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 in vitro effects of piperine on three bioenergetic reactions namely, oxidative phosphorylation, ATPase activity and calcium transport by isolated rat liver mitochondria have been investigated. Piperine was found to inhibit state 3 and DNP-stimulated respiration by mitochondria respiring with glutamate plus malate or succinate as substrates. The I50 values of piperine on oxidative phosphorylation in the presence of glutamate plus malate and succinate were 22 and 12 micrograms/mg mitochondrial protein respectively. With HTM preparations, the oxidation of added NADH and succinate was depressed by piperine while ascorbate plus TMPD oxidation was slightly affected. Piperine did not inhibit the mitochondrial ATPase activity induced by DNP, but by itself exerted stimulating activity on this enzyme. Piperine was also found to diminish calcium uptake and to facilitate the release of accumulated calcium by the mitochondria incubated with succinate or ATP. These results suggest that piperine inhibits mitochondrial oxidative phosphorylation at the level of respiratory chain, and the inhibitory site(s) is in the segment(s) ahead of cytochrome C. The mechanism of the piperine-induced ATPase activity is not known; but the effect of piperine on calcium transport is likely to be consequential to the effects of this compound on the mitochondrial respiratory chain and ATPase activity.
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PMID:Effects of piperine on bioenergetic functions of isolated rat liver mitochondria. 296 41

The influence of vitamin D and C deficiency on the kinetic parameters of sucrase and alkali phosphatase activities was studied in the microsomal fraction of the small intestinal mucosa of guinea pigs. It was found that Km values for these enzymes did not depend on the animal providing with these vitamins. Deficiency of one of these vitamins did not influence sucrase activity, however, simultaneous elimination of vitamins D and C resulted in the activity rise by 92%. Alkali phosphatase and Ca-ATPase activities proved to be similarly dependent on providing with vitamin D in the presence of vitamin C in the ration, while in the absence of vitamin C this dependence was not observed.
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PMID:[Enzymatic activity of the microsomal fraction of the mucosa of the small intestine in guinea pigs with vitamin D and C deficiencies]. 296 18

Inactivation of Trypanosoma cruzi mitochondrial ATPase by oxygen radicals, generated by redox cycling of the ascorbate-Cu system (Cataldi de Flombaum, M.A. and Stoppani, A.O.M. (1986) Biochem. Int. 12, 785-793), involves oxidation of the enzyme thiols, as indicated by the competitive kinetics obtained with p-chloromercuribenzoate, a selective SH-reagent. Dithiothreitol prevented the ascorbate-Cu effect but did not reactivate the enzyme. Non-competitive kinetics were obtained with ascorbate-Cu and increasing MgATP concentration, or with phenylglyoxal, as second inhibitor. Since phenylglyoxal reacts with arginyl residues at the ATPase hydrolytic site, these results suggest that the oxgen-sensitive thiols were located outside the hydrolytic site.
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PMID:Inactivation of the mitochondrial adenosine triphosphatase from Trypanosoma cruzi by oxygen radicals: role of thiol groups. 296 97

The distribution of a lipophilic spin probe, 5-doxyl stearate, between the inner and outer halves of the sarcoplasmic reticulum (SR) bilayer was determined by titration with Ni X EDTA, a spin broadening agent. Titrations were also performed with Fe(CN)3-6 and with the solvated Ni2+ cation. Ni X EDTA titrations reached a clearly defined asymptote at 35% signal reduction. Fe(CN)3-6 and Ni2+ titrations gave biphasic curves but showed 35% of the signal to be readily eliminated at low concentrations. When the Ni2+ cation was used with ionophore, titrations indicated that 96% of the probe is aligned in the bilayer with the spin moiety at either the inner or outer interface. It was concluded that the spin probe distribution between the outer and inner halves of the SR bilayer is 35:65, respectively. Titrations performed on vesicles of purified SR lipids gave a ratio of 60 exposed:40 protected, consistent with the vesicular geometry. In addition the spin probe distribution in SR vesicles did not vary as a function of temperature, salt concentration, or spin probe concentration. On this basis it was concluded that the spin probe distribution gives a reasonable estimation of the volume of fluid lipids available to readily solubilize the probe in each half of the bilayer and that the observed asymmetry in distribution is due to the presence of SR proteins which were eliminated in the pure lipid vesicles. Furthermore, as EDTA is unique in its ability to chelate transition metals, Ca2+ and EGTA can be used in Ni X EDTA titrations without altering the chelation of Ni2+. Known changes in ATPase conformation accompanying Ca2+ and adenyl-5'-yl imidodiphosphate X Mg binding did not affect the spin probe distribution. However, phosphorylation of the enzyme by Pi gave a small, but clearly discernible, protection of spin probe signal. Chemical reduction with ascorbate indicated that this was due to occlusion of a small fraction of spin probes and thus possibly SR lipids.
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PMID:Distribution of a fatty acid spin probe in sarcoplasmic reticulum. Evidence of membrane asymmetry. 298 78

Experimental data are presented concerning inhibition of Na, K-ATPase in rat heart sarcolemmal and rat brain synaptosomal membranes upon generation of activated oxygen species. It is shown that the activity of Na, K-ATPase is inhibited in membranes of both types during incubation with Fe2+ + ascorbate system, which generates O2 and OH- radicals and thus induces lipid peroxidation. The inhibitory effect is linearly dependent on the amount of the lipid peroxidation products (malondialdehyde) accumulated. Exogenous unsaturated phosphatidylethanolamine, when added to partially inactivated enzyme, does not produce reactivation of Na, K-ATPase. Free radical scavenger 4-methyl-2,6-di-(tertbutyl) phenol exerts both inhibition of lipid peroxidation and protection of Na, K-ATPase. Mg-ATPase is resistant to the action of lipid peroxidation inducing system. Bubbling of oxygen through membrane suspension results in no malondialdehyde accumulation, but is accompanied by Na, K-ATPase inhibition, which could not be prevented by free radical scavengers. It is suggested that generation of activated oxygen species results in oxidation of one of the essential amino acid residues in the active site of the enzyme.
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PMID:Mode of lipid peroxidation-induced inhibition of Na, K-ATPase. 299 67

The reactions of cytochrome b561 with other redox-active components of the adrenal chromaffin granule were examined using optical difference spectroscopy. It was shown that there is no direct electron transfer between the cytochrome and dopamine beta-hydroxylase, but that in the presence of ascorbate, turnover of dopamine beta-hydroxylase causes an oxidation of the cytochrome, which is partially reversed by the action of the mitochondrial NADH:A-. oxidoreductase. Thus, these three proteins may be functionally coupled via ascorbate. A quantitative study of the relationship between the redox state of the cytochrome and the ascorbate radical concentration measured by EPR showed that ascorbate reduces the cytochrome in a one-electron transfer reaction. Generation of a proton electrochemical gradient across the granule membrane causes only a small (20 mV) increase in the cytochrome midpoint potential suggesting the cytochrome is not a proton pump. The data are consistent with a model in which cytochrome b561, by reacting with ascorbate or ascorbate free radical on either side of the granule membrane, could couple the ascorbate-consuming reaction of the dopamine beta-hydroxylase inside the chromaffin granule to the ascorbate-regenerating reaction of the NADH:A-. oxidoreductase on the outer mitochondrial membrane. The H+-ATPase of the granule membrane could both drive the flow of electrons in the direction from cytosol to granule and replenish protons consumed by the turnover of dopamine beta-hydroxylase inside the granule.
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PMID:Functional coupling between enzymes of the chromaffin granule membrane. 301 4

Incubation of Trypanosoma cruzi mitochondrial ATPase (Fo-F1) with the xanthine oxidase system (XO), Fenton's reagent (Fe2+ + H2O2) and the ascorbate-Cu system, caused gradual loss of enzyme activity, which increased as a function of incubation time and rate of oxygen radical generation. The essential role of OH. radicals for ATPase inactivation was supported by a) the enzyme protection afforded by superoxide dismutase, catalase and mannitol, when using the XO system; b) the similar effect of mannitol and benzoate with Fenton's reagent; c) the similar effect of catalase, EDTA and histidine with the ascorbate-Cu system; d) the increased rate of ATPase inactivation by 1) the XO system supplemented with chelated iron, and 2) the ascorbate-Cu system supplemented with H2O2. Comparison of oxygen radical generators for their action on membrane-bound (Fo-F1) and soluble F1 revealed that ascorbate-Cu was the most effective one, possibly because of its capability of producing OH. radicals that react preferentially with the enzyme at their formation site.
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PMID:Inactivation of mitochondrial adenosine triphosphatase from Trypanosoma cruzi by oxygen radicals. 301 49

On analyzing the mechanisms of the internal environment type redox regulation of physiological processes it was observed on frog rectus muscles that during acetylcholine contractures methylene blue pretreatment inhibited, but ascorbate pretreatment enhanced the slow transient changes of extracellular Na+-activity. At the same time, these modifications were inverse for K+-transients. Because k-strophantoside was capable of influencing these effects radically it seems highly plausible to assume that the principal site of action of these modulations is the inhibitory impact of methylene blue, while the enhancing effect of ascorbate on (Na+ + K+)-ATPase may likely be explained on redox basis.
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PMID:Inverse modulation of extracellular Na+- and K+-activities by ascorbate or methylene blue. 302 56

Proline porter II is rapidly activated when nongrowing bacteria are subjected to a hyperosmotic shift (Grothe, S., Krogsrud, R. L., McClellan, D. J., Milner, J. L., and Wood, J. M. (1986) J. Bacteriol. 166, 253-259). Proline porter II was active in membrane vesicles prepared from bacteria grown under optimal conditions, nutritional stress, or osmotic stress. That activity was: (i) dependent on the presence of the energy sources phenazine methosulphate plus ascorbate or D-lactate; (ii) observed only when a hyperosmotic shift accompanied the transport measurement; (iii) inhibited by glycine betaine in a manner analogous to that observed in whole cells; and (iv) eliminated by lesions in proP. Membrane vesicles were able to transport serine but not glutamine and serine transport was reduced by the hyperosmotic shift. In whole cells, proline porter II activity was supported by glucose and by D-lactate in a strain defective for proline porters I and III and the F1F0-ATPase. Glucose energized proline uptake was eliminated by carbonyl cyanide m-chlorophenylhydrazone and KCN as was serine uptake. These results suggested that proline porter II was respiration-dependent and probably ion-linked. Activation of proline porter II in whole cells by sucrose or NaCl was sustained over 30 min, whereas activation by glycerol was transient. Proline porter II was activated by NaCl and sucrose with a half-time of approximately 1 min in both whole cells and membrane vesicles. Thus, activation of proline porter II was reversible. It occurred at a rate comparable to that of K+ influx and much more rapid than the genetic regulatory responses that follow a hyperosmotic shift.
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PMID:Proline porter II is activated by a hyperosmotic shift in both whole cells and membrane vesicles of Escherichia coli K12. 304 95

Blood transfusion is the second most important mechanism of transmission of Chagas' disease. Gentian violet, a cationic dye, is currently used in blood banks in endemic areas in attempts to eliminate such transmission. A photodynamic action of gentian violet has been demonstrated in Trypanosoma cruzi. Visible light causes photoreduction of gentian violet to a carbon-centered radical. Under aerobic conditions this free radical autooxidizes generating superoxide anion whose dismutation yields hydrogen peroxide. This photodynamic action of gentian violet is thus probably mediated by the oxygen reduction products. Since irradiation with visible light in the presence of sodium ascorbate reduces the effective dose and time of contact of the dye with T. cruzi-infected blood, a possible application of these findings can be envisaged. In addition to this photodynamic action, an uncoupling effect of gentian violet on mitochondrial oxidative phosphorylation has been described in rat liver and T. cruzi mitochondria. Gentian violet released respiratory control, hindered ATP synthesis, enhanced ATPase activity, released the inhibition of State 3 respiration by oligomycin, and produced swelling of isolated rat liver mitochondria or T. cruzi mitochondria in situ. Taken together, these results indicate that the T. cruzi mitochondrion is the main target of gentian violet toxicity in the dark.
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PMID:Prevention of Chagas' disease resulting from blood transfusion by treatment of blood: toxicity and mode of action of gentian violet. 315 57


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