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

---

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

1. Slices of rat cerebral cortex, incubated anaerobically at 37 degrees , lost K(+) from an initial concentration of 102m-equiv./kg. to a concentration of 57m-equiv./kg. after 10min. On subsequent aerobic incubation they regained K(+) rapidly at a rate that varied with the K(+) concentration of the medium. 2. Lower aliphatic alcohols, present at equal thermodynamic activity, produced approximately equal degrees of inhibition of K(+) uptake during the aerobic incubation. This inhibition was reduced by an increase in K(+) content of the medium. Ethanol did not affect the rate of K(+) loss during anaerobic incubation. 3. Li(+), in concentrations of 1-10mm, also inhibited K(+) uptake by brain-cortex slices, the degree of inhibition varying with the Li(+) concentration. Ouabain also inhibited K(+) uptake. 4. The same series of alcohols, at equal thermodynamic activity, produced comparable degrees of inhibition of Na(+),K(+),Mg(2+)-stimulated adenosine-triphosphatase activity in brain microsomes. 5. It is suggested that inhibition of cation transport is an important, but not a primary, mechanism in the production of central nervous depression by alcohols and other substances.
...
PMID:Effects of lower alcohols on potassium transport and microsomal adenosine-triphosphatase activity of rat cerebral cortex. 422 75

The isozymes of NaK-ATPase were studied in the particulate fraction of homogenates prepared from cortex of LS and SS mice, two lines of mice that have been selectively bred for differential response to ethanol. In addition to a ouabain-insensitive Mg-ATPase, ouabain dose-response curves have suggested the presence, in brain, of two NaK-ATPase activities with different sensitivities to ouabain. These are designated low Ki (4 X 10(-7) M) and high Ki (2 X 10(-4) M). Ethanol differentially inhibited the ATPases: The ouabain-insensitive activity was less sensitive to ethanol inhibition than were the two ouabain-inhibitable activities. The low Ki (brain specific) NaK-ATPase was more sensitive than was the high Ki activity. However, ethanol inhibited all three components of the ATPase activity in an identical fashion in the two mouse lines. The low Ki activity was also more labile to thermal and p-hydroxymercurobenzoate denaturation than was the high Ki activity. These measures did not differ between the LS and SS lines. SDS-polyacrylamide electrophoresis of particulate fraction of cortical homogenates obtained from LS and SS mice revealed the presence of two protein bands with similar 32P labeling in both lines. Given that electrophoretic pattern and heat or p-hydroxymercurobenzoate inhibition were identical, it seems unlikely that differences in ATPase activity, or inhibition by ethanol, are responsible for the different response of LS and SS mice to ethanol.
...
PMID:Brain NaK-ATPases in mice differentially sensitive to alcohols. 609 91

The effects of ethanol on the activities of five membrane bound enzymes were determined using a crude membrane preparation obtained from cortex of long-sleep (LS) and short-sleep (SS) mice. These two mouse lines were selectively bred for differences in duration of ethanol-induced sleep time. The enzymes studied were two forms of NaK-ATPase, Mg-ATPase, 5'nucleotidase, and acetylcholinesterase. Arrhenius plots of the ethanol-temperature-enzyme activity studies indicate specificity in ethanol's actions. NaK-ATPase activity consists of two enzymes which were distinguished by sensitivity to ouabain. The Arrhenius plot of the high ouabain sensitivity enzyme (low Ki) exhibited a transition temperature which was reduced twice as much by ethanol in LS membranes as in SS membranes. Ethanol did not affect the transition temperature of the high Ki NaK-ATPase but the control (no ethanol) transition temperature was 2.7 degrees higher in SS membranes. Arrhenius plots of Mg-ATPase activity did not exhibit a transition temperature and ethanol did not alter enzyme activity. Ethanol did not alter the transition temperatures of 5'nucleotidase or acetylcholinesterase but the control transition temperature for acetylcholinesterase was 2.3 degrees higher in SS membranes. These results indicate specificity in ethanol's actions on membranes and that inhibition of the lipid-enzyme interactions for the low Ki NaK-ATPase is correlated with the difference in sensitivity to ethanol seen between the LS and SS mice.
...
PMID:Ethanol and temperature effects on five membrane bound enzymes. 615 1

Sarcoplasmic reticulum (SR) of high purity and functional integrity was isolated from skeletal muscle of normal and ethanol-tolerant rats. Ethanol at low concentrations (0.1 to 0.2 M), added in vitro to isolated SR, resulted in slight inhibition of both calcium loading and calcium-stimulated ATPase rates. Higher concentrations of ethanol resulted in further inhibition of calcium loading, but not of calcium-stimulated ATPase. Fluorescence polarization of 1,6-diphenyl-1,3,5-hexatriene (DPH) in isolated SR membranes showed a small decrease in anisotropy with the addition of ethanol in vitro. Sarcoplasmic reticulum from normal and ethanol-tolerant rats did not differ in calcium pump function or in fluorescence polarization of DPH, in the presence or absence of ethanol.
...
PMID:Calcium transport and fluorescence polarization of 1,6-diphenyl-1, 3,5-hexatriene in sarcoplasmic reticulum from normal and ethanol-tolerant rats. 622 40

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.
...
PMID:Effect of ethanol on early stages in nitrosamine carcinogenesis in rat liver. 622 54

Muscle ion composition, Na-K-ATPase activity, tissue respiration, and transmembrane potential differences were measured after 28 and 56 days of ethanol consumption (6.2 g X kg-1 X day-1) or an isocaloric amount of glucose in 12 and 4 dogs, respectively. Ethanol and glucose were given as supplements to an otherwise nutritious diet. After 28 and 56 days of alcohol consumption, skeletal muscle contents of phosphorus, magnesium, and potassium were significantly reduced as compared with either the control values or those in glucose-fed animals. In alcohol-fed animals, muscle sodium chloride, and calcium were significantly elevated. Ethanol consumption also resulted in hyperpolarization of the resting transmembrane potential of skeletal muscle fibers and a significant increase in Na-K-ATPase activity. No change was noted in Mg-ATPase activity. The increase in Na-K-ATPase activity was accompanied by increased sodium transport-dependent respiration. These results indicate that a subclinical myopathy may be induced by alcohol in the dog. Malnutrition did not appear to be a factor in this study, and thus the changes observed are believed to be due to ethanol per se. The magnitude and direction of these changes are similar to those observed in the skeletal muscle of chronically alcoholic humans. The changes in Na-K-ATPase activity and sodium transport-dependent respiration may represent adaptive responses of the muscle cell to ion transport or membrane disorders induced by ethanol.
...
PMID:Derangements of muscle composition, ion transport, and oxygen consumption in chronically alcoholic dogs. 623 59

Neurochemical changes which are associated with the development or expression of tolerance to or physical dependence on ethanol may be expected to display a time course of appearance and disappearance which correlates positively with the time course for tolerance or dependence. Previous studies of striatal dopaminergic receptor function indicated that ethanol-withdrawn mice displayed decreased physiological and biochemical responses to dopamine (DA) agonists, which could be best explained by postulating an inefficient coupling between DA receptors and various receptor-mediated processes, possibly as a result of ethanol-induced changes in neuronal membrane properties. The membrane-bound enzyme, (Na+-K+)ATPase, obtained from ethanol-withdrawn animals, displays an altered transition temperature and resistance to the effects of ethanol on enzyme activity. These changes also suggest compensatory alterations in neuronal membrane properties. All of these alterations show a time course of disappearance which corresponds to that for the disappearance of tolerance to the hypothermic and sedative effects of ethanol. Ethanol-withdrawn mice also display increased numbers of hippocampal muscarinic cholinergic receptors; however, the time course for the increase in receptor number appears to correlate with that of withdrawal symptomatology. Thus, compensatory changes in neuronal membrane properties in response to ethanol may be expressed via diverse functional changes.
...
PMID:Receptor and membrane function in the alcohol tolerant/dependent animal. 625 71

In the United States and other developed countries thiamin deficiency is often related to chronic alcoholism. A number of mechanisms may be involved in the pathogenesis of thiamin deficiency in the alcoholic population. An important cause is inadequate intake of thiamin. Moreover, there may be decreased converstion of thiamin to the active coenzyme, reduced hepatic storage of the vitamin in patients with fatty metamorphosis, ethanol inhibition of intestinal thiamin transport, and impaired thiamin absorption secondary to other states of nutritional deficiency. The present discussion focuses on the mechanism of ethanol-related thiamin malabsorption. Under normal conditions thiamin transport in animals and humans is biphasic. At low or physiological thiamin concentrations, transport is a saturable, carrier-mediated, active process; but at higher concentrations, the transport of thiamin is predominantly passive. Ethanol reduces the rate of intestinal absorption and the net transmural flux of thiamin. Furthermore, ethanol inhibits only the active and not the passive component of thiamin transport by impeding the cellular exit of thiamin across the basolateral or serosal membrane. The impairment of thiamin movement out of the enterocyte correlates with a fall in the activity of Na-K ATPase. Bound to the basolateral membrane, Na-K ATPase is believed to be involved in the kinetics of active transport. Ethanol also increases the fluidity of enterocyte brush border and basolateral membranes. Since ethanol increases membrane fluidity it is possible that tahe impairment of thiamin transport and the diminution of Na-K ATPase activity may be related, at least partly, to a physical perturbation of the enterocyte membrane.
...
PMID:Mechanisms of thiamin deficiency in chronic alcoholism. 625 54

In this report the disturbances in biochemistry of the heart muscle exposed to alcohol are delineated. All elements of cellular substructures are affected. In plasma membranes, (Na+ + K+)-activated ATPase (EC 3.6.1.3) is inhibited. Mitochondrial damage consists in diminished respiratory function and calcium uptake and binding. High-energy phosphates remain intact. Alcohol also affects the malate-aspartate shuttle. Acetaldehyde, a metabolite of ethanol, has a direct effect on myocardial protein synthesis through microsomal inhibition; however, the development of cardiac hypertrophy is not affected. Malfunction of sarcoplasmic reticulum is evidenced by disturbances in calcium binding and uptake. Effects of ethanol on the contractile machinery are deficiencies in the turnover rate of chemical into mechanical energy (diminished Vmax), and in the number of cross-bridges formed (P0). It increases stiffness of series elastic elements. There is diminished fatty acid oxidation with increased esterification. The involvement of CoA synthetase (EC 6.2.1.1), palmityl-carnitine transferase (EC 2.3.1.7), and pyruvate dehydrogenase complex in disturbed fatty acid oxidation is not certain. The role of catalase in myocardial ethanol oxidation was examined. Ethanol activates myocardial catalase-H2O2 complex (EC 1.11.1.6). The biochemical basis of fetal alcohol syndrome is low hepatic alcohol dehydrogenase (EC 1.1.1.1) activity during fetal life.
...
PMID:Effect of alcohol on the heart and cardiac metabolism. 628 54

To determine whether and how ethanol and acetaldehyde alter brain oxidative metabolic activity, reduction/oxidation shifts of components of the mitochondrial respiratory chain were optically measured, in situ, from cat cerebral cortex. Oxidative shifts of nicotinamide adenine dinucleotide (NADH) were recorded in response to increased energy demand provoked by stimulation of the cortical surface by electrical pulses. Ethanol or acetaldehyde did not alter the direction of the responses but each slowed the rates of oxidation with little effect upon the rates of subsequent re-reduction. There was no apparent change produced by either drug upon the kinetics of the negative shifts of the cortical steady potential in response to the stimulation. However, stimulus-evoked electrical and metabolic responses were decreased in amplitude with increasing drug doses. It is suggested that the slowed mitochondrial oxidation results from inhibition of Na+, K+-ATPase. This supports the concept that ethanol or acetaldehyde inhibit the processes that lead to increased oxygen consumption following cell depolarization in vivo, as has been demonstrated in vitro.
...
PMID:Ethanol and acetaldehyde alter brain mitochondrial redox responses to direct cortical stimulation in vivo. 629 68


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---