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)

The pH optimum of the ATPase activity in plasma membranes from Saccharomyces cerevisiae NCYC 431 from 8 h cultures was around 6.5 and that in membranes from organisms from 16 h cultures near 6.0. The Km[ATP] of the enzyme was virtually unaffected by the age of the culture from which organisms were harvested, although the Vmax of the enzyme in membranes from organisms from 8 h cultures was higher than that for organisms from 16 h cultures. Ethanol non-competitively inhibited ATPase activity in membranes, although the inhibition constant for the enzyme from organisms from 8 h cultures was lower than that from organisms from 16 h cultures. Glycine accumulation by the general amino acid permease was non-competitively inhibited by ethanol. Inhibition constants were virtually the same for glycine uptake by deenergized organisms from 8 h and 16 h cultures, but under energized conditions the value was greater for organisms from 16 h rather than 8 h cultures. The data indicate that inhibition of plasma-membrane ATPase activity by ethanol could account, at least in part, for inhibition of glycine accumulation by ethanol.
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PMID:Effect of ethanol on activity of the plasma-membrane ATPase in, and accumulation of glycine by, Saccharomyces cerevisiae. 295 98

The Na+,K+-ATPase activity of human leucocytes was assayed by measuring the release of inorganic phosphate (Pi) from ATP. The maximum enzyme activity was achieved under the following conditions: concentration (mmol/l), Tris/HCl 50, Na 100, K 15, ATP 5, Mg 7, EDTA 1; pH 7.2 and temperature 37 degrees C, were optimal. Ouabain showed maximal inhibition at a concentration of 10-100 mumol/l. Ethanol, the solvent for ouabain, had a dose-related inhibitory effect. Heparin or citrate used as an anticoagulant gave similar results. Leucocyte samples could be stored at -20 degrees C for up to 6 days without loss of activity. Hypotonic lysis had advantages over sonication as the technique for cell disruption. The leucocyte Na+,K+-ATPase enzyme activity in healthy subjects was 186 mumol of Pi h-1g-1 of protein (median) with a range 136-243 mumol of Pi h-1g-1 of protein. The within-batch coefficient of variation was 6.4% and the between-batch precision was 9.6%.
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PMID:Optimal conditions for measurement of Na+,K+-ATPase activity of human leucocytes. 298 51

Norepinephrine (0.1 mM) has been reported to "sensitize" (Na+ + K+)-ATPase activity of rat brain homogenates to inhibition by ethanol. The present study extends these investigations to the mouse and includes other ATPase activities. We measured the effects of norepinephrine on the sensitivity of ethanol-induced inhibition of (Na+ + K+)-stimulated (E.C. 3.6.1.3), (Mg++)-dependent (E.C. 3.6.1.4) and (Ca++)-dependent ATPase activities. Whole forebrains from C57BL/6J mice were homogenized and assayed in vitro for ATPase activity using standard conditions. Ethanol (0.125-2.0 M) caused a dose-dependent inhibition of all three ATPases. Norepinephrine (0.1 mM) had no appreciable effect on ethanol's inhibition of (Na+ + K+)-stimulated or (Ca++)-dependent ATPase activities, but slightly antagonized ethanol's effect on (Mg++)-ATPase. These results suggest that norepinephrine has little effect on the sensitivities of specific ATPases to ethanol inhibition in mouse brain.
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PMID:Effect of norepinephrine on inhibition of mouse brain (Na+ + K+)-stimulated, (Mg++)-dependent, and (Ca++)-dependent ATPase activities by ethanol. 299 May

Mechanisms of alcoholic liver disease are still ill defined. We evaluated in two outbred lines of mice whether chronic ingestion of ethanol alters the lipid composition and/or enzyme activity of liver plasma membranes. Two mouse lines with different sensitivities towards the hypnotic effect of ethanol, designated long sleep and short sleep, were fed a liquid diet containing ethanol for 30 days. Ethanol intake reached 30 gm per kg per day in both lines, and serum ethanol levels were similar. In addition, hepatic triglyceride levels were similarly increased 2-fold with ethanol feeding. The following effects of ethanol treatment were observed in liver plasma membrane fractions: (i) Na+,K+-ATPase was significantly increased to 26% above control in long sleep only; (ii) alkaline phosphatase activity was 2-fold increased in both lines; (iii) 5'-nucleotidase, leucine aminopeptidase and Mg2+-ATPase activities remained unchanged in both lines; (iv) unesterified cholesterol and total phospholipid contents were unaltered in both lines, and (v) cholesteryl esters were increased in both lines, but to a greater extent in short sleep (1.5 vs. 4-fold). Thus, chronic ethanol ingestion induces specific alterations in liver plasma membrane structure and function, suggesting that adaptive responses to ethanol may be determined in part by inherited factors.
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PMID:Effect of chronic ethanol administration on enzyme and lipid properties of liver plasma membranes in long and short sleep mice. 299 Nov 3

Neuronal membrane enzyme activities were determined in naive and ethanol-treated (30 min after 2 g/kg) male and female rats of lines developed for more (ANT) and less (AT) ethanol-induced motor impairment. Ethanol did not affect acetylcholinesterase, (Na+K)-ATPase or 5'-nucleotidase activities, but adenylate cyclase activities were lowered in both cerebellum and cerebrum. Cerebral acetylcholinesterase activities were higher in ANT than AT rats. No consistent line difference was observed regarding (Na+K)-ATPase activities. Slightly higher cerebellar 5'-nucleotidase activities were found in the ANT line. Cerebellar adenylate cyclase levels were substantially higher in the AT line. No line differences were displayed in the activation of adenylate cyclase activity by dopamine or norepinephrine. It is concluded that ethanol in vivo may inhibit neuronal adenylate cyclase activity and that cerebellar phosphorylation may be a regulator of motor impairment. Cholinergic mechanisms may also be connected to the ethanol-induced motor impairment.
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PMID:Neuronal membrane enzymes in rat lines selected for differential motor impairment by ethanol. 301 92

Isolated gastric glands from rabbit, as well as basolateral and microsomal membranes derived therefrom, were used to examine the effect of ethanol on several parameters related to acid secretion. Low concentrations of ethanol, 0.2%-5% (vol/vol), had no effect on basal aminopyrine accumulation by isolated gastric glands but significantly potentiated aminopyrine accumulation stimulated by histamine. In contrast, this dose range of ethanol inhibited aminopyrine accumulation stimulated by forskolin or dibutyryl-cyclic adenosine monophosphate. This dose range of ethanol produced a similar effect on adenylate cyclase activity of basolateral membranes from isolated gastric glands, with potentiation of histamine stimulation and inhibition of forskolin stimulation. Low-dose ethanol was found to produce increased proton permeability of the apical membrane of the parietal cell but had no effect on hydrogen-potassium-stimulated adenosine triphosphatase activity. Ethanol (10%) significantly inhibited all parameters of acid secretion studied. Ethanol has a biphasic effect on acid secretion with potentiation of histamine-stimulated aminopyrine accumulation and adenylate cyclase activity at low doses and inhibition of all parameters of acid secretion at high doses.
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PMID:Effect of ethanol on acid secretion by isolated gastric glands from rabbit. 301 11

The in vitro effects of ethanol on C57BL/6J mouse forebrain ATPase activities were investigated in the presence and absence of norepinephrine. Three enzyme activities (Na + K-ATPase, Mg-ATPase, and low affinity Ca-ATPase) were studied in forebrain homogenates using a colorimetric assay. The effect of norepinephrine on ethanol inhibition of Sprague-Dawley rat brain Na + K-ATPase activity was examined in selected experiments for direct comparison with the results obtained using mouse brain. Ethanol (250-2000 mM) inhibited all ATPase activities in a concentration-dependent manner. In each case the IC50 was well beyond what would be a lethal concentration in vivo. Ethanol inhibition of mouse forebrain Na + K-ATPase activity was competitive with regards to K+ ion concentration, but was uncompetitive for inhibition of Mg-ATPase and Ca-ATPase activities. Norepinephrine (0.1 mM) did not sensitize mouse brain Na + K-ATPase activity to ethanol-induced inhibition. In contrast, norepinephrine sensitized rat brain Na + K-ATPase to ethanol inhibition when tested simultaneously with mouse brain under identical conditions. These results cannot be explained by differences in assay conditions and suggest that the interaction between norepinephrine and ethanol inhibition of Na + K-ATPase activity may be species specific. Norepinephrine alone stimulated mouse and rat brain Na + K-ATPase activity when assayed in imidazole buffer, but not when assayed in tris buffer. Furthermore, 0.1 mM norepinephrine slightly antagonized the inhibitory effect of ethanol on mouse brain Mg-ATPase activity, but did not affect ethanol-induced inhibition of Ca-ATPase activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Ethanol-induced inhibition of mouse brain adenosine triphosphatase activities: lack of interaction with norepinephrine in vitro. 302 99

The experiments in this paper examined interactions between ethanol and repeated noradrenergic stimulation in vivo on regulation of (Na+,K+)-ATPase. The increase in ouabain binding and K+-phosphatase activity associated with (Na+,K+)-ATPase in rats treated with repeated yohimbine injections was prevented by chronic ethanol. Ethanol did not affect the yohimbine-induced alterations in noradrenergic receptor binding or in content of the norepinephrine metabolite 3-methoxy-4-hydroxyphenylglycol, showing that prevention of noradrenergic stimulation of (Na+,K+)-ATPase was not caused by a decrease in availability of norepinephrine. In addition, norepinephrine depletion with the neurotoxin DSP4 did not prevent the increases in (Na+,K+)-ATPase indices during chronic ethanol treatment, showing that they did not result from increased norepinephrine exposure. These results suggest that chronic ethanol reduces sensitivity of (Na+,K+)-ATPase to norepinephrine in vivo, possibly as a consequence of membrane effects of ethanol tolerance.
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PMID:(Na+,K+)-ATPase and noradrenergic function: effects of chronic ethanol. 303 51

Plots of ouabain inhibition of mouse cerebral cortical (Na+,K+)ATPase activity fitted a two-site model significantly better than a one-site model, consistent with the presence of two forms of the enzyme with different affinities for ouabain. The fraction of enzyme activity with high affinity for ouabain (HAO: Ki = 500 nM), suggested to be localized neuronally, constituted the major portion (60-70%) of activity. Ouabain inhibition of both components of enzyme activity was reduced as KCl concentrations were increased. In vitro, only high concentrations of ethanol affected (Na+,K+)ATPase activity and ouabain inhibition of activity. Ethanol (500 mM) selectively reduced the activity, and increased the sensitivity to ouabain inhibition, of the HAO component, with no significant effect on the low-affinity (LAO) component. On the other hand, following chronic treatment of mice with ethanol in vivo, in a paradigm that produced tolerance and physical dependence, the sensitivity to ouabain of the HAO form of the enzyme was selectively increased. The relative proportions, and the activities of the HAO and LAO components, were not altered. The effects of ethanol, added in vitro, on the HAO component were decreased in ethanol-tolerant animals. The selective effect of chronic ethanol ingestion on (Na+,K+)ATPase activity indicates the specificity of action of ethanol in the CNS.
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PMID:Effects of ethanol on ouabain inhibition of mouse brain (Na+,K+)ATPase activity. 303 59

Ethanol has a wide range of biochemical and behavioral effects. Many of these can be explained by the ability of ethanol to reduce the amount of order, or increase the fluidity, in biological membranes. During chronic ethanol administration, membrane fluidity in the absence of ethanol and the sensitivity of membrane fluidity to added ethanol are decreased. Changes in membrane lipid composition that are consistent with decreased fluidity or with resistance to ethanol including increases in membrane cholesterol, reductions in the double bond index of phospholipid acyl chains, and increases in anionic phospholipids, have been reported during ethanol treatment. These changes are not found uniformly, however, and membrane tolerance and resistance have been reported in their absence. A variety of changes in lipid metabolism have been reported; their possible relevance to these adaptive changes is discussed. Ethanol treatment affects several transport systems in membranes; Na+, K+-ATPase, Ca++-ATPase, and other Ca++ transport systems all appear to undergo adaptive changes during ethanol treatment. Alterations in these systems may account for some of the effects of ethanol on activity-dependent energy metabolism and neurotransmitter release. Paradoxes in the membrane actions of ethanol remain to be resolved, including the weakness of membrane fluidization by ethanol in vitro compared to the evidence that it occurs in vivo, and the consistency with which adaptive changes in membrane fluidity and in Na+, K+-ATPase are observed compared to the inconsistency in changes in membrane composition.
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PMID:Membrane effects of ethanol in excitable cells. 331 Jan 32


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