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 possibility that the cardiac SR undergoes developmental changes at about the time of birth, and that these changes affect its ability to accumulate Ca2+ and to hydrolyse ATP has been studied. SR-rich microsomal fractions were prepared from heart muscle excised from foetal guinea pigs and rabbits 1 day before their anticipated date of birth, and from 1 day old and adult animals. For control purposes microsomes were also prepared from the relevant maternal stock animals. One day before birth the cardiac microsomes of the foetal but not of the maternal animals exhibited a decreased ability to accumulate Ca2+ by uptake but not by the binding process, and a decreased ability to hydrolyse ATP. This reduction in ATPase activity involved both the Ca2+-dependent and the Ca2+-independent ATPase enzymes. One day after birth the Ca2+-accumulating activity of the neonatal microsomes had increased, that of the rabbit via an increase in Ca2+ uptake and that of the guinea pig by an increase in Ca2+ binding. These changes were accompanied by an increase in the activity of the Ca2+-dependent ATPase. The results are interpreted to mean that the cardiac SR changes at about the time of birth, and that although the pattern of these changes may be species specific they result in an increase in the Ca2+-accumulating activity of the SR.
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PMID:Calcium accumulating and ATPase activity of cardiac sarcoplasmic reticulum before and after birth. 14 28

Shifts in the distribution of the monovalent cations Na+ and K+ between the extra- and intracellular space seem to be important for the secretory response of the beta-cell. An attempt was therefore made to study the enzyme responsible for monovalent cation transport, the (NaK)-activated ATPase. In the presence of NaN3 as inhibitor of the mitochondrial Mg-ATPase, a NaK-ATPase with a specific activity of 72 mU X mg protein-1 could be demonstrated in crude membrane preparations of rat pancreatic islets. The enzyme, which was inactive in the absence of Mg++, needed both Na+ and K+ for activation and was inhibited by ouabain and PCMB. The main part of the NaK-ATPase was localized in the microsomal fraction. Glucose, sulphonylureas, somatostatin and diazoxide were without effect on NaK-ATPase.
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PMID:NaK-ATPase in rat pancreatic islets. 14 87

Liposomes containing either purified or microsomal (Na+,K+)-ATPase preparations from lamb kidney medulla catalyzed ATP-dependent transport of Na+ and K+ with a ratio of approximately 3Na+ to 2K+, which was inhibited by ouabain. Similar results were obtained with liposomes containing a partially purified (Na+,K+)-ATPase from cardiac muscle. This contrasts with an earlier report by Goldin and Tong (J. Biol. Chem. 249, 5907-5915, 1974), in which liposomes containing purified dog kidney (Na+,K+)-ATPase did not transport K+ but catalyzed ATP-dependent symport of Na+ and Cl-. When purified by our procedure, dog kidney (Na+,K+)-ATPase showed some ability to transport K+ but the ratio of Na+ : K+ was 5 : 1.
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PMID:A reconstituted Na+ + K+ pump in liposomes containing purified (Na+ + K+)-ATPase from kidney medulla. 14 41

Effects of three diuretics on the urinary Ca2+ excretion and on the microsomal Ca2+-activated ATPase were examined in the rat kidney. Furosemide and bumetanide increased Na+, K+, and Ca2+ excretion in the rats. Acetazolamide increased Na+ and K+ excretion but not Ca2+. Urinary inorganic phosphate excretion was not affected during the administration of acetazolamide. It is suggested that acetazolamide inhibits Na+ transport without affecting Ca2+ reabsorption in the rat nephron. Microsomal ATPase of the rat kidney cortex was stimulated by Ca2+ or Mg2+ alone and an additive effect of the two cations was not observed. Microsomal ATPase activated by Ca2+ or Mg2+ was not inhibited by furosemide, bumetanide, and acetazolamide. These data suggest that the inhibitory effect of furosemide and bumetanide on the Ca2+ reabsorption is not related to the inhibition of Ca2+-activated ATPase.
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PMID:Effects of diuretics on calcium excretion and Ca2+-activated ATPase in rat kidney. 14 65

A study has been made to determine whether renal plasma membranes contain an HCO3 stimulated, ouabain insensitive Mg ATPase. Purified mitochondrial, microsomal and brush border membrane fractions have been isolated from rabbit kidney. The microsomal anion-sensitive ATPase activity appears to be entirely of mitochondrial origin on the basis of the effects of inhibitors of mitochondrial Mg ATPase. The brush border membrane fraction is contaminated with mitochondrial fragments and contains an Mg ATPase activity with low anion-sensitivity. Further purification of this fraction causes parallel decreases in anion-sensitivity of the Mg ATPase activity and in cytochrome c oxidase activity. These results indicate that conclusions previously reached by other investigators for a role of anion-sensitive Mg ATPase in the bicarbonate reabsorption of the proximal tubule may no longer be tenable.
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PMID:Is there a plasma-membrane-located anion-sensitive ATPase? II. Further studies on rabbit kidney. 14 30

Depletion of divalent cations before fractionation of the longitudinal muscle of the guinea pig ileum yielded a sarcolemma-enriched microsomal fraction free of mitochondria. A major portion of the ATPase activity in the presence of Mg, Na, and K was due to stimulation by Na alone. A further small stimulation by K was demonstrated only in the presence of an activating factor from the 105 000 X g supernatant. Ouabain inhibited only the K activation and had no effect on the Na-stimulated Mg-ATPase.
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PMID:The effect of ouabain on the guinea pig ileum longitudinal smooth muscle: 1. ATPase activities in a sarcolemma-enriched fraction prepared with the aid of divalent cation depletion of the intact muscle. 14 50

1. The influence of various Na+ concentrations on [3H]-ouabain binding was studied in experiments on a microsomal Na+-K+-adenosine triphosphatase (ATPase) from guinea-pig hearts. 2. The ATP-independent cardiac glycoside binding was not influenced by increasing Na+ concentrations. However, a good correlation was found between the ATP-dependent [3H]-ouabain binding and Na+ concentration. 3. A more detailed analysis of these results according to Hofstee (1952) revealed two distinct processes involved in this interaction: one ouabain binding process was activated at rather low Na+ concentrations, (K0.5 = 4.5 mM); this type of [3H]-ouabain binding was strongly correlated to the Na+ concentration necessary for half maximum phosphorylation (K0.5 = 1 mM). The other ouabain binding process was predominant at high Na+ concentrations (K0.5 = 69 mM). 4. On the basis of the commonly accepted ATPase reaction cycle a model for the interaction of cardiac glycosides with the Na+-K+-ATPase is proposed, assuming two different binding sites for cardiac glycosides (E2-P and E1-P) and involving a translocation of these drugs from an outer to an inner compartment of the cell membrane.
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PMID:Evidence for two different Na+-dependent [3H]-ouabain binding sites of a Na+-K+-ATPase of guinea-pig hearts. 14 57

Adult mallard ducks were fed a diet containing 50 ppm DDT for 6 months. Eggs laid during this period were collected and eggshell weight, thickness, and calcium were determined. Chronic ingestion of DDT resulted in production of eggshells that were significantly thinner and lighter than those of controls. Total calcium of thinned eggshells was also reduced; however, calcium per gram of eggshell was not altered, indicating that other eggshell constituents were not incorporated as well. Calcium adenosine triphosphatase activity in the microsomal fraction of eggshell gland epithelium was assayed in control and DDT-fed ducks. Enzyme activity in DDT-fed ducks was reduced to 65% of control values. Since Ca-ATPase has been shown to be associated with calcium transport, enzyme inhibition may be responsible for decreased eggshell weight and thickness. Electron microscopic evaluation of microsomal fractions showed elements of the plasma membrane, including cilia and microvilli, as well as rough and smooth endoplasmic reticulum. Inhibition of calcium transport at the plasma membrane of mucosal epithelium is proposed as a possible mechanism of DDT-induced eggshell thinning.
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PMID:Effects of DDT on eggshell quality and calcium adenosine triphosphatase. 14 96

Dietary polyethylene glycol (PEG) induces an increase in the specific activity of Na+-K+-activated adenosine triphosphatase (Na-K-ATPase) in the cecum mucosa of rats. Using cecum mucosa homogenates and cellular subfractions obtained by differential centrifugation, the induction process was studied with respect to time course, subcellular distribution and properties of the enzyme. In comparison with controls, Na-K-ATPase specific activity was stimulated in PEG treated rats in the total homogenate and the microsomal (105000 X g) but not in the mitochondrial (9000 X g) or nuclear (1000 X g) sediment. The specific activity of Mg-ATPase did not change in any of the fractions. Na-K-ATPase induction was statistically significant after 2 days and complete after 1-2 weeks, in parallel with the previously described stimulation in net sodium absorption. Kinetic analysis showed Vmax for ATP to be doubled while Km for ATP, Na and K as well as the optimal Mg/ATP ratio and Ki for ouabain remained unchanged. It is proposed that Na-K-ATPase and active sodium transport are closely associated in rat cecum and that dietary Na-K-ATPase stimulation is due to the induction of more enzyme molecules per unit basolateral cell membrane.
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PMID:Induction of Na-K-ATPase in plasma membranes to rat cecum mucosa by diet: time course and kinetics. 14 84

The effect of acetaldehyde, the hepatic metabolite of alcohol, on the functioning of cardiac muscle was investigated at the subcellular level. Concentrations of acetaldehyde that occur in plasma failed to alter either the microsomal Ca2+-accumulating and ATPase activity or the Ca2+-accumulating activity of the mitochondria. These same concentrations of acetaldehyde inhibited the Ca2+-dependent myofibrillar ATPase.
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PMID:Effect of acetaldehyde on functioning of cardiac muscle at the ultrastructural level. 14 33


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