Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chronic ammonia toxicity in experimental mice was induced by exposing them for 2 and 5 days to 5 % (v/v) ammonia solution. The enzymes concerned with glutamate metabolism (aspartate-, alanine- and tyrosine aminotransferases, glutamate dehydrogenase and glutamine synthetase) and (Na+ + K+)-ATPase were estimated in the three regions of brain (cerebellum, cerebral cortex and brain stem) and in liver. Glutamate, aspartate, alanine, glutamine and GABA, RNA and protein were also estimated in the three regions of brain and liver. A significant rise in the activity of (Na+ + K+)-ATPase in all the three regions of brain along with a fall in the activity of alanine aminotransferase was noticed. Changes in the activities of other enzymes were also observed. A significant increase in alanine and a decrease in glutamic acid was observed while no change was observed in the content of other amino acids belonging to the glutamate family. As a result of this, changes in the ratios of glutamate/glutamine and glutamate + aspartate/GABA was observed. The results indicated that the brain was in a state of more depression and less of excitation. Under these conditions the liver tissue was showing a profound rise in the activity of the enzymes of glutamate metabolism. The results are further discussed.
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PMID:Chronic metabolic effects of ammonia in mouse brain. 9 19

Ubiquinol-1 in aerated aqueous solution inactivates several enzymes--alanine aminotransferase, alkaline phosphatase, Na+/K(+)-ATPase, creatine kinase and glutamine synthetase--but not isocitrate dehydrogenase and malate dehydrogenase. Ubiquinone-1 and/or H2O2 do not affect the activity of alkaline phosphatase and glutamine synthetase chosen as model enzymes. Dioxygen and transition metal ions, even if in trace amounts, are essential for the enzyme inactivation, which indeed does not occur under argon atmosphere or in the presence of metal chelators. Supplementation with redox-active metal ions (Fe3+ or Cu2+), moreover, potentiates alkaline phosphatase inactivation. Since catalase and peroxidase protect while superoxide dismutase does not, hydrogen peroxide rather than superoxide anion seems to be involved in the inactivation mechanism through which oxygen active species (hydroxyl radical or any other equivalent species) are produced via a modified Haber-Weiss cycle, triggered by metal-catalyzed oxidation of ubiquinol-1. The lack of efficiency of radical scavengers and the almost complete protection afforded by enzyme substrates and metal cofactors indicate a 'site-specific' radical attack as responsible for the oxidative damage.
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PMID:Enzyme inactivation by metal-catalyzed oxidation of coenzyme Q1. 135 46

Embryonal nervous tissue from Wistar rats was transplanted into male rats of Wistar and August strains. Activity of eight enzymes belonging to various systems was estimated in brain cortex of rats recipients within 36 days after the transplantation. Lactate dehydrogenase, alanine aminotransferase, acid phosphatase, 5'-nucleotidase, ATPase and aldolase exhibited the dissimilarly decreased rate of activity in brain cortex of Wistar rats after transplantation as compared with the enzymatic activity in intact animals of this strain, while activity of alkaline phosphatase and esterases hydrolyzing alpha-naphthyl acetate was increased. Activation of almost all the enzymes studied was found within 36 days in Wistar rats after the transplantation. The rate of activity of zonal esterase isoenzymes was higher in brain cortex of August rats after transplantation of embryonal nervous tissue from Wistar strain as compared with that of Wistar to Wistar rats transplantation. The data obtained suggest that tissues of donors affected definitely the enzymatic activity in brain cells of rats-recipients as activity of most enzymes studied was higher in brain cortex of donors as compared with that of recipients.
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PMID:[Specifics of changes in various groups of enzymes in rat cerebral cortex after interstrain transplantation of embryonal nerve tissue]. 141 28

In the present study, we investigated the toxic response to repeated oral administration of 2-chloroethyl linoleate (2-CEL) in male rats at 250 mg/kg body weight for 2 weeks on alternate days (total 7 doses). Control rats received an equal volume of mineral oil. The five animals from each group were sacrificed on days 1, 7 and 28 following the last dose. No significant changes were observed in body weight, as well as organ-to-body weight ratios due to 2-CEL treatment. The red blood cell counts increased significantly in 2-CEL treated animals at day 28 as compared to the controls. Elevated counts of platelets, monocytes and eosinophils and low counts of basophils and large unstained cells were also observed at some time points in 2-CEL treated rats. Significantly reduced activities of total serum lactate dehydrogenase (LDH), aspartate aminotransferase and alanine aminotransferase were found at most of the time points except for LDH at day 28. Adenosine triphosphatase activity was also significantly reduced in liver mitochondrial fraction at all time points. Histopathological studies showed consistent centrilobular lesions (incidence 4/4) in the liver consisting of hepatocyte vacuolar degeneration and focal necrosis at day 28. A few centrilobular lesions were also observed (incidence 2/4) at day 7, while no changes were observed at day 1. These results indicate that 2-CEL is a hepatotoxin, however, the observed decrease in serum enzyme levels in relation to hepatotoxicity of 2-CEL, needs to be elucidated.
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PMID:Toxic response to repeated oral administration of 2-chloroethyl linoleate in rats. 160 45

A number of chemicals are known to potentiate the hepatotoxicity of carbon tetrachloride. The halocarbon trichloroethylene was shown in a previous study to enhance both carbon tetrachloride-induced toxicity and lipid peroxidation in isolated hepatocytes. In this study three other chlorocarbons have been investigated in order to determine whether this interaction was peculiar to trichloroethylene or common to chlorinated solvents. Hepatocyte suspensions were exposed to carbon tetrachloride at subthreshold levels of toxicity and various concentrations of 1,1,1-trichloroethane, tetrachloroethylene, and chloroform over an eightfold concentration range. Plasma membrane preparations were exposed to tetrachloroethylene and carbon tetrachloride and effects on Mg(2+)- and Na(+)-K(+)-ATPase activities determined. None of the treatments alone caused statistically significant toxicity. Combined treatments resulted in toxicity as demonstrated by potassium ion, alanine aminotransferase, and lactate dehydrogenase leakage from the cells on coincubation of carbon tetrachloride with each of the other halocarbons studied. Only tetrachloroethylene and chloroform were found to potentiate lipid peroxidation, however. In liver plasma membranes no changes in Na(+)-K(+)-ATPase were observed with any of the treatments and only the highest dose of tetrachloroethylene was able to inhibit Mg(2+)-ATPase activity. There was no increase in this inhibition on coincubation with carbon tetrachloride, which does not support involvement of ATPases in combined halocarbon toxicity. In conclusion, the data suggest a mechanism of action common to this class of chemical although its specific nature remains to be established.
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PMID:Potentiating effects of chlorinated hydrocarbons on carbon tetrachloride toxicity in isolated rat hepatocytes and plasma membranes. 182 22

The status of Na+ regulation was examined during early stages of alkylation insult to rat liver. Na+/K+-ATPase activity in plasma membranes declined by 52% within 3 hr of treatment with 850 mg/kg acetaminophen. This loss preceded the release of alanine aminotransferase (2880 +/- 1550 U/ml) and necrosis (2+) seen at 24 hr. Activities of 5'-nucleotidase and Mg2+-ATPase and recovery of plasma membranes were comparatively unchanged at 3 hr. Because damage to Na+/K+-ATPase appeared early in the pathogenesis of acetaminophen hepatotoxicity, loss of hepatocellular Na+ regulation could represent one of the critical molecular consequences of lethal alkylation by acetaminophen.
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PMID:Early inhibition of the Na+/K+-ATPase ion pump during acetaminophen-induced hepatotoxicity in rat. 244 17

The pharmacology, pharmacokinetics, clinical efficacy, adverse effects, and dosage and administration of omeprazole are reviewed. Omeprazole, a substituted benzimidazole, has a unique site and mechanism of action because it inhibits the proton pump--i.e., hydrogen, potassium adenosine triphosphatase (H+,K+-ATPase)--and consequently blocks the final common step in the gastric acid secretory pathway. Omeprazole inhibits basal and histamine-, gastrin- and pentagastrin-stimulated gastric hydrochloric acid secretion. It produces a dose-dependent reduction in gastric acidity, gastric acid output, and gastric juice volume and has variable effects on pepsin secretion. Omeprazole has no documented effect on esophageal motility or lower esophageal sphincter pressure. Omeprazole is variably absorbed from the gastrointestinal tract, and food appears to decrease the rate, but not the extent, of drug absorption. The drug is approximately 95% bound to plasma proteins and is metabolized to inactive components that are enterohepatically or renally eliminated. Omeprazole is more effective (in most studies) than H2-receptor antagonists in treating duodenal ulcer, at least as effective in treating benign gastric ulcer, and more effective in treating reflux esophagitis. Omeprazole has been used successfully in patients with Zollinger-Ellison syndrome refractory to treatment with H2-receptor antagonists. Gastrointestinal complaints (nausea and diarrhea) are the most commonly reported adverse effects associated with omeprazole therapy. The most frequently reported laboratory abnormality occurring with omeprazole use is elevation of serum aspartate aminotransferase and alanine aminotransferase concentrations. Omeprazole will serve a valuable role in the management of gastrointestinal tract ulcers and hypersecretory conditions.
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PMID:Therapeutic evaluation of omeprazole. 306 85

Glycosomes and mitochondrial vesicles from cultured promastigotes of Leishmania mexicana mexicana have been separated using isopycnic centrifugation on linear sucrose gradients. Hexokinase (EC 2.7.1.2), glucose phosphate isomerase (EC 5.3.1.9), phosphofructokinase (EC 2.7.1.11), glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), and phosphoenolpyruvate carboxykinase (EC 4.1.1.49) were recovered largely in association with glycosomes (density; 1.215 g/ml). Phosphoglycerate kinase (EC 2.7.2.3) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) had some small glycosomal activity, but were mostly recovered in the soluble fractions. Malate dehydrogenase (EC 1.1.1.37) showed a broad peak corresponding to that of the mitochondrial marker oligomycin-sensitive ATPase (EC 3.6.1.4) (density; 1.190 g/ml). Glutamate dehydrogenase (EC 1.4.1.3) and alanine aminotransferase (EC 2.6.1.2) both showed small mitochondrial peaks, but most of the activities were recovered elsewhere on the gradient and in the soluble fractions. The subcellular location of enzymes in L.m. mexicana amastigotes was investigated by following the release of soluble enzymes from digitonin-treated amastigotes. This revealed distinct cytosolic, mitochondrial, and glycosomal compartments. The findings give an insight into the organization and control of L.m. mexicana promastigote and amastigote energy metabolism.
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PMID:Leishmania mexicana: subcellular distribution of enzymes in amastigotes and promastigotes. 315 38

The activities of some enzymes of glycolysis, the citric acid cycle, and amino acid metabolism have been measured in the fetal guinea pig heart over the last third of gestation and correlated with heart ultrastructural development. There is little change in glycolytic enzyme activity except for a two- to threefold increase in phosphofructokinase activity. Mitochondrial content and enzyme activities are low in the early fetal heart, and, although content is similar in the late fetus and adult, enzyme activities increase twofold postnatally, indicating fetal heart mitochondria are incompletely developed. The activities of aspartate and particularly alanine aminotransferase are low in the fetal heart. Over the last third of gestation the myofibrillar content of the fetal myocyte increases twofold to the adult value by term. Associated with this is a fourfold rise in myofibrillar and sarcoplasmic reticulum Ca2+-ATPase activity. Na+-K+-ATPase activity is similar in the late fetal and adult heart but one-third lower in the early fetal heart.
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PMID:Ultrastructural and enzymatic development of fetal guinea pig heart. 621 93

The activity levels of aspartate aminotransferase (AAT), alanine aminotransferase (AlAT) and total adenosine triphosphatase (ATPase) were studied in muscle, gill, liver and brain tissues of control and methyl parathion exposed (MPE) fish. Both aminotransferases were elevated in all the tissues inferring the diversion of alpha-amino acids into the TCA cycle as keto acids to augment energy production during methyl parathion (MP) stress. In gill, liver and brain tissues, there seemed to be a shift in the aminotransferase reactions under MP impact. The total ATPase activity was decreased in all tissues, suggesting inhibition of active transport and oxidative phosphorylation.
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PMID:Tissue specific alteration of aminotransferases and total ATPases in the fish (Tilapia mossambica) under methyl parathion impact. 622 5


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