Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT03226 (vitamin E)
 17,558 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hepatic microsomes from rats fed a crude or a purified diet were compared by measureing their contents of protein, cytochrome P-450, and cytochrome b5, their rates of activity of NADPH- and NADH-cytochrome c reductases, NADPH-cytochrome P-450 reductase, NADPH oxidase, lipid peroxidase, ethylmorphine N-demethylase, aniline hydroxylase, benzpyrene hydroxylase, and their substrate-binding spectra (ethylmorphine, hexobarbital, aniline, and ethyl isoyanide). With the exception of lipid peroxidase activity, which was much higher in microsomes from animals fed the crude diet, little or no consistent diet-related differences in these measurements were observed over a 4-week experimental period, nor were results significantly less variable with one or the other diet. No consistent significant differences were observed with two strains of rats. The lower lipid peroxidase activity seen with the purified diet appeared to be due to the high vitamin E intake when that diet was employed; rats fed the crude diet and an oral supplement of alpha-tocopherol yielded microsomes with low lipid peroxidase activities similar to those seen in microsomes from rats fed the purified diet. A gradual temporal increase in benzpyrene hydroxylase activity was observed with both diets. This was interpreted to be due to environment inducing agents other than those present in the diet.
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PMID:Comparison of hepatic microsomal drug-metabolizing systems from rats fed crude and purified diets. 0 25

The effect of cholesterol feeding on liver and aortic nonenzymatic lipid peroxidation and glutathione peroxidase activities, and on liver microsomal NADPH-dependent lipid peroxidation, codeine hydroxylation and cytochrome P-450 levels was examined in rats and guinea pigs. One percent cholesterol was added to a casein-sucrose-soybean oil basal diet for rats or a stock diet with 2% soybean oil for guinea pigs. The effect of vitamin E and cholestyramine was also examined in some experiments. Cholesterol feeding increased the rate of lipid peroxidation in liver and aortic homogenate both in rats and guinea pigs when fed non-vitamin E supplemented basal diets. Vitamin E supplementation prevented the increase in the aorta, but not as completely in the liver in rats, while the reverse was true in guinea pigs. The effect of cholestyramine was dependent on the level of vitamin E in the diet. Cholesterol feeding decreased glutathione peroxidase activities in rats and guinea pigs. In guinea pigs, cholesterol feeding also markedly decreased liver microsomal NADPH-dependent lipid peroxidation, codein hydroxylation and cytochrome P-450 levels especially when fed non-vitamin E supplemented basal diets. In rats, cholesterol feeding reduced liver microsomal NADPH-dependent lipid peroxidation and in some cases, increased microsomal codeine hydroxylation activities, but had no effect on microsomal cytochrome P-450 levels. Vitamin E supplementation increased liver and serum cholesterol levels in guinea pigs, but had no such effect in rats. Results of this study indicate that cholesterol feeding can result in various metabolic alterations in rats and guinea pigs. The implication of these alterations in atherogenesis requires further investigations.
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PMID:Effect of cholesterol feeding on tissue lipid perioxidation, glutathione peroxidase activity and liver microsomal functions in rats and guinea pigs. 1 70

The time required for red blood cells (RBC) from vitamin E-deficient lead-poisoned (-E + Pb) rats to pass through polycarbonate filters after incubation in vitro was much greater than that of RBC from vitamin E-supplemented non-poisoned rats. Vitamin E deficiency per se (i.e., in non-poisoned rats) often increased filtration times, but in all such experiments the RBC from -E + Pb groups had even longer filtration times. Administration of lead to rats supplemented with vitamin E had little effect on the filtration rate of RBC. N,N'-diphenyl-p-phenylenediamine (DPPD) prevented the increased filtration times characteristic of RBC from -E + Pb rats, but replacement of the lard in the vitamin E-deficient basal diet by more highly polyunsaturated fats did not exacerbate the increased filtration times of RBC from -E + Pb rats. The increased filtration time of RBC from -E + Pb rats appeared to be related to the extent of RBC lipid peroxidation. Decreasing the pH of the RBC incubation medium from 7.4 to 6.6, an acidity typical of the spleen, markedly increased the filtration times of RBC from -E + Pb rats. Addition of lead in vitro increased filtration times of RBC from both vitamin E-deficient and supplemented non-poisoned rats, but filtration times tended to be longer in the deficient group. These results suggest that vitamin E deficiency and lead toxicity act synergistically to alter the deformability of the RBC thereby rendering it vulnerable to sequestration in the spleen.
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PMID:Filterability of erythrocytes from vitamin E-deficient lead-poisoned rats. 1 50

The effects of dietary vitamin B-2 and vitamin E on delta9-desaturation of stearoyl-CoA, catalase, glutathione peroxidase, superoxide dismutase and electron transport components in rat liver microsomes have been investigated. delta9-desaturase activities were decreased on diets deficient of vitamin B-2, E and supplemented with E. Among the peroxide-scavenging enzymes, only the catalase activity in microsomes correlates significantly with delta9-desaturase activity. In vitro addition of bovine catalase had no effect on microsomal delta9-desaturase activity on control diet. However, it enhanced the delta9-desaturation in microsomes on vitamin B-2-deficient diet which contained low catalase and high superoxide dismutase activities, compared to those in microsomes of control diet. It is suggested that the hydrogen peroxide-generating and -decomposing systems may play an important role on the delta9-desaturase activity in microsomes.
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PMID:Effects of dietary vitamin B-2 and vitamin E on the delta9-desaturase and catalase activities in the rat liver microsomes. 2 49

Peroxidation of the unsaturated lipid of tissue homogenates is an established method to assess the antioxidant or vitamin E status of animals. In the present study the spontaneous lipid peroxidation in air of rat brain homogenates is reported. The effects of various factors like pH, time, concentration of tissues, temperature, ferrocompounds and catalysis by added tissues like liver are described. Rat brain homogenates appear to be a suitable preparation for in vitro studies of lipid peroxidation.
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PMID:Factors affecting in vitro lipid peroxidation of rat brain homogenate. 2 88

Three distinct isoenzymes of acid phosphatase have been separated from extracts of m.gastrocnemius of normal and of vitamin E deficient rabbits by gel filtration and polyacrylamide gel electrophoresis. These isoenzymes, termed I, II and III, have molecular weights of: 110,000--130,000, 60,000--78,000 and 12,500--14,500. Isoenzymes I and II split the substrates 4-methylumbelliferyl phosphate and naphthol AS-BI phosphate and the activity is strongly increased in the muscles of vitamin E deficient rabbits. Isoenzyme III splits only 4-methylumbelliferyl phosphate and the activity is not increased in the muscles of vitamin E deficient rabbits. The pH-optimum for isoenzymes I and II is 4.8 and for isoenzyme III 5.5. It has been shown that the histochemical semipermeable membrane technique, using substrate naphthol AS-BI phosphate, is a very reliable technique for demonstrating activity of the isoenzymes I and II in tissue sections. On the other hand, activity of isoenzyme III cannot be demonstrated with this histochemical technique. In pathologically altered muscles, the activity of the isoenzymes I and II is greatly increased whilst the activity of isoenzyme III is not significantly altered.
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PMID:Evaluation of histochemical observations of activity of acid hydrolases obtained with semipermeable membrane techniques. 3. The substrate specificity of isoenzymes of acid phosphatase in m.gastrocnemius of rabbits. 3 96

Enzymic activity of tyrosine aminotransferase is unchanged in subcellular fractions of the liver tissue of control, E-hypovitaminotic rats and of the same animals subjected to a single vitamin E administration. Enzymic activity of phenyl alanine-4-hydroxylase in the supernatant fraction determined in the incubation medium without biopterin in animals with E-hypovitaminosis is 39% lower than in the control rats. The coefficient of phenyl alanine-4-hydroxylase activation with biopterin in vitro in E-hypovitaminotic animals is thrice as high as that in the control rats. A single vitamin E administration produces a 1.8-fold decrease in the activation coefficient. The data obtained give reason to suggest the possible influence to vitamin E on the biopterin level in the liver.
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PMID:[Phenylalanine-4-hydroxylase and tyrosine aminotransferase activities in rat liver tissue under different vitamin E content in the organism]. 4 93

Peroxidation of endogenous lipid by rat liver microsomes, coupled with oxidation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) was markedly stimulated in the presence of indomethacin [1-(p-chlorobenzyl)-5-methoxy-2-methyl-3-indole acetic acid], a potent anti-inflammatory drug. This system also generated a rapidly developed chemiluminescense (CL), the intensity and rate of development of which were related to indomethacin concentration and the amount of peroxidation in the sample. Microsomes from rats fed a liquid diet based on Sego diet drink (Pet Incorporated) failed to chemiluminesce with or without added indomethacin. Supplementation of the Sego diet with a polyunsaturated fatty acid (C18:3) did not restore the chemiluminescense. In vitro and in vivo studies indicate that vitamin E (a component of the Sego liquid diet) inhibited the microsomal chemiluminescense reaction in a dose related manner.
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PMID:The effect of dietary vitamin E on indomethacin stimulated chemiluminescense in rat liver microsomes. 4 40

Determination of the complement titer in the serum and plasm of 120 patients with chronic liver diseases showed that in eight (7%) patients with cirrhosis of the liver, chronic active or chronic inactive hepatitis complement in the serum was less than half in the plasma. The dissociation of complement serum and plasma was due to cold activation of the classical pathway of complement in vitro since serum drawn from these patients at 37 degrees C lost hemolytic activity in 4 hours when transferred to a cold environment. Neither HB antigen nor cryoglobulin participated in this phenomenon. The activation of complement in the cold could be prevented by increasing the ionic strength, or by adding vitamin E or, to a lesser extent its vehicle HCO-60, while heparin, Trasylol, soybean trypsin inhibitor, or hirudin had no effect. Trans-AMCHA prevented activation in one case. It is speculated that a factor appearing as a result of blood clotting is able to activate the classical pathway of complement in the cold; it is probably not related to Hageman factor (factor XII), factor VII, thrombin, kallikrein.
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PMID:Cold activation of complement i. presence of coagulation-related activator. 5 81

Diffuse deposition of ceroid pigment in the muscularis propria of the gastrointestinal tract in a patient with a long history of malabsorption of unknown origin is reported. The depostion of this waste pigment is not reversible and is related to prolonged depletion of vitamin E. Progressive dilatation and hypomotility of the entire gastrointestinal tract are demonstrated by radiographic studies and possibly related to infiltrate of ceroid pigment in the smooth muscle cell with resulting functional impairment. In the differential diagnosis of ceroidosis with other disease, scleroderma has the closest roentgenographic similarity. Pseudoobstruction of the small bowel which can develop must be treated conservatively to avoid unnecessary bowel resection.
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PMID:Pseudoobstruction in ceroidosis. 6 64


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