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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)

A study was conducted on the reconstituted erythrocytes obtained by the method of fast reversible hemolysis. The concentration of free Ca2+ ions in the reconstituted erythrocytes was supported by Ca-EGTA and Ca-nitrate buffers. Oubain-uninhibited ATPase component with a high affinity for Ca2+ (K0.5=4 micron) and alteration of passive and active K+-permeability in the region of free Ca2+ concentration up to 10 micron could be determined only when the content of membrane-bound Ca+ varied. Depletion of the inner side of the membrane of reconstituted erythrocyte is accompanied by alteration of hydrophobic character of the hydrocarbon region of the membrane. It is suggested that Ca+-induced alterations in the structure of the erythrocyte membrane may be a direct cause of the alterations in ATPase activity with a high Ca2+ affinity and permeability for univalent cations.
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PMID:[Role of membrane-bound calcium in changes in the ATPase activity, permeability and structural state of human erythrocyte membranes]. 14 75

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

Differential centrifugation of rat small intestinal homogenates produced a crude brush border (BB) fraction that was enriched 15-fold for the marker enzymes, alkaline phosphatase and sucrase; contamination with mitochondrial enzymes, monoamine oxidase and succinate dehydrogenase, was minimal. ATP hydrolysis by this BB fraction was stimulated by addition of several anions to the incubation medium: HCO3 and Cl were equally effective in this regard, with NO3, NO2, SO4, and acetate being less stimulatory. SCN and CNO inhibited ATPase activity, whereas the divalent anion SO3 was stimulatory at low concentrations (less than 25 mM) but inhibitory at 100 mM. Maximum anion stimulation was observed at a Mg concentration of 0.5 mM, and pH optimum was 8.5. Kinetic analysis showed that HCO3 increased the Vmax without altering the Km for ATP; the Ka for this effect of HCO3 was 35 mM. This enzyme activity was completely inhibited by 20 mM L-phenylalanine, 10 mM L-cysteine, and 3 mM EDTA, compounds that also inhibited intestinal alkaline phosphatase. These results demonstrate the presence of anion-stimulated ATPase activity in rat small intestinal brush border and suggest that this activity may be related to intestinal alkaline phosphatase. The role of this enzyme in intestinal transport is not known, but could relate to the regulation of intestinal absorption and secretion.
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PMID:Anion-stimulated ATPase activity of brush border from rat small intestine. 15 3

Dual localization of acid phosphatase in lysosomal and extralysosomal sites of the tubule epithelial cells of normal mouse kidney was observed at the light and electron microscope level using a modified Gomori lead-salt method with p-nitrophenylphosphate (pNPP) as substrate. Based on previous biochemical and cytochemical findings, we developed optimal conditions for the enzyme activity in extralysosomal sites. The conditions used for the light microscopic level consisted of 1.5 mM PNPP, 2.0 MM Pb(NO3)2 and 0.05 M acetate buffer (pH 5.8). Those for the electron microscopic study required 3.0 mM PNPP, 3.6 MM Pb(NO3)2 and 0.1 M acetate buffer (pH 5.8). This modified lead-salt technique was highly specific and provided a suitable method for the demonstration of nonlysosomal as well as lysosomal sites of acid phosphatase activity in the tubule epithelial cells of normal mouse kidney. As expected, the enzyme activity appeared in the lysosomes, but the prominent reaction in the brush border, the rough endoplasmic reticulum and basal infolding plasma membranes was not anticipated. We were able to demonstrate in situ organelle precursors of microsomal acid phosphatase such as endoplasmic reticulum, plasma membrane and basal infolding membranes showing the same substrate preference, which had been observed previously in biochemical studies in our laboratory. Since the possible participation of alkaline phosphatases, K+-pNPPase or Na+-K+-adenosine triphosphatase was ruled out by use of appropriate inhibitors, the enzyme-reactive sites can be interpreted as reflecting nonspecific acid phosphatase.
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PMID:Demonstration of lysosomal and extralysosomal sites for acid phosphatase in mouse kidney tubule cells with p-nitrophenylphosphate lead-salt technique. 23 53

Proximal convoluted tubules were dissected from rabbit kidneys and perfused in vitro in order to determine the effect of monovalent ions on fluid absorption and transepithelial voltage. Replacement of sodium in the perfusate and bath by lithium, tetramethyl ammonium or choline caused the rate of fluid absorption and voltage to fall to near zero. Replacement of potassium in the bath by sodium had the identical effect. Replacement of chloride by nitrate or perchlorate had comparatively little effect. The results are consistent with the generally held view that active sodium transport (mediated by a Na- and K- activated adenosine triphosphatase) is the primary process responsible for the absorption of the fluid and the voltage. Replacement of bicarbonate in the perfusate and bath by chloride caused the rate of fluid absorption to decrease by 33%. The possible relation between sodium transport and bicarbonate is discussed.
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PMID:Role of monovalent ions in the reabsorption of fluid by isolated perfused proximal renal tubules of the rabbit. 97 42

Ethanol (3%) decreases the potential difference and short-circuit current across the isolated frog skin in chloride Ringer's solution. Unidirectional fluxes of Na and Cl indicate that the drop in short-circuit current is due to an inhibition of the sodium influx. However, ethanol had no effect on the electrical parameters or sodium fluxes, when the frog skin was bathed in chloride-free solutions on both sides or the outside alone. The ethanol response is anion-dependent. In addition, chloride-free media in the inside bathing solution reduced the short-circuit current, indicating a sodium transport pathway which is dependent on chloride and confirming previous data in the literature. Other anions such as sulfate and nitrate could not substitute for chloride. The vasopressin-induced natriferic response and the ethanol effect were found to work independently of each other and different pathways of action are suggested for these agents. The intracellular sodium content of the isolated frog skin epithelium increased and potassium decreased in the presence of the Na-K adenosine triphosphatase inhibitor, ouabain, whereas ethanol or amiloride had no effect. The oxygen consumption of the isolated frog skin was unaffected by up to 10% ethanol. A general metabolic action is probably thus not mediating the response. Urea, in iso-osmotic concentrations to the ethanol, did not mimic its effect. Tritiated water fluxes (in the absence of an osmotic gradient) were reduced by 30% in the presence of 3% ethanol. It is suggested that ethanol may impede the flow of water across frog skin by a physicochemical interaction with membrane pores and the water molecules. The permeability coefficient (Ktrans) for ethanol was found to be 10 times smaller than the Ktrans for water.
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PMID:Effects of ethanol on the permeability of frog skin. 108 5

By means of silver nitrate impregnation and ATPase methods the distribution of all links of the lymph node vascular bed has been investigated. Structure of the blood capillary wall has been studied electron microscopically; they are defined as capillaries of the I type, that is having a continuous endothelial and basal layers and a small diameter. An essential amount of ribosomes is specific for blood capillary endothelium in the lymph nodes. A dendrite-like ramification of the portal veins is described, dichotomic--for the cerebral arteries, as well as the distribution of cortical arteries and arterioles. The postcapillary venules are found to localize around the lymphoid noduli and in the paracortical zone. Morphological bases for better exchange between blood and lymph are demonstrated in the cortex of the lymph node. Morphological signs of littoral cells of the lymphatic sinuses have been investigated and a conclusion is made on similarity in the structure of the lymphatic sinus wall and the wall of the lymphatic capillaries. Tight structural interrelations have been stated to exist between the wall of the lymph node blood vessels, its stroma and the wall of the lymphatic sinuses.
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PMID:[The morphofunctional characteristics of the vascular bed of the lymph nodes]. 128 89

The freshwater cyanobacterium Synechococcus PCC 6311 is able to adapt to grow after sudden exposure to salt (NaCl) stress. We have investigated the mechanism of Na+ transport in these cells during adaptation to high salinity. Na+ influx under dark aerobic conditions occurred independently of delta pH or delta psi across the cytoplasmic membrane, ATPase activity, and respiratory electron transport. These findings are consistent with the existence of Na+/monovalent anion cotransport or simultaneous Na+/H(+)+anion/OH- exchange. Na+ influx was dependent on Cl-, Br-, NO3-, or NO2-. No Na+ uptake occurred after addition of NaI, NaHCO3, or Na2SO4. Na+ extrusion was absolutely dependent on delta pH and on an ATPase activity and/or on respiratory electron transport. This indicates that Na+ extrusion via Na+/H+ exchange is driven by primary H+ pumps in the cytoplasmic membrane. Cells grown for 4 days in 0.5 M NaCl medium, "salt-grown cells," differ from control cells by a lower vmax of Na+ influx and by lower steady-state ratios of [Na+]in/[Na+]out. These results indicate that cells grown in high-salt medium increase their capacity to extrude Na+. During salt adaptation Na+ extrusion driven by respiratory electron transport increased from about 15 to 50%.
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PMID:NMR studies on Na+ transport in Synechococcus PCC 6311. 131 38

A subcellular fraction enriched in cytochrome c reductase (7.9-fold) and relatively de-enriched (0.64-fold) in Na+/K(+)-ATPase was prepared from canine kidney cortex by sucrose density gradient ultracentrifugation. It was shown by electron microscopy to consist primarily of a light fraction of endoplasmic reticulum (LER). LER vesicles displayed ATP-dependent 45Ca2+ uptake that was insensitive to 10 mM KCN or NaN3, and was promptly released by 20 microM A23187 or ionomycin. Inositol-1,4,5-trisphosphate (IP3) appeared to produce a time-dependent release of 45Ca2+. Vanadate inhibited 45Ca2+ uptake with a Ki approximately 0.3 mM, further suggesting that the activity resided in the ER rather than the plasma membrane. 45Ca2+ uptake by LER, at 5 microM total [Ca2+], displayed a strong dependence on divalent cations (Mg2+ greater than Co2+ greater than Mn2+ much greater than Ba2+ greater than or equal to Cd2+ greater than or equal to Sr2+, present at 2 mM) as well as on monovalent cations (Na+ greater than or equal to K+ + Na+ greater than K+ greater than Li+ greater than choline +), and anions (Cl- greater than acetate- greater than or equal to NO3- greater than or equal to F- greater than H2PO4- much greater than gluconate- greater than or equal to oxalate= much greater than SO4=). It had a fairly narrow pH optimum (7.25-7.50). Preincubation (10 min) of LER vesicles with 12-O-tetradecanoylphorbol-13-acetate (TPA) stimulated LER Ca2+ uptake; this effect was enhanced in the presence of renal cytosol [5% (vol/vol)].(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Ca2+ uptake by endoplasmic reticulum of renal cortex. I. Ionic requirements and regulation in vitro. 132 65

Metal-binding proteins are important components of retroviruses such as human immunodeficiency virus (HIV). Therefore, metals could be used as antiviral agents. However, most metals are toxic for humans with the exception of silver which is toxic only to prokaryotic cells and viruses. In addition, HIV infection causes a decrease in body cysteine. We formed a complex of silver and cysteine, named silver-cysteine. Healthy human lymphocytes were incubated with silver-nitrate or silver-cysteine. Negligible cell survival was seen at 50 microM silver-nitrate. However, in presence of 1 mM cysteine, the viability remained unaffected up to 1 mM of silver. Further, silver inhibition of isolated Na,K-ATPase was easily reversed by cysteine. Thus, non-toxic silver-cysteine could be used as an anti-viral and cysteine-replenishing agent.
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PMID:Cysteine protects Na,K-ATPase and isolated human lymphocytes from silver toxicity. 133 67


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