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)

1. The hypoglycaemic compound diphenyleneiodonium causes rapid and extensive swelling of rat liver mitochondria suspended in 150mm-NH(4)Cl, and in 150mm-KCl in the presence of 2,4-dinitrophenol and valinomycin. This indicates that diphenyleneiodonium catalyses a compulsory exchange of OH(-) for Cl(-) across the mitochondrial inner membrane. Br(-) and SCN(-) were the only other anions found whose exchange for OH(-) is catalysed by diphenyleneiodonium. 2. Diphenyleneiodonium inhibited state 3 respiration of mitochondria and slightly stimulated state 4 respiration with succinate or glutamate as substrate in a standard Cl(-)-containing medium. 3. Diphenyleneiodonium did not inhibit state 3 respiration significantly in two Cl(-)-free media (based on glycerol 2-phosphate or sucrose) but caused some stimulation of state 4. 4. In Cl(-)-containing medium diphenyleneiodonium only slightly inhibited the 2,4-dinitrophenol-stimulated adenosine triphosphatase and it had little effect in the absence of Cl(-). 5. The inhibition of respiration in the presence of Cl(-) is dependent on the Cl(-)-OH(-) exchange. 2,4-Dichlorodiphenyleneiodonium is ten times as active as diphenyleneiodonium both in causing swelling of mitochondria suspended in 150mm-NH(4)Cl and in inhibiting state 3 respiration in Cl(-)-containing medium. Indirect evidence suggests that the Cl(-)-OH(-) exchange impairs the rate of uptake of substrate anions. 6. It is proposed that stimulation of state 4 respiration in the absence of Cl(-) depends, at least in part, on an electrogenic uptake of diphenyleneiodonium cations. 7. Tripropyl-lead acetate, methylmercuric iodide and nine substituted diphenyleneiodonium derivatives also catalyse Cl(-)-OH(-) exchange across the mitochondrial membrane. 8. Diphenyleneiodonium is compared with the trialkyltin compounds, which are also known to mediate Cl(-)-OH(-) exchange and which have in addition strong oligomycin-like effects on respiration. It is concluded that diphenyleneiodonium is specific for catalysing anion-OH(-) exchange and will be a useful reagent for investigating membrane-dependent systems.
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PMID:Biochemical effects of the hypoglycaemic compound diphenyleneiodonnium. Catalysis of anion-hydroxyl ion exchange across the inner membrane of rat liver mitochondria and effects on oxygen uptake. 426 24

1. The effect of the diuretic drug furosemide was studied in detail on ouabain-insensitive, SCN- and OCN- -sensitive C1-/HCO-3-ATPase in homogenates from larval dragonfly rectum (Aeshna cyanea), frog (Rana temporaria) and mouse (Mus musculus) kidney. 2. The in vitro inhibition by the drug studied on the HCO-3-activated enzyme is non-competitive with an inhibitor constant of Ki=4.3 mM furosemide in the case of insect rectum and Ki=0.9 mM furosemide in the case of frog and mouse kidney. 3. Furosemide even at 10 mM concentration which completely inhibits the anion-dependent ATPase has only a little inhibitory effect on the Na+/K+-ATPase of the 3 tissues. 4. The data suggest that furosemide may affect an active chloride transport system involving a C1-/HCO-3-ATPase.
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PMID:The loop diuretic furosemide as non-competitive inhibitor of C1-/HCO3-ATPases of vertebrate kidneys and insect rectum. 612 70

1. HCO3(-)-stimulated ATPase activity was demonstrated in mantle tissue of the freshwater clam, Anodonta cataracta. 2. Calcium (1 mM) slightly inhibited and SCN- completely inhibited HCO3(-)-stimulation of the enzyme. 3. ATPase activity had a Km of 6.8 mM for HCO3(-)-activation and was inhibited at HCO3(-)-concentrations greater than 20 mM. 4. Subcellular fractionation studies revealed the presence of both a mitochondrial and a non-mitochondrial HCO3(-)-ATPase.
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PMID:Subcellular localization and characterization of HCO3(-)-ATPase from the mantle of the freshwater clam, Anodonta cataracta. 612 5

Insulin-secretory granules isolated from a pancreatic islet-cell tumour by centrifugation on Percoll density gradients exhibited a membrane-associated Mg(2+)-dependent ATPase activity. In granule suspensions incubated in iso-osmotic media, activity was increased 2-3-fold by carbonyl cyanide p-trifluoromethoxyphenylhydrazone, the combination of valinomycin, nigericin and K(2)SO(4) or by the addition of a detergent. Permeant anions also increased Mg(2+)-dependent ATPase activity under iso-osmotic conditions when combined with K(+) and nigericin, or NH(4) (+). It was deduced that a major component of the activity was coupled to the translocation of protons into the granule interior. The granule membrane appeared poorly permeable to H(+), K(+), NH(4) (+) and SO(4) (2-) but permeable, in increasing order, to phosphate or acetate, Cl(-), I(-) and SCN(-). Like the proton-translocating ATPase of mammalian mitochondria the granule enzyme when membrane-bound was inhibited by up to 85% by tributyltin or NN'-dicyclohexylcarbodi-imide and was solubilized in a tributyltin-insensitive form after extraction with dichloromethane. It was clearly not a mitochondrial contaminant as evidence by the distribution of marker proteins on density gradients. Unlike mitochondrial activity it was insensitive to oligomycin, efrapeptin, atractyloside, azide and oxyanions. Its properties, however, were indistinguishable from those of the proton-translocating ATPase found in the chromaffin granules of the adrenal medulla. Moreover, insulin granules and chromaffin granules exhibited similar levels of activity. This indicated that in spite of the differences in their internal composition, granules from tissues involved in polypeptide and amine hormone secretion possess catalytic components in common. Only a minor role for the ATPase in amine transport in insulin granules was apparent. Rather, its presence here may relate to the process of secretory vesicle morphogenesis or to the exocytotic mechanism.
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PMID:Proton-translocating Mg2+-dependent ATPase activity in insulin-secretory granules. 612 82

Phosphohydrolase activity of a highly enriched commercial preparation of calf intestinal alkaline phosphatase was stimulated in the presence of HCO3. SO4, Cl, SCN, and acetate did not stimulate hydrolysis, whereas SO3 exhibited a bimodal effect, stimulating at low (25mM) concentration but inhibiting at high (100 mM) concentration. The pH optimum of this stimulation by HCO3 or SO3 was 8.5--9.0 and was maximal at a Mg concentration of 0.5 mM. HCO3 increased the Vmax of the reaction without changing the Km for ATP. ATP, GTP, UTP, and xanthosine triphosphate were equally effective as substrates, whereas AMP and p-nitrophenyl phosphate were much less effective. Alkaline phosphatase activity was inhibited by L-cysteine and L-phenylalanine, compounds that also inhibited the HCO3-ATPase activity of the preparation. Passage of the commercial preparation through an anion-exchange column yielded a fraction with enriched alkaline phosphatase and HCO3-ATPase activities; this fraction proved to be a single protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, on isoelectric focusing, and by immunologic techniques. These studies strongly suggest that alkaline phosphatase and anion-stimulated phosphohydrolase activities are properties of the same protein in small intestine. It is possible that alkaline phosphatase may function as a HCO3-ATPase involved in intestinal absorption and secretion.
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PMID:Anion-stimulated phosphohydrolase activity of intestinal alkaline phosphatase. 615 12

Mucosal homogenates from rat jejunum were tested for both HCO-3-stimulated ATPase and anion-stimulated, SCN-inhibited ATPase in assay mixtures ungassed, gassed with pure oxygen or gassed with the appropriate gaseous phase. Experiments were performed at four different initial pHs (7.15; 7.45; 8.10; 8.55) with or without the presence of Triton X-100. Assay mixtures were tested for both pH and % CO2. Only at pH 7.15 and 7.45 anion-sensitive ATPase activities in ungassed conditions are different from those in mixtures gassed with the proper gaseous phase. Moreover, at cited pHs in ungassed mixtures the final pH is higher and % CO2 is lower than initial values. Therefore it seems possible to obtain the exact determination of anion-sensitive ATPases at all pH values only from mixtures gassed with the proper gaseous phase. Bicarbonate-stimulated ATPase activity is absent both at pH 7.15 and 7.45; this fact seems to exclude, at these pHs, an active transport of bicarbonate directly depending on this enzyme activity.
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PMID:ph-dependent, HCO-3-stimulated ATPase of rat jejunum. 618 53

ATP-dependent Ca2+ uptake into isolated pancreatic acinar cells with permeabilized plasma membranes, as well as into isolated endoplasmic reticulum prepared from these cells, was measured using a Ca2+ -specific electrode and 45Ca2+. Endoplasmic reticulum was purified on an isopycnic Percoll gradient and characterized by marker enzyme distribution. When compared to the total homogenate, the typical marker for the rough endoplasmic reticulum RNA was enriched threefold and the typical marker for the plasma membrane Na+,K+(Mg2+)ATPase was decreased 20-fold. When different fractions of the Percoll gradient were compared, 45Ca2+ uptake correlated with the RNA content and not with the Na+,K+(Mg2+)ATPase activity. The characteristics of nonmitochondrial Ca2+ uptake into leaky isolated cells and 45Ca2+ uptake into isolated endoplasmic reticulum were very similar: Calcium uptake was maximal at 0.3 and 0.2 mmol/liter free Mg2+, at 1 and 1 mmol/liter ATP, at pH 6.0 and 6.5, and free Ca2+ concentration of 2 and 2 mumol/liter, respectively. Calcium uptake decreased at higher free Ca2+ concentration. 45Ca2+ uptake was dependent on monovalent cations (Rb+ greater than K+ greater than Na+ greater than Li+ greater than choline+) and different anions (Cl- greater than Br- greater than SO4(2-) greater than NO3- greater than I- greater than cyclamate- greater than SCN-) in both preparations. Twenty mmol/liter oxalate enhanced 45Ca2+ uptake in permeabilized cells 10-fold and in vesicles of endoplasmic reticulum, fivefold. Calcium oxalate precipitates in the endoplasmic reticulum of both preparations could be demonstrated by electron microscopy. The nonmitochondrial Ca2+ pool in permeabilized cells characterized in this study has been previously shown to regulate the cytosolic free Ca2+ concentration to 0.4 mumol/liter. Our results provide firm evidence that the endoplasmic reticulum plays an important role in the regulation of the cytosolic free Ca2+ concentration in pancreatic acinar cells.
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PMID:Characterization of calcium uptake into rough endoplasmic reticulum of rat pancreas. 620 63

Active uptake of phalloidin and cholate in isolated rat liver cells depends upon both Na+ gradient and membrane potential. Omission of Na+ or inhibition of the (Na+ + K+)-ATPase diminished both phalloidin and cholate uptake. Dissipation of the sodium, potassium or proton gradient by monensin, nigericin, gramicidin and valinomycin blocked phalloidin uptake and also caused reduction of cholate transport. Chelation of Ca2+ and Mg2+ by EGTA or incubation of liver cells with NH4Cl neither influenced phalloidin nor cholate uptake. Hyperpolarization of liver cells by the lipophilic anions NO3- or SCN- enhanced phalloidin but reduced cholate uptake. Depolarization induced by a reversed K+ gradient reduced both kinds of transport. The results indicate that sodium ions and the membrane potential are driving forces for phalloidin and cholate uptake in hepatocytes.
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PMID:Driving forces in hepatocellular uptake of phalloidin and cholate. 621 Jan 9

The outward-facing (OFM) and inward-facing (IFM) membranes of the surface epithelial syncytium of Schistosoma mansoni were separated by sequential exposure to saponin solutions. The OFM, containing both inner and outer bilayers, contained ATPase activity that was stimulated by Mg2+ and Ma+, but not K+ or HCO-3, and was inhibited by Ca2+ and ethacrynic acid. The OFM enzyme was unaffected by ouabain, oligomycin, SCN- and azide and had a pH optimum of 7.5. The OFM ATPase therefore has properties similar to ATPases characterized from the apical membrane of a variety of epithelial cells where it is thought to augment the regulatory cell volume decreasing function of (Na++K+)Mg2+- ATPase. The IFM contained ATPase activity that was stimulated by Mg2+, Na+ and K+, and was inhibited by ouabain indicating the IFM enzyme was the Na+-pump ATPase. The results are discussed in terms of the transepithelial transport function of the surface epithelial syncytium and a Ca2+-ATPase reported previously from the OFM of S. mansoni.
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PMID:Enrichment and partial enzyme characterization of ATPase activity associated with the outward-facing membrane complex and inward-facing membrane of the surface epithelial syncytium of Schistosoma mansoni. 621 5

An anion-stimulated, ouabain-insensitive Mg2+ATPase activity has been found in fresh homogenates prepared from capsules and epithelia of bovine lenses. Approximately equal activity was observed in the presence of HCO3- or of Cl-. The stimulation of each anion obeys saturation kinetics, with an optimum at approximately 20 mM Cl- or HCO3-. Whereas SCN- inhibits anion-activated ATPase in most other tissues, it failed to inhibit Cl- - or HCO3--stimulated ATPase activity in the bovine lens. On the contrary, SCN- proved a potent activator of the enzyme. However, in keeping with other tissues, OCN- and the diuretic drugs, furosemide and ethacrynic acid are inhibitory. ATP is the primary substrate for the enzyme, which also shows some activity on GTP, ITP, and even ADP. Little Na+/K+-dependent ATPase activity was observed in the fresh homogenate, but it increased in lyophilized preparations. In contrast, the lyophilized preparations showed no anion-dependent ATPase activity. It is postulated that active bicarbonate ion transport in the lens may be mediated by this anion-dependent ATPase.
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PMID:Chloride- and bicarbonate-stimulated ATPase activity in bovine lens epithelium. 622 19


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