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PubMed1965

THE ADENOSINE-TRIPHOSPHATASE SYSTEM RESPONSIBLE FOR CATION TRANSPORT IN ELECTRIC ORGAN: EXCLUSION OF PHOSPHOLIPIDS AS INTERMEDIATES.

1. Subcellular fractions were prepared from the electric organs of Electrophorus and Torpedo and assayed for adenosine-triphosphatase activity. 2. Treatment of the ;low-speed' fraction from Torpedo with m-urea gave an adenosine-triphosphatase preparation that was almost completely (98%) inhibited by ouabain (0.1mg./ml.) and dependent on the simultaneous presence of Na(+) and K(+). 3. The adenosine-triphosphatase preparations were exposed to [gamma-(32)P]ATP for 30sec. in the presence of (i) Na(+), (ii) K(+), (iii) Na(+)+K(+) and (iv) Na(+)+K(+)+ouabain. No significant labelling of phosphatidic acid, triphosphoinositide or any other phospholipid was observed. 4. The results suggest that phospholipids do not act as phosphorylated intermediates in the ;transport adenosine-triphosphatase' system of electric organ.

Adenosine↗

PubMed1968

Adenosine triphosphate and adenosine triphosphatase in hormone-containing granules of posterior pituitary gland.

Neurosecretory granules prepared from bovine posterior pituitary glands by cell fractionation methods contain adenosine triphosphate and adenosine triphosphatase activity. Addition of adenosine triphosphate to suspensions of granules stimulates release of vasopressin. It is suggested that adenosine triphosphate and adenosine triphosphatase participate in the storage and release of vasopressin.

Adenosine Triphosphatases↗

PubMed1966

The adenosine diphosphate--adenosine triposphate-excange reaction of cerebral microsomes and its relation to he sodium ion-stimulatd adenosine-triphosphatase reaction.

Microsomes from guinea-pig cerebral cortex contain a system capable of exchanging ADP with ATP at rates of about 20mumoles/mg. of protein/hr. The ADP-ATP-exchange reaction requires Mg(2+) for activity. The reaction is not stimulated by Na(+) or K(+) and is not inhibited by ouabain, in contrast with the Na(+)-plus-K(+)-stimulated adenosine triphosphatase. The pH optimum also differs from that of the adenosine triphosphatase. The ADP-ATP-exchange reaction is stimulated two- to three-fold by non-ionic, anionic and cationic detergents, even when these agents are inhibiting the adenosine-triphosphatase reaction. This reaction may represent a component of the Na(+)-plus-K(+)-stimulated adenosine-triphosphatase reaction but is more likely to be due to other enzyme systems present in microsomal subfractions.

Adenine Nucleotides↗

PubMed1977

Ultrastructural localizations of adenosine triphosphatase activity in resting mammary gland.

Adenosine triphosphatase (ATPase) activity was localized at an ultrastructural level in the resting mammary glands of female BALB/c mice. A Mg++ dependent ATPase was localized in the plasma membranes of both the epithelial and myoepithelial cells of the mammary tubules. A second type of ATPase activity that was not Mg++-dependent but that was Na+ and K+ dependent was localized primarily in the plasma membranes of the myoepithelial cells. Preincubation with either ouabain or N-ethylmaleimide decreased the quantity of reaction product, indicating that both types of ATPase activity were sensitive to these inhibitors. Control media, containing adenosine triphosphate and Pb(NO3)2 without cations, demonstrated that the amount of nonezymatic hydrolysis was negligible. These differences in the cationic requirements for plasma membrane ATPase activity can be used to distinguish histochemically the epithelial from myoepithelial cells in mammary tissue.

Adenosine Triphosphatases↗

PubMed1968

Flagellar adenosine triphosphatase from sea urchin sperm: properties and relation to motility.

Adenosine triphosphatase activated by divalent cations is apparently a component of the motile apparatus in flagella of Arbacia sperm, as judged by the activity of this enzyme in intact flagella, glycerol-extracted flagella, and soluble extracts prepared from flagella. However, the variation in the physical properties and in the amount of enzyme obtained after a variety of treatments suggests that additional components are involved in the motile mechanism. These features distinguish the soluble flagellar enzyme from adenosine triphosphatases of other motile cells.

Adenosine Triphosphatases↗

PubMed1977

Effect of ouabain upon erythrocyte membrane adenosine triphosphatase in Duchenne muscular dystrophy.

The adenosine triphosphatase activity of erythrocyte ghosts from patients with Duchenne muscular dystrophy was inhibited by 10(-4) M ouabain to a smaller extent than in normals, when measured in the presence of either high or low concentrations of sodium or potassium ions. The inhibition by ouabain of the enzyme in normal ghosts, measured with low sodium or potassium ions, was less if the erythrocytes were first incubated with plasma from Duchenne patients than if incubated with normal plasma. Similar results were obtained when the ghosts themselves were incubated with Duchenne or normal plasma before assay.

Adenosine Triphosphatases↗

PubMed1981

Effects of inhibitors on mitochondrial adenosine triphosphatase of Tetrahymena pyriformis ST.

Mitochondrial adenosine triphosphatase (ATPase) of the ciliate protozoon Tetrahymena pyriformis ST is completely inhibited by antiserum prepared against F1-ATPase purified from Schizosaccharomyces pombe, and by naturally occurring inhibitor proteins from this yeast and from bovine heart mitochondria. An ATPase inhibitor protein is also present in extracts of T. pyriformis. Mitochondrial ATPase of T. pyriformis is only partially inhibited by the F0-ATPase inhibitors N,N'-dicyclohexylcarbodiimide, oligomycin, leucinostatin, triethyltin sulphate and venturicidin, and (at high titres) by the F1-ATPase inhibitors Dio-9, efrapeptin, 4-chloro-7-nitrobenzofurazan and spegazzinine. Aurovertin, citreoviridin and quercetin were not inhibitory. Resistance to inhibitors distinguishes this mitochondrial ATPase from all those previously examined.

Adenosine Triphosphatases↗

PubMed1974

Increased adenosine triphosphatase in leukocytes of asthmatic children.

Adenosine triphosphatase (ATPase) activities were compared in leukocytes of asthmatic and nonasthmatic children. Both Mg(2+)- and Ca(2+)-dependent ATPase activities were significantly elevated in two membrane fractions (59 to 66%) and in a superntant fraction (68 to 72%) prepared from sonicated leukocytes of asthmatic subjects. Intact cell surface or ecto ATPase was also elevated (67 to 76%) in asthmatic leukocytes. Alternate day glucocorticosteroid therapy was associated with leukocyte ATPase activities intermediate between those for asthmatics not receiving steroids and for nonasthmatic control subjects. Incubation of normal leukocytes with 10(-8) M hydrocortisone or leukocyte membranes with 10(-4)-10(-3) M hydrocortisone in vitro also resulted in decreased ATPase activities. The elevated leukocyte ATPase activities appear to relate to the adrenergic imbalance in asthma previously characterized by reduced beta adrenergic responsiveness of adenylate cyclase and suggest the possibility of more than one enzymatic abnormality intrinsic to the asthmatic condition.

Adenosine Triphosphatases↗

PubMed1970

Localization of adenosine triphosphatase activity on the chloroplast envelope in tendrils of Pisum sativum.

When samples of pea tendril tissue were incubated in the Wachstein-Meisel medium for the demonstration of adenosine triphosphatases, deposits of lead reaction product were localized between the membranes of the chloroplast envelope. The presence of Mg(2+) was necessary for adenosine triphosphatase activity, and Ca(2+) could not substitute for this requirement. Varying the pH of incubation to 5.5 or 9.4 inhibited enzyme activity, as did the addition of p-chloromercuribenzoic acid or N-ethylmaleimide. The adenosine triphosphatase was apparently inactivated or degraded when the plants were grown in the dark for 24 hours prior to incubation. The enzyme was substrate-specific for adenosine triphosphate; no reaction was obtained with adenosine diphosphate, uridine triphosphate, inosine triphosphate, p-nitrophenyl phosphate, and sodium beta-glycerophosphate. Sites of nonspecific depositions of lead are described. The adenosine triphosphatase on the chloroplast envelope may be involved in the light-induced contraction of this organelle.

Adenosine Triphosphatases↗

PubMed1984

Inhibition of renal Na+, K+-adenosine triphosphatase by gentamicin.

Inhibition of renal Na+,K+-adenosine triphosphatase is an early biochemical manifestation of gentamicin treatment in rats. Studies with isolated, perfused rat kidneys in filtering and nonfiltering modes indicate that gentamicin is transported across the brush border membrane before enzyme inhibition. The drug caused enzyme inhibition (42%) only in filtering kidneys, and this inhibition was blocked by spermine, an inhibitor of gentamicin binding. In purified rat renal basolateral membranes, bound [3H]gentamicin was displaced 88% by unlabeled gentamicin. After in vivo exposure to [3H]gentamicin, the radioactivity associated with the isolated basolateral membranes was displaced only 46% by unlabeled drug. These results suggest that inhibition of renal Na+,K+-adenosine triphosphatase by gentamicin is probably due to an interaction at the cytoplasmic face of the basolateral membrane. Scatchard plots of [3H]gentamicin binding to basolateral and brush border membranes revealed a single class of noninteracting sites in each membrane. Gentamicin did not change the bulk membrane lipid fluidity, as estimated by the fluorescence polarization of 1,6-diphenyl-1,3,5-hexatriene.

Animals↗

PubMed1967

A protein factor inhibiting the magnesium-activated adenosine triphosphatase of desensitized actomyosin.

1. The preparation and properties of a myofibrillar protein factor which inhibits the Mg(2+)-activated adenosine triphosphatase of desensitized actomyosin is described. 2. This factor had negligible effect on the Mg(2+)-activated adenosine triphosphatase of natural actomyosin and on the Ca(2+)-activated adenosine triphosphatases of desensitized actomyosin and myosin. 3. The Mg(2+)-activated inosine triphosphatase activity of desensitized actomyosin was not affected by the factor. 4. The inhibitory effect was sensitive to ionic strength. In addition to their ionic effects Mg(2+) and Ca(2+) appeared to have a specific action in reducing the effect of the inhibitor. 5. F-actin reduced the inhibition whereas Bailey-type tropo-myosin had little effect. 6. As far as can be judged from the reported experiments this factor is different from any of the previously described myofibrillar components.

Adenosine Triphosphatases↗

PubMed1976

Leukocyte adenosine triphosphatase activity in human bronchial asthma.

Changes in adenosine triphosphatase (ATPase) activity of the peripheral blood leukocytes were investigated in patients with bronchial asthma. Estimation of the leukocyte Mg++- and Ca++- dependent ATPases was carried out according to Hadden's method, incubating ATP with the membrane fraction of the leukocyte. The leukocyte ATPase activity was significantly elevated among asthmatic patients compared with control subjects. This elevated ATPase was seen in all asthmatics irrespective of acute attacks or the drug treatment. There was no clear correlation between the activity of ATPase and the percentage of leukocytes, neutrophils and eosinophils. There was no relationship between ATPase activity and adenyl cyclase activity of the same leukocytes from asthmatic patients.

Adenosine Triphosphatases↗

PubMed1966

The adenosine-triphosphatase activity of dissociated acto-heavy-meromyosin.

1. At low ionic strength, when turbidity and viscosity measurements indicated dissociation of acto-heavy-meromyosin, its adenosine triphosphatase was strongly activated by Mg(2+) and Ca(2+). 2. The characteristics of the adenosine triphosphatase of dissociated acto-heavy-meromyosin in the presence of Mg(2+) were similar to those reported for myofibrils and actomyosin. 3. In the presence of Ca(2+) the adenosine-triphosphatase activity was much less sensitive to ionic strength than was the case with Mg(2+). 4. At low ionic strength Mg(2+) was more effective in maintaining the dissociation of acto-heavy-meromyosin in the presence of ATP than was Ca(2+). This difference was not apparent when ATP was replaced by ITP. 5. Although the recovery of viscosity was complete on reassociation of acto-heavy-meromyosin the turbidity did not return to the original value. 6. The general implications of Mg(2+) activation of acto-heavy-meromyosin when classical interpretation indicates dissociation of the complex are discussed.

Adenosine Triphosphatases↗

PubMed1977

Transport adenosine triphosphatase activity in the rat cornea.

The sodium-potassium activated adenosine triphosphatase (NaKATPase) activity of the rat cornea was investigated histochemically using a Pb2+-precipitation technique in which adenosine triphosphate (ATP) is used as substrate and two methods for potassium-dependent para-nitrophenyl-phosphatase (K-NPPase) activity. With all the three techniques used it was demonstrated that the sodium-potassium-activated adenosine triphosphatase (NaK-ATPase) activity is localized in the cell membranes of the endothelium whereas a much weaker activity was observed in the epithelium. When the Pb2+-technique was used, the epithelial cell membranes showed a weaker reaction in the presence of ouabain. This activity was only Mg2+-dependent and was presumably due to an Mg2+-dependent ATPase. The validity of the histochemical techniques for NaK-ATPase activity is discussed. The results emphasize the importance of the endothelium as the main site of Na+ transport in the cornea. Small amounts of the enzyme are also present in the epithelium, which seems to be rich in Mg2+-ATPase. Provided that careful controls are performed, all the methods give consistent results in the cornea.

4-Nitrophenylphosphatase↗

PubMed1980

Inhibition of adenosine triphosphatases by gold.

Inhibition of adenosine triphosphatase (ATPase) by chlorauric acid (Au3+) and gold sodium thiomalate (Au+) was studied in dog brain and kidney and in human kidney enzyme preparations. Au3+ indiscriminately affected ouabain-sensitive (Na+ + K+-dependent) ATPase and ouabain-insensitive (Mg2+-dependent) ATPase with concentrations for 50% inhibition (I50) approximately 10(-6) M. The I50 of Au3+ for Na+ + K+ ATPase was several-fold higher in homogenates than in microsomal fractions. The enzyme was protected by bovine serum albumin. Although Au3+ and Au+ were equipotent against Mg2+ ATPase, Au+ inhibited Na+ + K+ ATPase 2 to 3 times more effectively than did Au3+. The inhibitory action of Au3+ (but not Au+) was potentiated by ascorbic acid, suggesting reduction of Au3+ to Au+ by ascorbic acid. The fractional inhibition of Na+ + K+ ATPase by Au3+ or Au+ was not affected by changing concentrations of NaCl, KCl, MgCl2, ATP, and MgATP. Decreasing pH from 8.0 to 6.8 enhanced both Au+ and Au3+ inhibition. We conclude that gold is one of the most potent nonspecific of Na+ + K+ ATPase, with characteristics differing from other metallic inhibitors of this enzyme system.

Animals↗

PubMed2000

A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphatase.

The H,K-adenosine triphosphatase (ATPase) of gastric parietal cells is targeted to a regulated membrane compartment that fuses with the apical plasma membrane in response to secretagogue stimulation. Previous work has demonstrated that the alpha subunit of the H, K-ATPase encodes localization information responsible for this pump's apical distribution, whereas the beta subunit carries the signal responsible for the cessation of acid secretion through the retrieval of the pump from the surface to the regulated intracellular compartment. By analyzing the sorting behaviors of a number of chimeric pumps composed of complementary portions of the H, K-ATPase alpha subunit and the highly homologous Na,K-ATPase alpha subunit, we have identified a portion of the gastric H,K-ATPase, which is sufficient to redirect the normally basolateral Na,K-ATPase to the apical surface in transfected epithelial cells. This motif resides within the fourth of the H,K-ATPase alpha subunit's ten predicted transmembrane domains. Although interactions with glycosphingolipid-rich membrane domains have been proposed to play an important role in the targeting of several apical membrane proteins, the apically located chimeras are not found in detergent-insoluble complexes, which are typically enriched in glycosphingolipids. Furthermore, a chimera incorporating the Na, K-ATPase alpha subunit fourth transmembrane domain is apically targeted when both of its flanking sequences derive from H,K-ATPase sequence. These results provide the identification of a defined apical localization signal in a polytopic membrane transport protein, and suggest that this signal functions through conformational interactions between the fourth transmembrane spanning segment and its surrounding sequence domains.

Amino Acid Sequence↗

PubMed1982

Effect of chronic ethanol treatment on temperature dependence and on norepinephrine sensitization of rat brain (Na+ + K+)-adenosine triphosphatase.

Rat brain (Na+ + K+)-adenosine triphosphatase is inhibited by ethanol (EtOH) in vitro, the inhibition being greater in the presence of norepinephrine (NE). Enzyme preparations from EtOH-tolerant rats show less inhibition by EtOH in vitro and less sensitization by NE. To investigate the mechanism of these changes, the enzyme activity of brain microsomes from tolerant and sucrose-control rats was measured at temperatures from 10-40 degrees C. Preparations from nonwithdrawn and 24-hr withdrawn rats were studied in the absence of in vitro additions, and in the presence of 1 microM NE, 50 mM EtOH or 440 mM EtOH separately, and of 1 microM NE + 50 mM EtOH. From Arrhenius plots of the results, the transition temperature (Td) was calculated by a method of successive approximations, and the activation energies were calculated from the segments above and below Td. Chronic EtOH treatment significantly decreased Td, but increased activation energies below Td. These findings suggest different effects on membrane matrix lipids than on boundary lipids adjacent to the enzyme. However, EtOH-tolerant preparations showed less effect of EtOH in vitro than did control preparations, on both Td and activation energies. Preparations from EtOH-tolerant and withdrawn rats behaved almost identically, indicating that the changes accompany tolerance and are not withdrawal effects. NE + 50 mM EtOH produced the same effects as 440 mM EtOH alone, in all preparations. EtOH tolerance reduced the sensitizing effect of NE. EtOH is interpreted as affecting both the boundary lipids and the apoenzyme itself.

Animals↗

PubMed1990

Immunohistochemical localization of sodium-potassium-stimulated adenosine triphosphatase and carbonic anhydrase in human colon and colonic neoplasms.

Sodium-potassium-stimulated adenosine triphosphatase and carbonic anhydrase isozymes I and II were localized immunocytochemically in adenomas, adenocarcinomas, and normal epithelium of human colon harboring non-neoplastic lesions. Non-neoplastic control colon showed carbonic anhydrase I and II in the cytoplasm of the columnar cells lining the upper half of the crypts. Antiserum to sodium-potassium-stimulated adenosine triphosphatase bound to the basolateral but not the apical plasmalemma of columnar epithelial cells. Staining was most intense in the superficial cells, which also contained carbonic anhydrase, but was also evident to a lesser degree in cells deep in the crypts. Adenomas and adenocarcinomas failed to stain for content of carbonic anhydrase but retained basolateral sodium-potassium adenosine triphosphatase positivity. The staining characteristics of colonic neoplasms for the two enzymes involved in the transport function of colonic epithelium thus resembled those of the less mature cells lining the base of normal crypts.

Adenocarcinoma↗