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)

Ca-dependent ATPase activity in the rat anterior pituitary was demonstrated in 50-microns tissue slices of aldehyde-fixed tissue with the medium of Takano et al. (Cell Tissue Res. 243:91. 1986).--The outer surface of the plasma membrane of the parenchymal as well as the folliculo-stellate cells was lined with lead precipitate. The reaction deposit was particularly well localized in intercellular spaces both between two parenchymal cells, and between a parenchymal and a folliculo-stellate cell. A fine reaction deposit was also seen in the endoplasmic reticulum and Golgi apparatus of some parenchymal cells. Elimination of Ca2+ from the tissue and the substrate medium drastically reduced the amount of reaction product. If ATP was omitted or replaced by sodium beta-glycerophosphate, no reaction product was seen. Changing the Ca2+ concentration or addition of Mg2+ to the standard medium caused a decrease in reaction intensity. Substitution of Mg2+ for Ca2+ resulted, again in well-localized lead deposition which we attribute to the activity of another enzyme. We suggest that the activity we described in the membrane of glandular cells may correspond to the enzyme involved in the long-term regulation of intracellular Ca2+ level.
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PMID:Ultrastructural study of the Ca2+-dependent ATPase activity in rat adenohypophyseal cells. 252 36

(Na+,K+)ATPase activity of rat liver plasma membranes was evaluated in female rats feeding an ethanol containing diet for 46 days (total ethanol ingested, 59.7 g/100 g body wt). Determinations were performed at the end of ethanol treatment or at various times after stopping treatment. (Na+,K+)ATPase and 5'-nucleotidase activities exhibited a 8- and 1.4-fold decrease, respectively, at the end of ethanol ingestion. In contrast no modifications of Mg2+-ATPase activity were observed. There also occurred, in ethanol-treated rats, release of sorbitol dehydrogenase into the blood, fat accumulation in liver cells, and decrease in reduced glutathione (GSH) liver content. A decrease in (Na+,K+)ATPase activity was also found in plasma membranes isolated from hepatocyte suspensions after a 2-hr incubation with 50 mM ethanol or 1 mM acetaldehyde (ACA), in conditions that caused a great fall in hepatocyte GSH content but did not cause cell death. After the cessation of ethanol administration, there occurred a progressive recovery of (Na+,K+)ATPase activity, GSH and triacylglycerol content, and release of sorbitol dehydrogenase. These parameters reached control values 12 hr after ethanol withdrawal. S-Adenosyl-L-methionine (SAM), L-methionine, and N-acetylcysteine (NAC), given to rats during ethanol treatment, prevented the decrease in (Na+,K+)ATPase activity and GSH content. They also reduced steatosis and liver necrosis. The efficiency of these compounds decreased in this order: SAM, methionine, NAC. SAM accelerated the recovery of all parameters studied after ethanol withdrawal, and also protected (Na+,K+)ATPase activity and GSH content of isolated hepatocytes from the deleterious effect of ethanol. These SAM effects were prevented by 1-chloro-2,4-dinitro-benzene, a compound which depletes cell GSH. Treatment of isolated hepatocytes with [35S]SAM led to the synthesis of labeled GSH. The total amount and specific activity of labeled GSH underwent a significant increase, in the presence of 2 mM ethanol or 0.5 mM ACA, which indicates a marked stimulation of GSH synthesis by ethanol and ACA. These data indicate that ethanol intoxication may inhibit (Na+,K+)ATPase activity; an effect that does not seem to depend on cell necrosis. SAM, methionine, and NAC exert various degrees of protection toward ethanol-induced cell injury, which are related to the efficiency of these compounds in maintaining a high GSH pool.
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PMID:Inhibition by ethanol of rat liver plasma membrane (Na+,K+)ATPase: protective effect of S-adenosyl-L-methionine, L-methionine, and N-acetylcysteine. 253 5

Maternal alcohol consumption produces various abnormalities in the offspring, termed fetal alcohol syndrome. We investigated various biochemical modifications occurring in the brain and the liver of pups born to alcohol-consuming rats. The parameters analysed were: superoxide dismutase, a protector against free radicals injury, enolase isoenzymes as markers of nerve cell maturation, glutamine synthetase involved in ammonia detoxification, alcohol and aldehyde deshydrogenases in order to evaluate the contribution of acetaldehyde teratogenicity and ATPase activities involved in ion and neurotransmitter transport. Activities of all these enzymes were decreased in the brain even when alcohol was withdrawn from the mother diet either during pregnancy or lactation. Activities were also decreased in the liver, except enolase and alcohol deshydrogenase activities, which were increased, suggesting possible adaptative events in the presence of alcohol. It seems likely that the multiple alterations observed in experimental fetal alcohol syndrome may be caused by free radicals following decreased superoxide dismutase activity in addition to the toxicity of alcohol and its metabolites.
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PMID:An experimental study of fetal alcohol syndrome in the rat: biochemical modifications in brain and liver. 256 12

The inhibition of myofibrillar ATPase activity by aldehyde fixation in tissue pieces of myocardium of the rat was measured by scanning histophotometry. The relative amount of the final reaction product of the histochemical method for ATPase (Padykula and Herman 1955) was taken as a measure for the enzyme activity. Along scanning lines in slides from the surface to the centre of tissue block, a higher activity was found in the centre in contrast to the marginal zone. Compared with the centre of the block (approximately equal to 100%), in the marginal region a loss of about 40% (in paraformaldehyde PFA) and of 75% (in glutaraldehyde GA) was found, the latter with a sharp decline between the marginal zone and the central part. For quantitative enzyme histochemistry by histophotometry unfixed material is recommended.
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PMID:Histophotometrical measurements concerning the distribution of myofibrillar ATPase activity within the tissue block after aldehyde fixation. 296 14

Kinetic studies on the action of monoamine oxidase (MAO) in the regulation of Na+,K+-ATPase were performed using 3-methoxy-4-hydroxybenzaldehyde (MHB), which is an analogue of 3-methoxy-4-hydroxy-phenylacetylaldehyde (product of MAO-catalysed reaction with dopamine as substrate). It was observed that at 2.6 microM MHB, the activation of Na+,K+-ATPase may be the result of the removal of the inhibitory Ca2+, thereby increasing the Vmax. Double-reciprocal plots of Pi versus MHB showed that Ca2+ counteracted the effect of the aldehyde not by changing the Km, but be decreasing the Vmax of the Na+,K+-ATPase stimulation. The removal of 3',5'-cyclic AMP-dependent protein kinase from the microsomes by sodium dodecyl sulphate treatment abolished the activation and/or inhibition of the Na+,K+-ATPase by aldehyde; it can therefore be inferred that 3',5'-cyclic AMP-dependent protein kinase is involved in the regulation of Na+,K+-ATPase.
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PMID:Kinetics of the mechanism of action of monoamine oxidase in the regulation of Na+,K+-ATPase activity in rat brain. 298 Nov

The effect of chronic acetaldehyde inhalation on (Na+ + K+)-ATPase (EC 3.6.1.3) activities of subcellular fractions of the rat cerebral cortex was studied. Chronic administration of acetaldehyde by inhalation for 4-21 weeks caused significant increases in the enzyme activities of both the synaptosomal plasma membrane (SPM) fraction and the microsomal (MC) fraction. This indicates the change in neural membrane functions of the brain after acetaldehyde treatment. Mg2+-ATPase activities of both subcellular fractions remained unchanged after acetaldehyde treatment.
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PMID:Effect of chronic administration of acetaldehyde by inhalation on (Na+ + K+)-activated adenosine triphosphatase activity of rat brain membranes. 298 17

Changes in the properties of rat liver plasma membranes were examined in studies designed to differentiate between direct and metabolic effects of acute and chronic ethanol ingestion. One hour after a single dose of ethanol (3 g/kg body weight) there were increases in Na+,K+-ATPase (32%) and 5'-nucleotidase (36%), and hepatic concentrations of ethanol and acetaldehyde were approximately 23 mM and 50 microM, respectively. Na+,K+-ATPase and 5'-nucleotidase activities in liver plasma membranes from control rats were not significantly changed by in vitro addition of 30 microM acetaldehyde or 50 mM ethanol. Increases in Na+,K+-ATPase (approximately 20%) and 5'-nucleotidase (approximately 30%) were also observed in liver plasma membranes isolated from rats 16 hr after feeding ethanol or sucrose supplements for 17 days. The intake of calories from dietary protein and lipid was decreased by about 25% in both the ethanol and sucrose-fed animals. Na+,K+-ATPase activities in liver plasma membranes isolated from control rats were inhibited (approximately 20%) by 100 mM ethanol in vitro, whereas no inhibition was observed using membrane preparations from rats fed ethanol or sucrose supplements. Our results show that changes in liver plasma membrane enzyme activities associated with a single dose of ethanol are not a direct effect correlated with blood, hepatic or plasma membrane concentrations of ethanol or acetaldehyde. Chronic ingestion of ethanol or sucrose supplements had similar effects on liver plasma membrane enzyme characteristics and parallel changes in nutrient intake may be a more feasible explanation of these results than any analogous direct effects of the two compounds.
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PMID:Effects of ethanol administration on rat liver plasma membrane-bound enzymes. 299 Apr 93

Myosin subfragment 1 (S1) can be specifically photomodified at the active site without polypeptide chain cleavage by irradiating the stable MgADP-orthovanadate-S1 complex with UV light above 300 nm [Grammer, J. C., Cremo, C. R., & Yount, R. G. (1988) Biochemistry (preceding paper in this issue)]. Here, the UV spectral properties of photomodified S1 were used to determine the nature and location of the photomodified residue(s) within S1. By comparison of the unusual pH dependence of the UV absorption spectrum of the photomodified S1 to that of the S1-MgADP-Vi complex as a control, the photomodified residue(s) was (were) localized to the 23-kDa NH2-terminal tryptic peptide of the heavy chain. NaBH4 reduced the photomodified S1, but not the control, to regenerate the original spectral properties and ATPase activities of the unmodified S1. Amino acid analysis of photomodified S1 reduced with NaB3H4 gave only [3H]serine, suggesting the hydroxyl group of serine had been oxidized to a "serine aldehyde". The pH dependence of the absorption spectrum of the photomodified enzyme can be explained by an equilibrium between a chromophoric enolate anion of the serine aldehyde (favored in base) and less chromophoric keto and enol forms (favored in acid). The oxidized serine(s) was (were) shown to be directly involved with the vanadate-dependent photocleavage of the S1 heavy chain previously described by Grammer et al. (1988). This serine(s) is (are) likely to be important to the binding and hydrolysis of the gamma-PO4 of ATP at the active site of S1.
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PMID:UV-induced vanadate-dependent modification and cleavage of skeletal myosin subfragment 1 heavy chain. 2. Oxidation of serine in the 23-kDa NH2-terminal tryptic peptide. 314 5

The lead salt method introduced by Wachstein and Meisel (12) for the cytochemical demonstration of ATPase activity was modified and used to determine sites of activity on red cell ghost membranes. Preliminary studies showed that aldehyde fixation and standard concentrations of the capture reagent Pb(NO(3))(2) resulted in marked inhibition of the ATPase activity of these membranes. By lowering the concentration of Pb(2+) and incubating unfixed red cell ghosts, over 50% of the total ATPase activity, which included an ouabain-sensitive, Na-K-activated component, could be demonstrated by quantitative biochemical assay. Cytochemical tests, carried out under the same conditions, gave a reaction product localized exclusively along the inner surfaces of the ghost membranes for both Mg-ATPase and Na-K-ATPase. These findings indicate that the ATPase activity of red cell ghosts results in the release of P(i) on the inside of the ghost membrane at sites scattered over its inner aspect. There were no deposits of reaction product on the outer surface of the ghost membrane, hence no indication that upon ATP hydrolysis P(i) is released outside the ghosts. Nor was there any clear difference in the localization of reaction product of Mg-ATPase as opposed to that of Na-K-ATPase.
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PMID:The localization of Mg-Na-K-activated adenosine triphosphatase on red cell ghost membranes. 422 35

A method has been developed for calculating rate constants for dehydration of aldehydes that induce ATPase reactions by kinases and where 18O is transferred from the aldehyde or its hydrate to inorganic phosphate during the reaction. The method involves measurement of the fraction of 18O in phosphate by 31P NMR after the ATPase reaction has proceeded for several minutes with zero-order kinetics. The reaction is started by addition of the aldehyde in a small volume of H2 18O, and the speed of washout of 18O by reversible dehydration relative to the rate of the ATPase reaction allows calculation of the rate constants if the hydration equilibrium constant is known from the proton NMR spectrum of the aldehyde. Dehydration rate constants (s-1 at pH 8-8.5, 0.1 M buffer, 25 degrees C) for the following aldehydes (all over 95% hydrated) and kinases used are as follows: D-glyceraldehyde with glycerokinase, 0.03; 2,5-anhydro-D-mannose 6-phosphate with fructose-6-phosphate kinase, 0.025; 2,5-anhydro-D-mannose or 2,5-anhydro-D-talose with fructokinase, 0.029 and 0.017, respectively; D-gluco-hexodialdose with hexokinase, 0.068. With betaine aldehyde and choline kinase or glyoxylate and pyruvate kinase, no 18O was transferred to phosphate during the ATPase reactions. However, the dehydration rate constant for glyoxylate (0.007 s-1 at pH 7 extrapolated to zero buffer concentration and up to 0.11 s-1 at pH 9.0 with 0.3 M buffer) was determined by extrapolating the initial rate of reduction of the free aldehyde catalyzed by lactate dehydrogenase to infinite enzyme levels.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:A novel method for determining rate constants for dehydration of aldehyde hydrates. 609 90


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