Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using the incubated isolated rat retina, the effects of hyaluronidase on the electroretinogram (ERG) and metabolic activities were investigated. Initial experiments established the activity of hyaluronidase needed to liquefy, within 15 to 30 minutes, the vitreous of postmortem human eyes; this concentration was 1,000 units/mL. Rat retinas were superfused with a bicarbonate-buffered, oxygenated medium to which hyaluronidase was added in activities ranging from 100 to 5,000 units/mL. These concentrations of hyaluronidase did not significantly alter the amplitudes of the a waves and b waves of the ERG in comparison to their control amplitudes. Measurements were also made of lactic acid production, oxygen consumption, glutathione content, and adenosine triphosphatase activities in control and hyaluronidase-exposed retinas. In the presence of hyaluronidase, their respective values were similar to the controls for all biochemical factors studied. The present experiments demonstrate that addition of hyaluronidase to an "ocular irrigating" solution results in normal ERGs and normal retinal metabolic activity and suggests the possibility that hyaluronidase may be useful in enzyme-assisted vitrectomy.
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PMID:Hyaluronidase and retinal function. 293 18

Enoximone is a new cardiotonic agent, active by both intravenous and oral routes of administration, that is being studied clinically for the treatment of patients with congestive heart failure. The animal pharmacology pertinent to the clinical development of enoximone is reviewed. Direct positive inotropic, positive chronotropic and vasodilator properties have been demonstrated for enoximone in several in vivo and in vitro preparations. However, positive inotropism and vasodilation are the principal effects of this agent with the inotropic effect being the most prominent. In anesthetized dogs, the cardiovascular effects produced by enoximone (0.1 to 1 mg/kg) were not accompanied by significant alterations in myocardial oxygen consumption. Cardiac function was improved by enoximone in anesthetized dogs given myocardial depressant amounts of propranolol. Studies in vivo and in vitro have indicated that the actions of enoximone are direct and not mediated by stimulation of adrenergic receptors, histaminic receptors, cholinergic receptors, Ca++-adenosine triphosphatase, Mg++-adenosine triphosphatase, adenyl cyclase or inhibition of Na+, K+-adenosine triphosphatase. However, enoximone reversed the depressant effects of verapamil in the dog heart-lung preparation; this suggests that its action resulted in the activation of slow calcium channels. Enoximone was found to be potent and highly selective inhibitor of a high affinity cyclic adenosine monophosphate-phosphodiesterase type IV-phosphodiesterase from dog heart, whereas standard inhibitors (e.g., 3-isobutyl-1-methylxanthine and papaverine) inhibit all 3 cardiac phosphodiesterases. Further, enoximone produced an increase in cyclic adenosine monophosphate, but not cyclic guanosine monophosphate, in the isolated, blood perfused dog papillary muscle during the peak inotropic effect.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Pharmacology of enoximone. 295 61

The energy metabolism of two continuous cell lines of renal origin, MDCK (Madin-Darby dog kidney) and A6 (toad kidney), was investigated by measuring the oxygen consumption (QO2) and lactate production (Jlac) by cells taken into suspension from monolayer cultures. Cells suspended from fully differentiated monolayers produce approximately 80% of their ATP requirements from oxidative metabolism. The interrelationship between ion transport and metabolism was determined by analyzing the ouabain sensitive components of intermediary metabolism under control conditions and after the stimulation of active Na-K transport with nystatin. In both cell lines, approximately 25% of the net rate of ATP production was inhibited by ouabain. Ouabain inhibited Jlac by 40% in MDCK and 45% in A6 cells, whereas QO2 was decreased by only 20% in both cell lines. In the presence of 0.05 mg nystatin/mg cell protein, ouabain sensitive Jlac increased by 75% in MDCK and was more than doubled in A6, whereas the ouabain-sensitive QO2 was not statistically different than control. This preferential stimulation of glycolysis with nystatin was not due to a limited capacity of mitochondrial oxidative phosphorylation since nystatin treatment of cells incubated without glucose (no glycolysis) significantly elevated the rate of QO2. These data demonstrate that aerobic glycolysis is more sensitive than is QO2 to changes in hydrolytic activity of the Na-K-adenosine triphosphatase (ATPase), in both cell lines.
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PMID:Energy metabolism of renal cell lines, A6 and MDCK: regulation by Na-K-ATPase. 303 Jan 21

In vascular smooth muscle, oxidative phosphorylation and glycolysis are independently regulated. Previous studies indicated that the independent regulation of these pathways was related to a compartmentation of carbohydrate metabolism. To further study carbohydrate metabolism, glucose transport and the incorporation of radiolabel from glucose into glycogen and lactate were measured after the oxidative and glycolytic pathways were independently altered. Ouabain stimulated mechanical activity, oxygen consumption, and glycogenolysis, whereas lactate production was decreased. Although glycogenolysis was substantial, glucose was the only substrate for lactate, indicating that intermediates derived from glycogen do not mix with those from glucose uptake. Thus glycogenolysis and glycolysis are carried out by independent enzymatic pathways. Insulin-stimulated lactate production and glucose transport without affecting the other parameters. Again, lactate was produced only from glucose. Phenytoin decreased isometric tension and oxygen consumption, whereas stimulating lactate production and glycogenolysis. Glycogen was the primary substrate for the lactate produced. Our findings indicate that the compartmentation of substrate utilization is ascribable to the coordination of glycogenolysis with increases in oxygen consumption and the coupling of glycolysis to the Na-K-adenosine triphosphatase. The coupling of independent energy providing pathways to specific endergonic processes indicates a mechanism by which cellular energetic efficiency may be optimized.
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PMID:Compartmentation of carbohydrate metabolism in vascular smooth muscle. 303 Jan 31

Total injury in ischemic skeletal muscle is a function of ischemic damage and reperfusion injury. In an attempt to decrease reperfusion injury, we gave the oxygen-derived free radical scavengers allopurinol, superoxide dismutase, or mannitol during reperfusion of canine gracilis muscle made ischemic for 4 hours. We measured muscle O2 consumption (MVO2), and tissue calcium, water, and adenosine triphosphatase (ATP) before ischemia, after ischemia, and at 5 minutes and 60 minutes of reperfusion. The results at 60 minutes showed no improvement in MVO2 or ATP. In fact, ATP was significantly depressed with allopurinol and superoxide dismutase treatment, and tissue edema did not decrease in any of the groups. We conclude that the simple addition of oxygen-derived free radical scavengers during the initial reperfusion of totally ischemic skeletal muscle does not attenuate reperfusion injury.
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PMID:Oxygen-derived free radical scavengers and skeletal muscle ischemic/reperfusion injury. 314 90

1. Kidneys were kept anoxic at 4 degrees , 20 degrees and 38 degrees . Mitochondria were then isolated and their oxidative phosphorylation and respiration were determined. 2. Under all conditions the rate of phosphate esterification was affected to a greater extent, or earlier, than oxygen consumption. 3. Glutamate and succinate were used as substrates. The depression of P/O ratio was greater for glutamate at 4 degrees , and for succinate at 20 degrees . 4. Anoxia abolished the inhibiting effect of fluoride on respiration. 5. Phosphate esterification, after anoxia, was higher in the presence of fluoride than its absence, whereas in control preparations they were the same. 6. The decrease in P/O ratio did not appear to be due to activation of adenosine triphosphatase, as activities of both Mg(2+)-and dinitrophenol-activated adenosine triphosphatases were decreased after anoxia.
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PMID:The effect of temperature and anoxia of kidney on the subsequent oxidative phosphorylation of mitochondria. 422 26

The influence of mitochondrial inhibitors, including oligomycin, antimycin and rotenone, on the iodide and oxygen uptake and the nucleotide content of incubated sheep thyroid slices was investigated. Each inhibitor strongly suppressed both iodide and oxygen uptake, and decreased the nucleoside triphosphate content of the slices. In most cases the addition of glucose or mitochondrial substrates restored iodide uptake in inhibitor-treated slices. Inhibitor concentrations sufficient to inhibit iodide uptake strongly had only slight effects on the thyroidal Na(+)+K(+)-activated adenosine triphosphatase. It is concluded that the inhibitors produce their effects by the inhibition in vivo of mitochondrial oxidative phosphorylation. ATP synthesis appears to be essential for iodide uptake to occur, and the high-energy intermediates (or energized state) of oxidative phosphorylation cannot be used to energize the uptake process. To a limited extent glycolytic ATP synthesis can support iodide uptake, which is therefore not exclusively dependent on aerobic metabolism. The mechanism of energy-linked iodide uptake is discussed.
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PMID:Influence of mitochondrial inhibitors on the respiration and energy-dependent uptake of iodide by thyroid slices. 423 89

A neomycin-resistant mutant of Escherichia coli, NR70, lacking membrane-bound Mg(2+)-adenosine triphosphatase (EC 3.6.1.3) activity has been isolated. Both whole cells and membrane vesicles exhibit a reduced ability to accumulate amino acids and sugars. Other membrane-related functions such as oxygen consumption, the in vivo hydrolysis of o-nitrophenyl-beta-d-galactoside, and the phosphoenolpyruvate-dependent phosphotransferase system did not exhibit reduced activities in NR70. Amino acid transport could be partially restored by the addition of N,N'-dicyclohexylcarbodiimide. The results suggest that a role of the Mg(2+)-adenosine triphosphatase may be to participate in the coupling of energy derived from the electron transport chain to other processes such as transport.
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PMID:Restoration of active transport in an Mg2+-adenosine triphosphatase-deficient mutant of Escherichia coli. 427 Sep 46

1. The intracellular location and maximal activities of enzymes involved in phosphoenolpyruvate synthesis have been investigated in pigeon liver. Enolase and pyruvate kinase were cytoplasmic, and the activities were 50-60 and 180-210mumoles/min./g. dry wt. at 25 degrees respectively. Phosphoenolpyruvate carboxykinase was present exclusively, and nucleoside diphosphokinase predominantly, in the mitochondria; the particles had to be disrupted to elicit maximal activities, which were 27-33 and 400-600mumoles/min./g. dry wt. at 25 degrees respectively. The activities of all four enzymes did not change significantly during 48hr. of starvation. 2. Conditions for incubation of washed isolated mitochondria were established, to give high rates of synthesis of phosphoenolpyruvate, linear with time and proportional to mitochondrial concentration. Inorganic phosphate and added adenine nucleotides were stimulatory, whereas added Mg(2+) inhibited, partly owing to activation of contaminant pyruvate kinase. Phosphoenolpyruvate formation occurred from oxaloacetate, malate, fumarate, succinate, alpha-oxoglutarate and citrate, in decreasing order of effectiveness. 3. The steady-state ATP/ADP ratio of mitochondrial suspensions was decreased in the presence of added 2.5mm-Mg(2+) (owing to stimulation of adenylate kinase and possibly of an adenosine triphosphatase), 0.5mm-Ca(2+) or 0.4mm-dinitrophenol. In each case the rate of substrate removal and oxygen uptake was increased, whereas phosphoenolpyruvate synthesis was inhibited. Citrate formation was enhanced, owing to de-inhibition of citrate synthase. These effects were not primarily related to changes in the oxaloacetate concentration. 4. Both phosphoenolpyruvate carboxykinase and nucleoside diphosphokinase were active within the atractylosidesensitive barrier to the mitochondrial metabolism of added adenine nucleotides. There was no correlation between the rate of substrate-level phosphorylation associated with the oxidation of alpha-oxoglutarate, and the synthesis of phosphoenolpyruvate. 5. The results suggest that phosphoenolpyruvate formation in pigeon-liver mitochondria is regulated partly by the phosphorylation state of the adenine and guanine nucleotides, and partly by variations in the oxaloacetate concentration, all in the mitochondrial matrix. 6. Phosphoenolpyruvate is assumed to be the metabolite transported from the mitochondria to the cytoplasm during gluconeogenesis from oxaloacetate in pigeon liver.
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PMID:The regulation of phosphoenolpyruvate synthesis in pigeon liver. 496 63

1. The respiration and aerobic glycolysis of pig ciliary processes in oxygenated phosphate and bicarbonate buffers have been investigated. 2. Significant amounts of lactic acid are produced only in the presence of added glucose, but this does not change the endogenous respiration rate. 3. Succinate and citrate increase the oxygen uptake considerably, but pyruvate has almost no effect; oxaloacetate and fumarate stimulate slightly in the presence of glucose. Aspartate and fumarate together stimulate pyruvate utilization and are oxidized as fast as citrate. 4. Ouabain inhibits the oxidation of glucose and other substrates by limiting the ADP supply from the sodium transport system. Cyanide and azide inhibit respiration and stimulate glycolysis. 5. The transport mechanism depends largely on ATP from oxidative phosphorylation and regulates the rate of respiration and glycolysis by controlling ADP production from the Na(+)-K(+)-activated adenosine triphosphatase.
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PMID:The tricarboxylic acid cycle and glycolysis in relation to ion transport by the ciliary body. 591 34


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