Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Treatment with neuraminidase decreased the activity of Na+,K+-activated Mg2+-adenosine triphosphatase in plasma membranes isolated from experimental granulation tissue but not that of 5'-nucleotidase or leucine-beta-naphthylamidase. A temporary lowering of the pH of the plasma membrane suspension to 2-3 inactivated all three enzymes, which remained inactive after the pH had been readjusted to 7.4. Addition of dextran preparations to the membrane suspension decreased the activity of adenosine triphosphatase. Ethanol (0.4%) had a similar effect. These marker enzymes of plasma membranes were not affected by additions of hyaluronate, chondroitin sulfate, protein polysaccharide or soluble collagen. Serotonin stimulated the adenosine triphosphatase activity slightly. About 10-20% of the protein in the plasma membrane preparation was extracted with EDTA. This "fuzzy coat" fraction yielded a distinct gel-electrophoretic protein pattern. Hyaluronidase was not helpful in cleaving this surface layer from the plasma membranes.
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PMID:Properties of plasma membranes from granulation tissue with reference to extracellular matrix. 0 56

Mutations at the OLI 1 or OLI 2 loci of mitochondria DNA in Saccharomyces cerevisiae are associated with a diminished growth rate in nutritionally suboptimal cultures supplemented with an oxidizable carbon source. In the case of mutant OR146(OLI1) there is a 35% loss of mitochondrial protein during fractionation in vitro, suggesting that the mutationally altered adenosine triphosphatase(ATPase) confers some instability on the mitochondrial membrane. The possibility is discussed that this reflects an unstable mitchondrial population in vivo, leading the observed growth deficiency. Mitochondria from mutant OR146 at the OLI 1 locus show a relatively oligomycin-resistant State-3 respiration, but the same ADP/O and respiratory-control quotients as the isonuclear wild-type. A slightly lowered Qo2 with NADH-linked substrates was observed and is discussed. For both strains the apparent H+/O ratios were close to 4 with pyruvate, ethanol and alpha-oxoglutarate, but consistently lower with succinate and citrate. For each substrate a characteristic t 1/2 (time for half-decay of the transmembrane pH differential) range was found, consistent with the view that the substrates effecitvely carry the protons back across the membrane. As expected, H+/O ratios were independent of t 1/2 for all substrates, with the exception of alpha-oxoglutarate in the case of the wild-type, where an inverse correlation was found. The lack of this correlation in the case of the mutant was the only apparent difference in the translocation parameters observed. A hypothesis relating this to the functioning of the oligomycin-resistant ATPase is proposed.
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PMID:An oligomycin-resistant adenosine triphosphatase and its effects on cellular growth, mitochondrial oxidative phosphorylation and respiratory proton translocation in Saccharomyces cerevisiae. 1 56

The effects of acute and chronic administration of D-Galactosamine (GalN), Ethanol and Phenobarbital were investigated on the activities of lysosomal enzymes, i.e.; acid phosphatase, beta-glucuronidase and n-acetyl-beta-glucosaminidase, and others such as gamma-GTP and adenosine triphosphatase. The histochemical distribution of gamma-GTP in the liver was also studied on biopsy specimens from patients with chronic hepatitis, and gamma-GTP levels in the serum of patients receiving drugs inductable of hepatic microsomal enzymes. 1) After a single intraperitoneal injection of GalN, the lysosomal enzyme activities were lowered in the necrotic areas, but raised in the perinecrotic areas, the proliferative Kupffer cells and intra- and/or extra-cellular eosine bodies. 2) gamma-GTP activities in rat liver after chronic administration of GalN were markedly increased in bile canalicular membrane of periportal parenchymal cells, the epithelium of bile duct and ductules, and som inflammatory cells of portal fields. Levels of serum gamma-GTP were also elevated. On histochemical studies with biopsy specimens from patients with chronic active hepatitis showing elevated gamma-GTP activity, the activity was revealed a similar localization to GalN-treated rats. These data suggested that the increased activities might be reflected on the active stage in chronic hepatitis. 3) Chronic ethanol treatment in rats induced clearly-stained lysosomes varied in size, especially large-sized. The activities of hepatic gamma-GTP were slightly increased in the bile canalicular membrane of periportal parenchymal cells and the epithelium of proliferative bile ductules. 4) It has been shown by histochemical and biochemical techniques that hepatic gamma-GTP activity was increased after phenobarbital administration in rats. A significant rise in serum gamma-GTP was observed in patients on long-term treatment with anti-epileptic drugs. These data indicated that the increased activities of serum gamma-GTP might be accompanied with induction of hepatic microsomal drug-metabolizing enzymes.
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PMID:[Clinical and experimental histochemical studies on the activities of liver lysosomal enzymes and gamma-glutamyl transpeptidase (gamma-GTP) (author's transl)]. 3 25

The effects of fixation with various concentrations of glutaraldehyde or formaldehyde, acetone or ethanol, and freeze-drying on 5 phosphatases of Eimeria tenella and chick kidney cell cultures were demonstrated in situ. Gultaraldehyde inactivated the phosphatases more than did the formaldehyde, but the effect of the combination of the 2 (Karnovsky's fixative) was greater than that of either glutaraldehyde or formaldehyde alone. The higher the concentration of aldehyde and the longer the duration of exposure, the greater the inactivation. The order of sensitivity to aldehyde fixation of the enzymes tested was glucose-6-phosphatase greater than thiamine pyrophosphatase greater than 5'-nucleotidase greater than adenosine triphosphatase greater than acid phosphatase. Cytologic detail was preserved more efficiently with glutaraldehyde than with formaldehyde. Optimal preservation of enzyme activity for cytochemistry was with 2% glutaraldehyde for 30 min or 2% formaldehyde for 1 hr for G-6-Pase, TPPase, and 5'-nucleotidase, and with 2% glutaraldehyde or 2% formaldehyde for 2 hr with ATPase and AcPase. Quenching with subsequent fixation in cold acetone or ethanol resulted in complete inactivation of G-6-Pase, TPPase, and 5'-nucleotidase; although cells fixed in this manner yielded large amounts of reaction product for ATPase and AcPase, the distribution was diffuse, and some of it appeared to be artifactual. Quenching with subsequent freeze-drying was unsatisfactory because nearly all of the cell layers rolled off the cover glasses.
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PMID:Effect of fixation on demonstration of phosphatases of Eimeria tenella grown in chick kidney cell cultures. 6 Dec 71

Transverse cryostat sections of skeletal muscle were fixed in a solution containing 1.5% glutaraldehyde and 1.5% sulfosalicylic acid and stained in a solution containing equal volumes of 3% hydrogen peroxide and 50% ethanol saturated with o-tolidine. Myoglobin in the sarcoplasm of muscle fibers was precipitated and stained blue. Applicability of this method to cryostat sections, without glutaraldehyde fixations prior to freezing, allowed the myoglobin content of individual muscle fibers to be correlated with other histochemical characteristics of the same fibers seen in serial sections. In the dark red bovine sternomandibularis muscle, fibers with weak adenosine triphosphatase (ATPase) and strong succinate dehydrogenase (SDH) activity always exhibited strong myoglobin staining. An equal degree of staining was found in many fibers with strong ATPase and intermediate to strong SDH activity. Fibers with strong ATPase and weak SDH activity were less strongly stained than the preceding types.
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PMID:A method for myoglobin in cryostat sections of muscle by precipitation with sulfosalicylic acid. 9 25

After the exposure of isolated segments of guinea-pig jejunum to 2% ethanol for one hour, a significant reduction (P less than 0-001) in the adenosine triphosphate content (ATP) was observed when compared with levels found in segments perfused with Krebs' solution. However, no alteration was noted in the activity of adenosine triphosphatase (ATPase). The chronic administration of 50% ethanol in a dose of 2-5 g/kg for two weeks did not affect either the ATP content or ATPase activity in jejunal mucosa.
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PMID:Alcohol and absorption from the small intestine. 2. Effect of ethanol on ATP and ATPase activities in guinea-pig jejunum. 13 51

1. The fatty acid composition of the ole-1 and ole-1 petite mutants of Saccharomyces cerevisiae was manipulated by growing the organism in the presence of defined supplements of Tween 80 or by allowing cells that had first been grown in the presence of Tween 80 to deplete their unsaturated fatty acids by sequent growth in the absence of Tween 80. 2. The transition temperature of Arrhenius plots of mitochondrial ATPase (adenosine triphosphatase) increases as the unsaturated fatty acid content is lowered. 3. Cells require larger amounts of unsaturated fatty acids to grow on ethanol at lower temperatures. 4. Cells that stop growing owing to unsaturated fatty acid depletion at low temperatures are induced to grow further by raising the temperature and this results in a further depletion of unsaturated acids. This is due to a higher rate, but not a greater efficiency, of mitochondrial ATP synthesis. 5. Arrhenius plots of the passive permeability of mitochondria to protons between 4 and 37 degrees C are linear. The rate and the Arrhenius activation energy of proton entry increase greatly as the unsaturated fatty acid content is lowered. 6. Unsaturated fatty acid depletion has the same effects on the proton permeability of ole-1 petite mitochondria, indicating that the mitochondrially synthesized subunits of the ATPase are not involved in the enhanced rates of proton entry. 7. The adenylate energy charge of depleted ole-1 cells is greatly decreased by growth on ethanol medium. 8. The adenylate energy charge of isolated mitochondria is also lowered by unsaturated fatty acid depletion. 9. The results confirm that unsaturated fatty acid depletion uncouples oxidative phosphorylation in yeast both in vivo and in vitro, and is a consequence of changes in the lipid part of the membrane.
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PMID:The effects of unsaturated fatty acid depletion on the proton permeability and energetic functions of yeast mitochondria. 14 59

Hydrophobic agents, e.g. methanol, ethanol, isopropanol, acetone and dioxane were shown to induce irreversible inactivation of Na+, K+-adenosine triphosphatase beginning with their concentrations of 20 to 35%, whereas dimethyl sulphoxide exerted similar effect only at concentration of 50% and higher. Urea also irreversibly inactivated Na+, K+-adenosine triphosphatase, beginning with a concentration of about 20%. It was found that, dimethyl sulphoxide contrary to the other hydrophobic agents studied, protected Na+, K+-adenosine triphosphatase against the inactivating (denaturing) action of urea. The highest stabilizing effect of dimethyl sulphoxide was displayed at concentrations from 20 to 30%.
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PMID:[Stabilization of Na+, K+-adenosine triphosphatase by dimethyl sulfoxide under inactivation by urea]. 14 22

1 The specific [3H]-ouabain binding to microsomal fractions derived from cat heart, liver, spleen, and kidney increased significantly following chronic administration of ethanol. 2 Since ouabain binds exclusively to cell membrane (Na+ + K+)-adenosine triphosphatase ((Na+ + K+)-ATPase), these results provide evidence for an increase in number of (Na+ + K+)-ATPase macromolecules during chronic alcoholism. 3 The importance of the increase in number of (Na+ + K+)-ATPase molecules in the adaptive increase in ethanol metabolism and cardiac myopathy in chronic alcoholism is discussed.
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PMID:[3H]-Ouabain binding to peripheral organs of cats: effect of ethanol. 14 33

Programmed-feeding polydipsia results in a reliable model of chronic alcoholism in the rat. High oral ethanol comsumption and a predictable withdrawal reaction associated with audiogenic seizures are produced. The maintenance of high blood ethanol levels for three weeks in 18 male Charles River rats was associated with audiogenic seizures after 6 or 8 hours of withdrawal. These chronic alcoholic rats had enhanced blood clearance of ethanol. The cerebral cortical crude mitochondrial fraction showed a decrease in total and magnesium-dependent adenosine triphosphatase activity in alcoholic and control (water-fed) rats compared with normal rats.
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PMID:Programmed feeding as a model of chronic alcoholism in the rat. 15 1


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