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)

Comparison between the effects on various rat liver mitochondrial functions of ethacrynate, a thiol reagent inhibitor of oxidative phosphorylations [3, 4] and those of dihydroethacrynate its saturated derivative which is not a thiol reagent, has been performed. Both, ethacrynate and dihydroethacrynate increase oxygen consumption by mitochondria in state 4 (succinate as substrate) in a concentration dependent way (from 1 to 5 X 10(-4) M EA or DHEA). This activation is followed, only with ethacrynate, by an inhibition appearing sooner with higher concentrations. After preincubation or mitochondria with ethacrynate (1 to 5 X 10(-4) M), the stimulation of respiration by (ADP + Pi) is completely inhibited whereas it is only weakly affected by dihydroethacrynate at the same concentrations. Ethacrynate and dihydroethacrynate provoke variations of intramitochondrial Mg2+ and K+ levels which need energy from the respiratory chain. These are affected by Pi or (Pi + ADP) in a different way with ethacrynate and with dihydroethacrynate. After preincubation with mitochondria, ethacrynate and to a smaller extent dihydroethacrynate, inhibit partially ADP translocation; ADP increases the inhibitory effect of EA on translocation and not that of dihydroethacrynate. Ethacrynate increases the oligomycin sensitive ATPase activity and dihydroethacrynate still more. After a ten minutes preincubation with mitochondria, ethacrynate and dihydroethacrynate hardly affect the 2.4 DNP stimulated ATPase activity. Preincubation with succinate or ADP strongly increases the ethacrynate inhibition whereas it decreases dihydroethacrynate inhibition. Ethacrynate and dihydroethacrynate do not affect the efflux of Pi produced by ATP hydrolysis but ethacrynate enforces the inhibitory effect of mersalyl (Mg2+ containing medium). After ten minutes of preincubation with mitochondria, ethacrynate binds 25 nmoles of -SH/mg protein (DTNB titration) and dihydroethacrynate has no effect. These results show an effect of ethacrynate on two types of thiols linked with energy conservation mechanisms and ADP translocation. These thiols could be unmasked or made accessible by conformational modifications of the inner membrane upon energization or addition of ADP.
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PMID:Thiols related to mitochondrial ATPase and transports: unmasking upon conformational changes supported by the comparative effects of ethacrynate and dihydroethacrynate. 13 33

Disrupted cells of Bdellovibrio bacteriovorus exhibited adenosine triphosphatase activity, 60 to 80% of which was in the soluble fraction. Dicyclohexylcarbodiimide did not inhibit the adenosine triphosphatase activity in membrane particles. The particles did not show energy-linked transhydrogenase activity. The activity of non-energy-linked transhydrogenase as well as the rate of oxygen consumption were higher in membrane particles of the host-independent strain than in the host-dependent strains. The uptake of amino acid uptake was inhibited by cyanide and by carbonyl cyanide p-trifluoromethoxyphenyl hydrazone. Valinomycin, in the presence of K+, did not inhibit the uptake, and only partial inhibition was exerted by arsenate and dicyclohexylarbodiimide. Sulfhydryl reagents inhibited amino acid uptake.
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PMID:Membrane-associated, energy-linked reactions in Bdellovibrio bacteriovorus. 13 28

The total Mg2+-ATPase and Na+, K+-ATPase activity was studied in the fractions of "400 g X for 20 min" and "900 g X for 30 min" conditionally called the fraction of the external cellular membranes and total fraction of mitochondria. The subcellular fractions were isolated from great hemispheres and stem part of the rat brain. The brain of control animals and those during a severe spasmodic attact induced by the oxygen action at a pressure of 6 ati was studied. The total ATPase activity is established to be practically the same in the studied brain areas and unchanged with hyperoxia. Hyperoxia accompanying by convulsions results in an increase in the activity of Mg2+-ATPase and in a decrease in that of Na+, K+-ATPase both in the cerebral cortex and the stem part. The authors suppose that the decrease in the enzyme activity may occur due to an inhibitory effect on it of the lipids reoxidation products formed in the brain with hyperoxia.
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PMID:[ATPase activity of subcellular rat brain fractions following hyperoxia]. 13 79

The effects of a moderate physical training program on the hearts of rats have been studied. The mechanical responses of these hearts are improved. Possible contributing factors in this improvement are increased coronary reserve and capacity to deliver oxygen to the myocardium, increased myocardial glycogen stores and increased turnover of fatty acids through the endogenous triglyceride pool. Myocardial oxidative compounds and high energy phosphate stores are not altered. Major changes are found in the energy utilization pathways. Actomyosin, myosin, and heavy meromyosin ATPase activity and binding activity of isolated sarcoplasmic reticulum are all enhanced. Sulfhydryl control of the active site of myosin ATPase is altered. The biochemical effects of conditioning are short lived when training is decreased or discontinued.
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PMID:Effects of physical training and detraining on intrinsic cardiac control mechanisms. 13 72

Increased pressure of O2, N2,or He exert inhibitory or stimulatory effects on activity of Na-K-Mg ATPase obtained from beef brain cortex. Oxygen at 2 ATA and N2 at 4 ATA exert significant inhibitory effects whereas 3 & 4 ATA O2, 1-3 ATA N2 exert significant stimulatory effects. Effects of He on ATPase activity are qualitatively similar to those of N2. The effects of the gases are not qualitatively altered by the presence or absence of ATP. A pressure compensated analysis reveals that at the same pressures, O2 and N2 exert different effects of ATPase activity.
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PMID:Effect of increased pressures of oxygen, nitrogen, and helium on activity of a Na-K-Mg ATPase of beef brain. 13 12

The involvement of membrane (Na+ + K+)-ATPase (Mg2+-dependent, (Na+ + K+)-activated ATP phosphohydrolase, E.C. 3.6.1.3) in the oxygen consumption of rat brain cortical slices was studied in order to determine whether (Na+ + K+)-ATPase activity in intact cells can be estimated from oxygen consumption. The stimulation of brain slice respiration with K+ required the simultaneous presence of Na+. Ouabain, a specific inhibitor of (Na+ + K+)-ATPase, significantly inhibited the (Na+ + K+)-stimulation of respiration. These observations suggest that the (Na+ + K+)-stimulation of brain slice respiration is related to ADP production as a result of (Na+ + K+)-ATPase activity. However, ouabain also inhibited non-K+ -stimulated respiration. Additionally, ouabain markedly reduced the stimulation of respiration by 2,4-dinitrophenol in a high (Na+ + K+)-medium. Thus, ouabain depresses brain slice respiration by reducing the availability of ADP through (Na+ + K+)-ATPase inhibition and acts additionally by increasing the intracellular Na+ concentration. These studies indicate that the use of ouabain results in an over-estimation of the respiration related to (Na+ + K+)-ATPase activity. This fraction of the respiration can be estimated more precisely from the difference between slice respiration in high Na+ and K+ media and that in choline, K+ media. Studies were performed with two (Na+ + K+)-ATPase inhibitors to determine whether administration of these agents to intact rats would produce changes in brain respiration and (Na+ + K+)-ATPase activity. The intraperitoneal injection of digitoxin in rats caused an inhibition of brain (Na+ + K+)-ATPase and related respiration, but chlorpromazine failed to alter either (Na+ + K+)-ATPase activity or related respiration.
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PMID:Control of brain slice respiration by (Na+ + K+)-activated adenosine triphosphate and the effects of enzyme inhibitors. 13 40

The oxygen requirement of the Na-K-ATPase-dependent sodium transport system was examined in anesthetized dogs infused with 15% mannitol-Ringer solutions at a rate of 35 ml/min. Because of renal vasodilatation and abolished autoregulation, filtered sodium (FNa) could be varied over a wide range by progressive aortic constriction. Sodium reabsorption (RNa) and renal oxygen consumption (RVO2) varied in proportion to FNa (r greater than 0.9). Ouabain, which inhibits Na-K-ATPases, reduced RVO2 by 45 +/- 6%. During subsequent aortic constriction, the ratio delta RNa/delta FNa averaged 0.45 (glomerulotubular balance) (r less than 0.9), whereas RVO2 was not significantly altered. Comparisons of deltaRNa/deltaFNa before and after ouabain administration, indicate that about half of an increase in sodium delivery to the distal nephron is reabsorbed by the Na-K-ATPase-dependent sodium transport system and that deltaRNa/deltaRVO2 (Na/O2 ratio) of this system averages 14.5 +/- 1.3. This Na/O2 ratio corresponds to 2.4 sodium ions transported per ATP dephosphorylated as found in other tissues.
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PMID:Oxygen requirement of renal Na-K-ATPase-dependent sodium reabsorption. 13 8

The main parameters of contraction and relaxation of papillary muscle strips taken from the left ventricle of control and exercise-adapted rats were measured. The contractile velocity and amplitude of thin and thick strips of the cardiac muscle of adapted rats were found to be 2--3 times higher than in the controls. This fact can be explained by an elevation of myosine ATP-ase activity. The developed tension was higher than in the controls only in thick strips of adapted rats. This increase depends on the adaptive augmentation of the functional power of systems responsible for the transport of oxygen and substrates to the mitochondria. The myocardium of adapted rats differed from that of the controls in that the relaxation velocity and compliance were significantly elevated. These facts suggested an increase in the funcitonal power of the ionic transport system that is responsible for Ca++ elimination from the myofibrils. In general, the results suggest that an elevation of maximal myocardial performance after adaptation to exercises may be due to a coordinative increase in the power of three basic systems of the myocardial cells--ion transport system, myosine ATPase and resynthesis ATP system.
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PMID:[Mechanism of increasing the functional capacity of the cardiac muscle after adaptation to physical exertion]. 13 93

An adenosine triphosphatase (ATPase) mutant of Bacillus megaterium was isolated and characterized. This mutant (designated A37) was unable to grow on nonfermentable carbon sources and possessed less than 5% of the wild-type ATPase activity. Oxygen uptake by the mutant was comparable to that in the wild type. Sporulation in the wild type occurred in both glucose- and nitrogen-limiting media; however, A37 sporulated only in the nitrogen-limiting medium. The inability of A37 to sporulate in glucose-limiting medium seemed to be due to insufficient adenosine 5'-triphosphate (ATP) levels during the sporulation stages. Fructose, which can generate ATP via substrate-level phosphorylation, is equally efficient in stimulating ATP synthesis in the wild type and A37. Malate-stimulated ATP synthesis in the wild type was shown to have many characteristics associated with oxidative phosphorylation and was absent in the mutant. These data suggest that the ATPase deficiency results in the loss of oxidative phosphorylation.
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PMID:Bacillus megaterium mutant deficient in membrane-bound adenosine triphosphatase activity. 14 49

Effect of circulatory, hypoxic and cytotoxic hypoxia on the ATPase activity was studied in mitochondrial fractions of brain, heart and liver tissues and in nuclear fractions of brain and liver tissues. All types of oxygen deficiency caused alterations in the activity of enyzmes studied. The observed alterations in the ATPase activity possessed the distinct phase type.
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PMID:[Effect of experiment hypoxia on the ATPase activity of brain, liver and myocardial nuclei and mitochondria]. 14 67


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