Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.49 (glucose-6-phosphate dehydrogenase)
7,794 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of iron deficiency on a number or iron containing enzymes in rat liver has been examined. In addition, 6-phosphogluconate dehydrogenase and glucose 6-phosphate dehydrogenase have been assayed. Of the mitochondrial electron transport reactions only succinate-cytochrome C reductase activity was decreased in iron deficient animals. Microsomal reductase enzymes associated with the NADPH-oxidase system were also markedly decreased although cytochrome P450 concentrations were unaffected. Both 6-phosphogluconate dehydrogenase and glucose 6-phosphate dehydrogenase were reduced in young iron deficient rats but the former had returned to control levels at the age of 14 weeks.
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PMID:The effects of iron deficiency on rat liver enzymes. 17 99

All of the superoxide dismutase isozymes of Escherichia coli have been shown to occur in the cell matrix, and none have been found in the periplasm. This was the case with both E. coli B and E. coli K-12, whether grown on a low phosphate medium or on a Trypticase soy-yeast extract medium. Alkaline phosphatase was used as a marker of the periplasm; adenosine deaminase and glucose 6-phosphate dehydrogenase were used as matrix markers, and consistent results were obtained by osmotic shock, spheroplast formation, and use of a diazonium salt that penetrates the periplasm but cannot cross the plasma membrane. A previous report that the iron-containing superoxide dismutase of E. coli is a periplasmic enzyme is now seen to have been in error.
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PMID:Intracellular localization of the superoxide dismutases of Escherichia coli: a reevaluation. 33 Apr 99

Blood samples were collected monthly over a nine-month period from 19 high-producing Holstein-Friesian dairy cows. Dry cows on the lowest (13 per cent) protein ration had the highest mean values for packed cell volume (PCV), haemoglobin (Hb) and red blood cells (RBC). Among the lactating cows, the group on the 13 per cent protein diet had the highest mean PCV, Hb and RBC values. Other constituents were not affected significantly by dietary protein levels. Packed cell volume, RBC, Hb, serum iron (SI), iron binding capacity (IBC) and serum albumin concentrations decreased early in lactation and rose to pre-lactation levels by mid-lactation. PCV and Hb concentrations remained low for periods up to four months. RBC count was lowest in the second month while albumin concentration was lowest in the first month and remained low up to the second month. IBC was lowest in the first month of lactation while SI concentrations were lowest in the third month. There were no significant variations in the activities of erythrocyte glucose-6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD) and reduced glutathione (GSH). The 13 per cent protein ration had no anaemia-inducing effect on the cows.
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PMID:Effects of dietary protein and stage of lactation on the haematology and erythrocyte enzymes activities of high-producing dairy cattle. 47 89

In experiments using rats it was shown that inadequate dietary supply of Ni reduces growth and lowers the erythrocyte count, hematocrit and hemoglobin level in blood, that the Ni supply affects the trace element content of iron, copper and zinc in various body organs, and that the absorption of iron is greatly impaired by Ni deficiency. For further biochemical criteria on the essentiality of nickel, the activities of two dehydrogenases, malate dehydrogenase and glucose-6-phosphate dehydrogenase, were measured in liver homogenates from two generations of rats at 30 and 50 days of age. In the 30-day-old rats of both the F1 and F2 generation, the activity of the malate dehydrogenase fell to about two-thirds the level of control animals. In the liver of the 50-day-old rats the activity of this enzyme was about the same in deficient animals as in the controls. The activity of glucose-6-phosphate dehydrogenase of Ni-deficient rats was reduced by 85% in the F1 generation and by 56% in the F2 generation at 30 days of age as compared with control levels. In 50-day-old rats the activity had fallen to half the level of control animals at 30 days of age. At the age of 50 days, there was no significant difference between the deficient and the control groups of either generation.
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PMID:Malate dehydrogenase and glucose-6-phosphate dehydrogenase activity in livers of Ni-deficient rats. 105 37

We examined the efficacy and safety of meso-2,3-dimercaptosuccinic acid (DMSA) in children with markedly elevated blood lead (BPb) concentrations. Among 19 children with BPb concentrations of 50 to 69 micrograms/dl (2.41 to 3.33 mumol/L) who received a 5-day inpatient oral course of DMSA (1050 mg/m2 per day), the mean BPb concentration decreased by 61%; in four who received calcium disodium ethylenediaminetetraacetic acid (CaNa2EDTA) (1000 mg/m2 per day intravenously), it decreased by 45% (p less than 0.0007). Urinary lead excretion was comparable in both groups. Treatment with DMSA was more effective than treatment with CaNa2EDTA in restoring metabolic activity to the heme pathway and was well tolerated even among nine patients who received concomitant iron supplementation and two who had homozygous deficiency of glucose-6-phosphate dehydrogenase. On discharge, these 19 children received either no chelation therapy or DMSA, 350 or 700 mg/m2 per day for 14 days on an outpatient basis. After 14 days the mean BPb values for the no-chelation, low-DMSA, and high-DMSA groups were 73%, 66%, and 50% of the pretreatment values, respectively. We conclude that a 5-day oral course of DMSA is effective in the treatment of children with severe lead poisoning. In addition, on an outpatient basis the administration of DMSA, 700 mg/m2 per day, is capable of delaying the typical rebound in BPb values and should ultimately reduce the need for repeated hospitalizations.
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PMID:Controlled study of meso-2,3-dimercaptosuccinic acid for the management of childhood lead intoxication. 130 65

It is established that previously observed increased rate of the induced lipid peroxidation in brain tissue of rats with hereditary retinal degeneration as compared with normal rats is due to the change of the rate of this process in the microsome cortex brain fraction and was not observed in the mitochondrial-synaptosomal and nuclear fractions. The content of nonheme iron ions in microsome cortex brain fraction of the Campbell rats is decreased by 35% and of the Fe ion was in the reduced form as compared with the Wistar rats. The ratio of Fe2+/Fe3+ in this fraction of the Campbell rats will be 5.21; Wistar rats--0.51. The increase of the reduced form of the Fe ion may be a result of the increased rate of the glucose-6-phosphate dehydrogenase activity in cortex brain tissue of the Campbell rats. We accept change of the content and the forms of the Fe ions in the microsome cortex brain fraction as a cause of the increased rate of induced lipid peroxidation in brain of the Campbell rats. All the observed phenomena are manifested at the early stage of life and indicated that different metabolic disorders can be observed in the Campbell rats not only in the retina and eye pigment epithelium but also in the brain tissue.
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PMID:[Localization and causes of lipid peroxidation disorders in the rat cerebral cortex in the early stages of hereditary retinal degeneration]. 141 21

The PAR1/SNQ3 gene of S. cerevisiae, which increases resistance to iron chelators in multi-copy transformants, is identical to the YAP1 gene, a yeast activator protein isolated as a functional homologue of the human c-jun oncogene by binding specifically to the AP-1 consensus box. The observed H2O2-sensitivity of par1 mutants has been attributed to an increased sensitivity to reduced oxygen intermediates. Accordingly, par1 mutants did not survive an elevated oxygen pressure and were very sensitive to menadione and methylviologene, two chemicals enhancing the deleterious effects of oxygen. The specific activities of enzymes involved in oxygen detoxification, such as superoxide dismutase, glucose 6-phosphate dehydrogenase and glutathione reductase, were decreased in par1 mutants and increased after PAR1 over-expression. As in the case of oxygen detoxification enzymes, the cellular levels of glutathione were similarly affected. These observations indicate that PAR1/YAP1/SNQ3 is involved in the gene regulation of certain oxygen detoxification enzymes. The finding that H2O2 promotes DNA-binding of human c-jun is consistent with a similar function for PAR1/YAP1/SNQ3 and c-jun in cellular metabolism.
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PMID:The PAR1 (YAP1/SNQ3) gene of Saccharomyces cerevisiae, a c-jun homologue, is involved in oxygen metabolism. 152 53

1. Aluminum is an established neurotoxin. Prolonged exposure to even low levels of aluminum permit its chelation and subsequent transport to brain where it is non-uniformly distributed. 2. Available evidence suggests that (i) aluminum interferes with glucose metabolism by inhibiting hexokinase and glucose-6-phosphate dehydrogenase; (ii) it binds to calmodulin and affects numerous phosphorylation-dephosphorylation reactions; (iii) it binds to transferrin and ferritin, affects the function of these proteins which in turn affect iron metabolism. 3. Thus accumulation of aluminum-induced metabolic errors colocalized in specific areas of the brain may lead to neurological disorders.
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PMID:Neurochemical hypothesis: participation by aluminum in producing critical mass of colocalized errors in brain leads to neurological disease. 167 37

Neutrophil myeloperoxidase, hydrogen peroxide, and chloride constitute a potent antimicrobial system with multiple effects on microbial cytoplasmic membranes. Among these is inhibition of succinate-dependent respiration mediated, principally, through inactivation of succinate dehydrogenase. Succinate-dependent respiration is inhibited at rates that correlate with loss of microbial viability, suggesting that loss of respiration might contribute to the microbicidal event. Because respiration in Escherichia coli can be mediated by dehydrogenases other than succinate dehydrogenase, the effects of the myeloperoxidase system on other membrane dehydrogenases were evaluated by histochemical activity stains of electrophoretically separated membrane proteins. Two bands of succinate dehydrogenase activity proved the most susceptible to inactivation with complete loss of staining activity within 20 min, under the conditions employed. A group with intermediate susceptibility, consisting of lactate, malate, glycerol-3-phosphate, and dihydroorotate dehydrogenases as well as three bands of glucose-6-phosphate dehydrogenase, was almost completely inactivated within 30 min. The relatively resistant group, including the dehydrogenases for glutamate, NADH, and NADPH and the remaining bands of glucose-6-phosphate dehydrogenase, retained substantial amounts of diaphorase activity for up to 60 min of incubation with the myeloperoxidase system. The differential effects of myeloperoxidase on dehydrogenase inactivation could not be correlated with published enzyme contents of flavin or iron-sulfur centers, potential targets of myeloperoxidase-derived oxidants. Despite the relative resistance of NADH dehydrogenase/diaphorase activity to myeloperoxidase-mediated inactivation, electron transport particles prepared from E. coli incubated for 20 min with the myeloperoxidase system lost 55% of their NADH oxidase activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Differential inactivation of Escherichia coli membrane dehydrogenases by a myeloperoxidase-mediated antimicrobial system. 169 36

174 serum ferritin assays in 121 patients with various haemolytic disorders have been performed. The mean serum ferritin levels were significantly increased in all these disorders in contrast to healthy controls. The highest serum ferritin levels were found in pyruvate kinase (PK) deficiency, moderate increase was observed in hereditary sphaerocytosis (HS) and in autoimmune haemolytic anaemia (AIHA) with massive haemolysis and in glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. Mild elevation of serum ferritin levels was depicted in paroxysmal nocturnal haemoglobinuria (PNH), in beta thalassaemia minor and in other types of haemoglobinopathies. The range of values was associated with a degree of haemolysis and its relation to duration of the disease was not apparent in most cases. Highly significant differences between serum ferritin levels in splenectomized and non-splenectomized patients with HS and between serum ferritin levels in patients with AIHA with massive haemolysis or in remission were found. As compared to normal controls, significant increase of serum ferritin levels was observed even in patients with AIHA in remission or in splenectomized patients with HS. In two patients with PK deficiency the levels exceeding 2,000 micrograms/l indicated manifest iron overload. A reliability of serum ferritin assay as an index of iron stores in haemolytic disorders has been discussed.
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PMID:Serum ferritin in patients with various haemolytic disorders. 169 23


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