochem Parasitol 1986 Aug
PMID:Hydrogen peroxide metabolism in Trypanosoma brucei. 374 70

Glutathione S-transferase (EC 2.5.1.18) was detected in the cytosolic and microsomal fractions of adult Dirofilaria immitis females at respective levels of 30 nmol and 3 nmol min-1 (mg protein)-1 activity with the substrate 1-chloro-2,4-dinitrobenzene (CDNB). The transferase activity in the cytosolic fraction of adult Brugia pahangi females was 10 nmol min-1 mg-1 with CDNB; determination of its activity in the microsomal fraction of this filariid was not attempted. These filarial glutathione S-transferases were further characterized after their purification by glutathione-affinity chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the cytosolic transferase from D. immitis, molecular weight 47000, yielded a single subunit of around 28 kDa. The cytosolic and microsomal transferases from D. immitis differed in their activity with CDNB, 1,2-dichloro-4-nitrobenzene, 4-benzylchloride and ethacrynic acid. The cytosolic transferase from B. pahangi was distinguished by its high activity with ethacrynic acid. Both glutathione S-transferases from D. immitis also functioned as a glutathione peroxidase, strongly preferring cumene hydroperoxide as a substrate over hydrogen peroxide. Both were equiactive inhibitors of malonaldehyde formation in the NADPH-microsomal lipid peroxidation system. Thus, in addition to the ability of filarial glutathione S-transferases to detoxify electrophilic xenobiotics, at least those from D. immitis also exhibited selenium-independent glutathione peroxidase activity. Their glutathione S-transferase function suggests a potential role for these enzymes in the leukotriene synthetic pathway, if filariae can form such eicosanoids from arachidonate. Functioning as a glutathione peroxidase, they could serve to protect filarial membrane lipids from peroxidation.
Mol Biochem Parasitol 1986 Aug
PMID:Glutathione S-transferase in adult Dirofilaria immitis and Brugia pahangi. 374 71

Glutathione peroxidase activity with both hydrogen peroxide and cumene hydroperoxide was measured in the cytosolic fractions prepared from five human hearts obtained from post-mortem victims. In all the samples the activity with cumene hydroperoxide was higher than that obtained with hydrogen peroxide, suggesting that the selenium-independent glutathione peroxidase could also be present in this tissue. To determine its presence in heart tissue we fractionated the cardiac cytosol fraction on a column of Sephadex G-100 and measured glutathione peroxidase activity with both the substrates. Glutathione transferase activity was measured with 1-chloro-2,4-dinitrobenzene in the fractionated cytosol. The results indicated that a selenium-independent glutathione peroxidase activity was present (about 30% of total activity). Fractionation of the cytosol by gel filtration showed that peroxidase activity co-eluted with glutathione transferase activity. Subsequently the fractions containing glutathione transferase and selenium-independent glutathione peroxidase activity obtained from gel filtration experiments were passed through an affinity column and analyzed by isoelectric focusing. It was found that the selenium-independent glutathione peroxidase copurified with three isoenzymes of glutathione transferase which had a pI of 9.2, 8.9 and 8.6 respectively. In contrast the acidic isoenzymes of glutathione transferase lacked peroxidase activity. It is suggested that the selenium-independent glutathione peroxidase may play an important role in neutralizing oxygen toxicity in heart when the selenium-dependent glutathione peroxidase activity is impaired.
J Mol Cell Cardiol 1986 Sep
PMID:Selenium independent glutathione peroxidase activity associated with cationic forms of glutathione transferase in human heart. 378 32

The possibility that myocardial ischaemia alters the defence mechanisms against oxygen toxicity has been investigated. Ischaemia was induced in isolated, perfused rabbit hearts by reducing coronary flow from 25 ml/min to 1 ml/min for 90 min. Two different degrees of ischaemic damage have been achieved using either spontaneously beating or electrically stimulated hearts. The effects of post-ischaemic reperfusion were also followed for 30 min. Tissue activity of superoxide dismutase (SOD), glutathione peroxidase and reductase (GPD and GRD) have been determined together with tissue content of reduced and oxidized glutathione (GSH and GSSG) and of protein SH groups. The changes in myocardial ATP and CP content and release of CPK and of GSH and GSSG were also determined. Systolic and diastolic pressures were continuously monitored. In the spontaneously beating hearts ischaemia induced a reduction of tissue GSH and protein SH groups. On reperfusion there was a recovery of mechanical function, a transient release of GSH into the coronary effluent and an increase of tissue GSH. In the paced hearts, ischaemia resulted in 50% reduction of mitochondrial SOD activity together with a reduction of tissue GSH and protein SH groups. Reperfusion induced a massive release of CPK and of GSH and GSSG, a further reduction of tissue GSH concomitant with an increase of GSSG and no recovery of mechanical function. GPD and GRD activity were not affected by ischaemia and reperfusion. These data indicate that severe ischaemia induces a reduction of the protective mechanisms against oxygen toxicity.
J Mol Cell Cardiol 1985 Oct
PMID:Oxygen-mediated myocardial damage during ischaemia and reperfusion: role of the cellular defences against oxygen toxicity. 406 39


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