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)

Genetically obese (ob/ob) mice, mice that became obese after treatment with gold thioglucose, and lean animals were studied in the euthyroid state, after induction of hypothyroidism, and after treatment with triiodothyronine. The activity of glycerol 3-phosphate dehydrogenase (sn-glycerol-3-phosphate:(acceptor) oxidoreductase; EC 1.1.99.5] was reduced in the livers from hypothyroid animals and was increased by treatment with triiodothyronine in all groups. The activity of the ouabain-suppressible sodium- and potassium-dependent ATPase (ATP phosphohydrolase; EC 3.6.1.3) was increased by triiodothyronine and reduced by hypothyroidism in the lean and gold thioglucose-treated obese animals. In the obese (ob/ob) mice, on the other hand, treatment with triiodothyronine did not increase the activity of this enzyme, which remained at the level found in hypothyroid animals. This enzymatic activity was reduced in both liver and kidney. Adenylate cyclase [ATP pyrophosphate-lyase (cyclizing); EC 4.6.1.1] activity in liver membranes, however, was similar in all three groups of mice. This enzyme complex was activated by glucagon and was unaffected by treatment with thyroid hormones. The lack of a thyroid-dependent ouabain-suppressible (Na(+) + K(+))-ATPase in the tissues of the obese (ob/ob) mouse could explain most, if not all, of the abnormalities that have been described in this animal.
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PMID:An enzymatic defect in the obese (ob/ob) mouse: loss of thyroid-induced sodium- and potassium-dependent adenosinetriphosphatase. 14 80

The regulation of adrenergic receptors in rat heart was measured in rats made hyperthyroid by injection with thyroxine and made hypothyroid by addition of propylthiouracil to the drinking water. Hyperthyroid rats display cardiac hypertrophy and a decrease in epididymal fat pad weight. The maximal beta-receptor level of ventricular membranes, as determined by (-)-[3H]dihydroalprenolol binding, was increased 60% by thyroxine treatment and decreased about 30% by propylthiouracil treatment. The affinity of the beta receptor was unchanged after thyroxine or propylthiouracil treatment. The maximal activity of the isoproterenol-stimulated adenylate cyclase (EC 4.6.1.1) varied with thyroid state in a manner parallel to the increase in beta-adrenergic binding sites. Thyroxine treatment also increases by 2-fold the beta receptors in isolated rat fat cells. Propylthiouracil treatment lowered the level of alpha receptors in heart by 30% as measured by [3H]dihydroergocryptine binding, but increased the affinity about 2.5-fold. The highest level of alpha receptors was seen in control hearts. These studies indicate that thyroxine may control the turnover of beta-adrenergic receptors in heart and fat cells and regulate physiological responses in these tissues via a hormone-hormone interplay system. Thyroxine treatment reduced the activity of the membrane-bound Mg2+-ATPase (EC 3.6.1.3) and 5'-mononucleotidase (EC 3.1.3.5) but appears to increase the activity of the (Na+ + K+)ATPase (EC 3.6.1.4).
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PMID:Hormone action at the membrane level. VIII. Adrenergic receptors in rat heart and adipocytes and their modulation by thyroxine. 14 63

Activity of specific mitochondrial enzymes was studied in rat liver during 2-acetylamine fluorene or diethylnitrosamine-induced hepatocancerogenesis. The results of enzymatic activities studied correlated with morphological changes in cancerogenesis. Alterations in activity of monoamine oxidase, adenylate cyclase and adenosine triphosphatase depended on the step of cancerogenesis. Activity of adenylate cyclase in cell membranes decreased gradually during the impairment. Change in activity of the enzymes, observed at the step of enhanced liver cell proliferation, proceeded at further steps of cancerogenesis. The data obtained suggest that alterations in activity of mitochondrial enzymes are related to modified metabolism observed in the impaired cells.
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PMID:[Changes in the activity of monoamine oxidase, adenylate cyclase and adenosine triphosphatase in liver cells during the process of hepatocarcinogenesis]. 15 Jul

Cytochemical techniques have been employed to study the localization of adenylate cyclase and (Ca2+ + Mg2+)-stimulated ATPase activities in platelets after fixation. Biochemical analysis of adenylate cyclase demonstrated a 70% reduction in activity in homogenates from fixed cells, but the residual activity could be stimulated 10--20 times by prostaglandin E1 (1 micrometer) under the same incubation conditions as employed in the cytochemical studies (e.g. media containing 2 mM lead nitrate and 10 mM NaF). Adenylate cyclase activity employing 5'-adenylyl-imiodiphosphate (AMP-P(NH)P) as substrate was found to be associated with the dense tubular system (smooth endoplasmic reticulum) in intact fixed platelets, and was apparent only when the cells were incubated with prostaglandin E1. Less activity was found along the membranes of the surface connected open canalicular system and occasionally at the outer cell surface. Enzymatic activity was blocked by the adenylate cyclase inhibitor 9-(tetrahydro-2-furyl) adenine and was not due to AMP-P(NH)P phosphohydrolase activity. The low adenylate cyclase activity in the surface membranes may be due to enzyme inactivation as a result of fixation, since a surface membrane fraction obtained by the glycerol lysis technique from unfixed cells had an adenylate cyclase specific activity equivalent to that in the microsomal membrane fraction. (Ca2+ + Mg2+)-stimulated ATPase activity was found associated with the membranes of the surface connected open canalicular system in unfixed cells. After brief fixation (5--15 min) with glutaradehyde, strong (Ca2+ + Mg2+)ATPase activity became apparent in the dense tubular system. Longer periods of fixation inactivated enzymatic activity. Addition of Ca2+ (1.0 mM) to incubation medium with low Mg2+ (0.2 mM), or increasing Mg2+ to 4.0 mM, in both cases strongly stimulated enzyme activity. The ATPase activity in the platelet membranes was not inhibited by ouabain. It is suggested that the Ca2+-stimulated ATPase and adenylate cyclase activities in the dense tubules may possibly be involved in regulation of intracellular Ca2+ transport.
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PMID:Cytochemical localization of adenylate cyclase and of calcium ion, magnesium ion-activated ATPases in the dense tubular system of human blood platelets. 15 Aug 66

1. Pancreatic plasma membranes containing a high adenylate cyclase activity and a low contamination by cytochrome c oxidase were isolated from the rat by sucrose density centrifugation. The preparation contained an (Mg,Ca)-ATPase of high activity with the following characteristics. 2. The ATPase activity was shown to have two apparent Km values for Mg-ATP (0.24 +/- 0.09 mM and 1.15 +/- 0.21 mM) and two apparent Km values for Ca-ATP (0.14 +/- 0.09 mM and 0.68 +/- 0.10 mM). Mg-GTP and Ca-GTP were also hydrolysed by the preparation. The phase transition temperature was 19.3 +/- 1.0 degrees C for the Mg-ATPase and 22.6 +/- 1.1 degrees C for the Ca-ATPase activities. 3. Three lines of evidence suggest that Mg-ATP and Ca-ATP were substrates for the same enzyme: Mg-dependent and Ca-dependent activities were not additive; the two activities showed the same pH optimum at 8.0; and the nonionic detergents Triton X-100, Triton X-305, Triton N-101, Lubrol P 12 A, and digitonin, produced a parallel solubilization of the two activities. 4. Enzyme activities were insensitive to potassium, sodium, ouabain, pancreozymin, carbamoyl-choline, secretin, concanavalin A, wheat germ agglutinin, and soybean lectin.
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PMID:Characterization of (Mg,Ca)-ATPase activity in rat pancreatic plasma membranes. 15 27

Platelets were examined to enable a simultaneous investigation to be made of indolylamine and electrolyte metabolism in affective disorder. No significant differences were detected in either platelet membrane ATPase or adenyl cyclase specific activity in any of the groups of patients studied, when compared with appropriate controls. A reduced Vmax and y for the 5-hydroxy-tryptamine uptake process into platelets was observed in both unipolar and bipolar depressed groups. The Km for this process was not significantly different in any of the patients from that found in control subjects. Lithium therapy was shown not to influence significantly any of the platelet parameters examined. It is suggested that membrane enzyme changes found in some peripheral cells in patients suffering from affective disorder, i.e. reduced Na+ + K+ - ATPase activity in erythrocytes in depression, is not common to all peripheral cells and may or may not reflect central nervous system changes.
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PMID:Studies on human blood platelets in affective disorder. 15 82

The effects of sodium pentobarbital on ATPase, Ca2+ binding and adenylate cyclase activities of the rat heart sarcolemmal preparations were investigated. The Na+ - K+ ATPase activity was diminished by pentobarbital in concentrations as low as 0.3 mM. Mg2+ ATPase, Ca2+ ATPase and adenylate cyclase activities were also depressed but required 10 to 15 mM of this agent. Pentobarbital in concentrations of 10 mM, however, caused an increase in sarcolemmal Ca2+ binding. Mitochondrial and microsomal ATPase activities were decreased by 1 and 5 mM concentrations of pentobarbital respectively, while myofibrillar ATPase activity was unaltered even at a concentration of 20 mM. These data suggest that cardiodepressant effects of high doses of pentobarbital may partly be explained on the basis of its actions on heart sarcolemma.
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PMID:Effects of sodium pentobarbital on rat heart sarcolemma. 15 80

The purpose of this study was to determine whether the previously reported differences in adenylate cyclase activity between the sarcolemma of normal and dystrophic chick muscles are also found in the SR, to search for a possible relationship between the adenylate cyclase changes and the pathophysiology of dystrophy, and to investigate whether the findings can be extended to Duchenne human muscular dystrophy by studying the adenylate cyclase and ATPase activities of erythrocyte ghosts from DMD patients and carriers. Microsomes were separated by standard techniques from the pectoralis muscles of normal and dystrophic ckeckens of various ages. The microsomal yields were significantly larger in dystrophic muscles. Adenylate cyclase activities in dystrophic microsomes were higher than those in matched controls and increased with the progression of the disease. The ratio between the two rose from one at 2 weeks of age to nine at about 9--10 weeks. Kinetic analyses showed that the ks for MgATP2- was about 40 microM (at 3 mM Mg2+ and 0.3 mM Ca2+) both in normal and dystrophic microsomes, that calcium caused umcompetitive inhibition of the enzyme (Ki = 0.2 mM), that the effect of calcium was noncooperative (Hill coefficient, nH = 1), that calcium did not affect the cooperativity for MgATP2-, and that magnesium competitively removed the calcium inhibition and caused additional, cooperative stimulation of the enzymatic activity (ka = 1.5 mM; NH =2). The major difference between normal and dystrophic adenylate cyclase was a higher enzymatic velocity in the latter, suggesting a larger amount of enzyme. We investigated whether altered cAMP levels may effect calcium accumulation. Calcium uptake measured (in the presence of oxalate) at several ages revealed no difference between normal and dystrophic chickens. The extent of calcium binding was also similar, although the kd for Ca2+ was lower in dystrophic microsomes. Binding was enhanced in the presence of exogenous protein kinase, but the responses of normal and dystrophic tissues were similar. We concluded that the elevation of adenylate cyclase in dystrophy was not related to microsomal calcium accumultion. Ivestigation of the localization of microsomal adenylate cyclase supported this view. Separation of calcium-loaded microsomes on a discontinuous sucrose gradient into four fractions demonstrated that adenylate cyclase activity, measured in the presence of Lubrol-PX and EGTA, was inversely related to calcium-accumulating activity. Na+, K+-ATPase comigrated with adenylate cyclase. Highest specific activities were found in the lightest fraction. These observations were confirmed by histochemical studies. The reaction product from adenylate cyclase activity was present predominantly in the terminal cisternae of the SR. In the context of the literature, our findings suggest that the rises in adenylate cyclase and Na+, K+-ATPase in avian dystrophy are compensatory changes, elicited by a defect in ECC at the calcium release step...
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PMID:Adenylate cyclase in muscular dystrophy. 15 10

Basal adenylate cyclase activity was increased in red cell ghosts from both patients with Duchenne muscular dystrophy and their mothers when the activities were compared to proper age-matched controls. The activity of ATPase measured in the presence of Na+, K+, and Mg2+ was not found to be different in erythrocyte ghosts from Duchenne dystrophic patients, age-matched controls, or the mothers of Duchenne patients, and ouabain inhibited ATPase in ghosts to the same extent in all membrane preparations.
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PMID:Adenylate cyclase and ATPase activities in red cell membranes of patients and genetic carriers of Duchenne muscular dystrophy. 15 46

We found considerable differences in the pattern of membrane proteins as well as in the relative amounts of individual components in isolated chick red blood cell membranes during the course of embryonic development. Of special interest in the increase in the relative amounts of two major polypeptides, band 3 and 3.1 (MW 100,000 daltons) with increasing age of the cells. With respect to functional studies, we found that the magnitude of sulfate influx decreases with increasing age of the embryo. Furthermore, the activity of ouabain-sensitive ATPase increases with increasing age (2.5-day embryo to adult). In addition, both the basal and the fluoride-stimulated adenylate cyclase activities decrease as the embryo age increases, whereas the enzyme sensitivity to epinephrine increases with increasing age of the embryo.
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PMID:Changes in membrane structure and function during chick embryonic erythropoiesis. 15 95


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