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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of Mg2+-activated, ouabain-sensitive adenosine triphosphatase, (Na+-K+)-ATPase, was determined in homogenates of hypothalamus, cortex, cerebellum, and brain stem from the 19-day-old offspring of rats that were pair-fed control or (6.6%, v/v) ethanol liquid diets on a chronic basis prior to parturition. In the offspring of both control and ethanol-fed rats the specific activity of (Na+-K+)-ATPase was significantly (p less than 0.01) greater in the cortex than it was in the hypothalamus, brain stem or cerebellum (hypothalamus approximately brain stem approximately cerebellum). When the offspring of ethanol-fed and control rats were compared we observed no significant (p greater than 0.05) differences in the activity of (Na+-K+)-ATPase in any of the four brain regions examined. In addition, the results of kinetic analyses of cortical (Na+-K+)-ATPase were similar in the 19-day-old offspring of ethanol-fed rats and those whose mothers consumed either the control liquid diet or standard laboratory chow. The results of these studies suggest that the activity of the plasma membrane enzyme, (Na+-K+)-ATPase, was not affected in the 19-day-old offspring of ethanol-fed rats.
Alcohol
PMID:Maternal ethanol consumption: effect on (Na+-K+)-ATPase in rat offspring. 299 11

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

Chronic feeding of male Wistar rats with food containing hexachlorobenzene (HCB) at 17.5 mmol/kg induced elevation of serum amino-transferases and bilirubin content, increase of microsomal cytochrome P-450 concentration, and decrease of 5'-nucleotidase, K+,Na+- and Mg2+-adenosine triphosphatase activities in liver plasma membrane preparations. These changes were potentiated by ethanol consumption suggesting a possible role of liver plasma membrane damage in the pathogenesis of HCB intoxication.
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PMID:Rat liver plasma membrane damage in hexachlorobenzene intoxication and its potentiation by ethanol. 302 30

Effects of K+, ethanol and norepinephrine on the binding kinetics of ouabain to (Na+,K+)-adenosine triphosphatase in beef brain microsomes were examined. K+ reduced the rate and apparent affinity for ouabain binding markedly. Whereas ethanol and norepinephrine themselves inhibited ouabain binding slightly, they stimulated binding in the presence of K+. Norepinephrine enhanced the effect of ethanol. Dissociation of ouabain was biphasic, with fast and slow components corresponding to high and low apparent affinity. About 65% of the enzyme had high affinity, regardless of conditions. Norepinephrine and ethanol had differential effects on the rate of dissociation from high and low affinity enzyme, however. Alpha receptor blockade generally prevented the effects of norepinephrine. These results show that, although norepinephrine and ethanol have a modest effect on the amount of enzyme that can bind ouabain, their main effect on (Na+,K+)-adenosine triphosphatase is to antagonize the binding of K+ to its allosteric site that inhibits ouabain binding. The data support the hypothesis that ouabain binds rapidly to a K+-insensitive form of phosphorylenzyme or to its dephosphorylated analog and dissociates rapidly from E1.
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PMID:Ouabain binding to brain (Na+,K+)-adenosine triphosphatase: interactions of K+, ethanol and norepinephrine with high- and low-affinity binding. 302 3

Male Wistar rats fed for 60 days a glucose diet containing 17.5 mmol hexachlorobenzene/kg show a less pronounced increase in serum parameters and microsomal cytochrome P-450 concentration and a lower decrease in liver plasma membrane 5'-nucleotidase, K+, Na+- and Mg++-adenosine triphosphatase activities than the controls fed standard diet + hexachlorobenzene. Addition of 10% ethanol to the drinking water eliminates the "glucose effect". The glucose diet and ethanol exert contrasting effects on microsomal enzyme induction and liver plasma membrane damage in hexachlorobenzene intoxication.
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PMID:Interaction between glucose diet and ethanol on rat liver microsomal induction and liver plasma membrane damage in chronic hexachlorobenzene intoxication. 361 33

The aim of this study was to investigate possible mechanisms involved in the elevation of serum alkaline phosphatase activity in alcoholics. Male Sprague-Dawley rats were pair-fed nutritionally adequate liquid diets containing ethanol as 36% of energy or an isocaloric amount of carbohydrate for 4-5 wk. Serum alkaline phosphatase activity was increased moderately but significantly. Hepatocytes isolated from ethanol-fed animals exhibited pronounced morphologic alterations of their plasma membranes by scanning electron microscopy and a reduced content of alkaline phosphatase despite an increase in total liver alkaline phosphatase content. Chronic ethanol feeding also potentiated the release of alkaline phosphatase from the cells during incubation with 50 mM ethanol. Furthermore, chronic ethanol feeding resulted in reduced recovery of alkaline phosphatase in hepatic plasma membranes isolated by sucrose gradient centrifugation but did not affect the recoveries of other plasma membrane markers (5'-nucleotidase and Na+,K+-adenosine triphosphatase) nor the subcellular distribution of alkaline phosphatase in the nuclear, mitochondrial, microsomal, and cytosolic fractions. These findings suggest that the increased serum alkaline phosphatase levels observed in response to chronic ethanol feeding may be due, at least in part, to increased lability of this plasma membrane enzyme.
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PMID:Chronic ethanol consumption alters rat liver plasma membranes and potentiates release of alkaline phosphatase. 403 95

Isocaloric replacement of either the fat or carbohydrate content of the diet by ethanol (36% of the total caloric intake) produced fatty infiltration of the liver in rats. The increase in hepatic triglyceride content was associated with a decrease in both ATP and glycogen contents. Increased activity of mitochondrial Mg(2+)-stimulated adenosine triphosphatase paralleled the increase in the free P(i) content of the liver homogenate. During the regression of the fatty liver, glycogen contents returned to normal within 24h of the removal of ethanol from the diet. Not until the third day after the withdrawal of ethanol had the Mg(2+)-stimulated adenosine triphosphatase activity and free P(i) content of the homogenate returned to normal. A slow regression of the triglyceride content from the liver occurred and by the fifth day both ATP and triglyceride concentrations had returned to the values observed in the rats given the liquid control diet.
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PMID:Biochemical aspects associated with an ethanol-induced fatty liver. 425 Aug 48

Brain (Na+ + K+)-adenosine triphosphatase activity from untreated rats was inhibited by a combination of 1 microM norepinephrine + 50 mM ethanol (NE + EtOH), in preparations from cerebral cortex (CX), cerebellum (CB), hippocampus (HC), hypothalamus (HT), thalamus-midbrain and pons-medulla, but not from striatum. The rank order of inhibition in these regions was more similar to that of alpha-1 receptor density than of regional NE content. EtOH administration for 3 weeks produced tolerance to the hypothermic effect of EtOH; increased basal adenosine triphosphatase activity in CX, CB and HC, as measured 24 hr after withdrawal; and decreased the inhibitory effect of NE + EtOH in CX, HT, HC and CB preparations. Tolerance to the inhibitory effects of high concentrations (0.22 or 0.44 M) of EtOH alone was found only in CX, HT and HC preparations. Tolerance to NE + EtOH or to EtOH alone was greatest in HC and CX, intermediate in HT and CB and least or absent in other regions. Temperature-dependence of (Na+ + K+)-adenosine triphosphatase activity was studied in preparations from CX (high initial sensitivity to NE + EtOH, high tolerance development), CB (intermediate initial sensitivity, intermediate tolerance) and striatum (no initial sensitivity, no tolerance). Arrhenius plots showed differences between these regions, with respect to changes in transition temperature and activation energy after chronic EtOH treatment in vivo. These changes did not explain the regional differences in tolerance development. Therefore it seems unlikely that a single mechanism, such as "stiffening" of the cell membrane, can explain the varied pattern of tolerance development in different brain regions.
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PMID:Effect of ethanol tolerance on norepinephrine-ethanol inhibition of (Na+ + K+)-adenosine triphosphatase in various regions of rat brain. 609 18

The effect of chronic alcohol consumption on the extent of adenosine triphosphatase(ATPase)-deficient preneoplastic lesions in rat liver induced by either diethylnitrosamine (DEN) (3 mg/kg, p.o.) or N-nitrosomorpholine (NNM) (40 ppm in the drinking water) was studied. Carcinogens were administered on 4 days in every week for 11 (DEN) and 15 (NNM) weeks, respectively. Ethanol was given at a concentration of 10% (w/v) in the drinking water either during carcinogen treatment or after withdrawal of carcinogen. An increase in both number and size of ATPase-deficient foci in liver was observed when the alcohol was given during the period of carcinogen administration. This increase may be associated with the known toxic action of ethanol which leads to single cell necrosis and liver regeneration. In contrast, when ethanol (10% in the drinking water for 16 weeks) was given after cessation of carcinogen treatment following a tumor-promotion feeding protocol, no such enhancement in preneoplastic response was obtained. Ethanol alone was ineffective in inducing ATPase-deficient foci. In liver, ethanol thus appears to possess, under certain conditions, co-carcinogenic but not tumor-promoting capacity.
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PMID:Effect of ethanol on early stages in nitrosamine carcinogenesis in rat liver. 622 54

(Na+-K+) activated adenosine triphosphatase of mouse synaptosomal membranes is inhibited by high concentrations of ethanol. When membranes were obtained from mice made tolerant to and physically dependent on ethanol by chronic exposure to an ethanol-containing liquid diet, the enzyme was resistant to the inhibitory effects of ethanol. Arrhenius plots of synaptosomal (Na+-K+) activated adenosine triphosphatase from control animals revealed that ethanol added in vitro lowered the transition temperature and altered the Arrhenius activation energies of this enzyme. Enzyme from ethanol-tolerant animals had a lower transition temperature than that from control animals, and ethanol added in vitro had no effect either on transition temperature or on activation energy of enzyme from ethanol-tolerant animals. The occurrence of lowered transition temperature and resistance to ethanol-induced alterations in transition temperature of the enzyme from ethanol-tolerant animals most likely reflects changes in membrane composition. Changes in Arrhenius plots correlated in time with resistance to the inhibitory effects of ethanol on (Na+-K+) activated adenosine triphosphatase activity and the time course of disappearance of these effects was similar to that of the disappearance of functional tolerance to ethanol. The resistance to the effects of ethanol on membrane function may be related to ethanol tolerance evidenced by behavioral and physiological measurements.
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PMID:Sodium-potassium-activated adenosine triphosphatase activity as a measure of neuronal membrane characteristics in ethanol-tolerant mice. 624 62


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