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 state of existence of cytoplasmic vanadium ion is known to be important: vanadyl ion forms complexes with ATP and vanadate form inhibits (Na++K+)-ATPase. Therefore, the formation of complexes between ATP and vanadyl ion was investigated. Formations of three types of complex were observed: a blue 1:1 complex formed in acidic pH region; a blue 1:1 complex formed in neutral pH region; a green 2:1 complex formed in alkaline pH region. On the basis of the results on potentiometric titration, optical and EPR spectra and 31P- and 13C-NMR spectra, three characteristic types of coordination environment are proposed.
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PMID:Structures of ATP(adenosine triphosphate)-vanadyl complexes. 630 4

Ionized forms of vanadium are known to exert diverse biological activities. Of particular interest in the inhibitory action of the vanadium ion on (Na+ + K+)-ATPase. This report describes another action of the vanadium ion on the rabbit colonic epithelium. Micromolar quantities of vanadate, applied to the serosal side of the isolated rabbit colonic epithelium, result in a stimulation of electrogenic chloride secretion by this epithelium. Sodium transport is unaffected by the vanadium ion in the concentrations used in this study. It is proposed that the vanadyl ion activates adenylate cyclase and thereby initiates subsequent secretory events.
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PMID:Vanadium ion stimulation of chloride secretion by rabbit colonic epithelium. 630 80

The impact of vanadate on the Na,K-ATPase system in the vascular smooth muscle cell is poorly understood. The present study describes the kinetics of the effect of vanadate on Na,K-ATPase and the Na-K pump in in vitro grown rat VSMC's. Vanadate interaction with the Na,K-ATPase system in vascular smooth muscle cells was examined by observing its influence on ouabain-sensitive adenosine triphosphate hydrolysis in disrupted cells rendered permeable by osmotic shock, and the uptake of rubidium by intact cells. The I50 for vanadate inhibition of ouabain-sensitive hydrolysis of adenosine triphosphate occurred at vanadate concentrations of 10(-6) to 10(-7) M. This inhibition was potassium dependent. The maximal inhibitory effect of vanadate occurred at potassium concentrations of 10-20 mEq/liter. Sodium exerted a moderate antagonistic influence on vanadate inhibition of ouabain-sensitive adenosine triphosphate hydrolysis. Rubidium uptake by vascular smooth muscle cells was not altered within 120 minutes when 10(-5) M vanadate was added to the medium containing intact vascular smooth muscle cells. Yet, vanadium concentrations in the vascular smooth muscle cells within this incubation period reached levels 1.48-fold higher than the extracellular vanadate concentrations of 10(-5) M. These observations indicate that vanadate is a potent inhibitor of the VSMC Na,K-ATPase in disrupted vascular smooth muscle cells. However, in intact vascular smooth muscle cells vanadium gaining access into the vascular smooth muscle cell's interior does not inhibit the Na-K pump, probably because of its binding to intracellular proteins and/or conversion from the vanadate to the vanadyl ion.
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PMID:Vanadate effect on the Na,K-ATPase and the Na-K pump in in vitro-grown rat vascular smooth muscle cells. 630 30

Vanadium (V), a metallic element of the first transition series, is widely distributed in the environment. Although an essential trace element in higher animals, chronic exposure to V is of concern because of its increased concentration near industrial operations, its occurrence in the ash of combustion products of petroleum and coal, and its subsequent biomagnification in the environment. V is found in trace amounts in both terrestrial and aquatic animals and in solution can form inorganic orthovanadate oxyanions that, if absorbed, are eliminated primarily by the kidneys. Because V is often found concentrated in renal tissue to the largest extent in the body, the kidneys may represent a major site of action. Moreover, V in the vanadate configuration increases the urinary excretion of solutes and water in the rat, and inhibits renal organic ion accumulation and renal Na+, K+-ATPase in vitro and in vivo. Furthermore, as a nutritionally required element, V may play a regulatory role in salt and water excretion by modification of the Na+ pump in the kidney.
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PMID:Vanadium: chemistry and the kidney. 631 32

Vanadium is distributed extensively in nature. It is a trace element and is present in almost all living organisms including man. Even though vanadium was originally recognized for its ability to inhibit membrane Na+-K+-ATPase, various laboratory studies now document that this element has the capacity to affect the activity of various intracellular enzyme systems and may modify their physiological functions. Vanadium may be an essential element for normal development and may play an important role in various homeostatic mechanisms, and thus vanadium deficiency may prove to be an important concern. Abnormalities in biological disposition of vanadium may be involved in the pathogenesis of certain neurological disorders or cardiovascular diseases. While the essentiality of this element for living organisms is yet to be established with certainty, vanadium has become an increasingly important element and is used extensively in various heavy industries such as steel, oil, etc.; thus, the incidence of exposure to toxic levels of vanadium to industrial workers has been an increasing concern for toxicologists. To date, little information is available on the physiological or pharmacological actions of vanadium; hence, it is difficult to reach any definitive conclusion concerning its biological significance, essentiality and its role in pathological states. An attempt has been made in this review to broadly document what is known of various biological actions of vanadium.
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PMID:Minireview: physiological and pharmacological properties of vanadium. 631 32

Changes in cytosolic free Ca may function as a second messenger in neutrophils. Since the plasma membrane seems to be a major regulator of intracellular Ca in many cells, we characterized an energy-dependent Ca transport system in plasma membrane-enriched fractions ("podosomes") from phorbol myristate acetate-stimulated guinea pig and human neutrophils. The active Ca transport system in guinea pig podosomes exhibited a high affinity for Ca (Michaelis constant [Km]Ca 280 +/- 120 nM) and a maximum velocity of 0.83 nmol Ca/mg protein per min. Uptake showed an absolute requirement for Mg ATP (Km ATP 67 microM), whereas other trinucleotides were inactive. Ca uptake was optimal at pH 7, was azide insensitive and temperature dependent. Vanadium, an inhibitor of the Ca/Mg ATPase of heart sarcolemma, inhibited Ca pump activity by 50% at 1 microM. Ca transport was not affected in a NaCl-containing medium, an observation arguing against the presence of a Na/Ca exchange system. Calmodulin at 0.5-10 micrograms/ml stimulated the Ca pumping activity of EGTA-washed podosomes. Calmodulin depletion decreased the affinity of the Ca pump for Ca (Km Ca 2.07 microM) and its readdition restored it (Km Ca 0.55 microM). ATP-dependent Ca transport by podosomes and phagocytic vesicles was inactivated by exposure to trypsin or to the nonpenetrating sulfhydryl reagent rho-chloromercuribenzene sulfonate. Human podosomes had a Ca uptake system with properties similar to those of the guinea pig. These findings demonstrate the presence of a Ca pump in the neutrophil plasma membrane, which is active at physiological concentrations of free cytosolic Ca. By changing Ca concentrations at the cell periphery, this pump could control various motile functions of the neutrophil, such as locomotion or degranulation.
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PMID:Adenosine triphosphate-dependent calcium pump in the plasma membrane of guinea pig and human neutrophils. 631 13

Vanadyl, the tetravalent state of vanadium and a divalent cation, VO2+, was a relatively powerful inhibitor of highly purified membrane-bound sodium and potassium ion transport adenosine triphosphatase. The sensitivity of the ATPase activity to vanadyl characteristically correlated positively with the specific activity of the enzyme preparation. Inhibition ranged from nearly complete inhibition at less than 5 microM vanadyl for some of the purest fractions (specific activity approximately 45 mumol/min/mg of protein) to no observable inhibition at 300 microM vanadyl in one crude preparation of the enzyme with a specific activity of 10 mumol/min/mg of protein. The level of free vanadyl was reduced by incubation with these membranes, but this reduction was not sufficient to account for the low sensitivity to vanadyl observed in crude preparations. A reduction in specific activity by partial inactivation of a sensitive preparation by treatment with FeCl3 and ascorbate reduced its sensitivity to vanadyl. Anionic ligands of the enzyme, vanadate or ATP, increased the rate of recovery from inhibition after chelation of free vanadyl. At pH 6.1, the inhibition was characteristically fully reversible (t1/2 approximately 10 min), whereas at pH 8.1 it was stable for hours. The degree and stability of enzyme inhibition by vanadyl increased for several hours during incubation of the vanadyl-enzyme mixture, and at pH 6.1 the properties of the inhibitor itself also changed with time. Preincubation of the ion at that pH for 5 h before addition of the enzyme produced a more stable inhibition. The time- and pH-dependent changes in the degree and stability of enzyme inhibition probably relate to the complex chemistry of the vanadyl ion in solution.
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PMID:Inhibition of (Na,K)-ATPase by tetravalent vanadium. 632 13

The effect of vanadium oxides on living systems may involve the in vivo conversion of vanadate and vanadyl ions. The addition of 5 mM orthovanadate (VO4(3-), V(V)), a known inhibitor of the (Na,K)-ATPase, to yeast cells stopped growth. In contrast, the addition of 5 mM vanadyl (VO2+, V(IV) stimulated growth. Orthovanadate addition to whole cells is known to stimulate various cellular processes. In yeast, both ions inhibited the plasma membrane Mg2+ ATPase and were transported into the cell as demonstrated with [48V]VO4(3-) and VO2+. ESR spectroscopy has been used to measure the cell-associated paramagnetic vandyl ion, while 51V NMR has detected cell-associated diamagnetic vanadium (e.g. V(V)). Cells were exposed to both toxic (5 mM) and nontoxic (1 mM) concentrations of vanadate in the culture medium. ESR showed that under both conditions, vanadate became cell associated and was converted to vanadyl which then accumulated in the cell culture medium. 51V NMR studies showed the accumulation of new cell-associated vanadium resonances identified as dimeric vanadate and decavanadate in cells exposed to toxic amounts of medium vanadate (5 mM). These vanadate compounds did not accumulate in cells exposed to 1 mM vanadate. These studies confirm that the inhibitory form of vanadium usually observed in in vitro experiments is vanadate, in one or more of its hydrated forms. These data also support the hypothesis that the stimulatory form of vanadium usually observed in whole cell experiments is the vanadyl ion or one or more of its liganded derivatives.
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PMID:Metabolism of added orthovanadate to vanadyl and high-molecular-weight vanadates by Saccharomyces cerevisiae. 638 12

The evidence for the involvement of vanadium in the aetiology of manic depressive psychosis is reviewed. Raised levels of vanadium have been reported in plasma in mania and depression and raised hair levels reported in mania. Lithium has been reported to reduce the inhibition of Na-K ATPase by vanadate. Several groups of psychotropic drugs (e.g. phenothiazines, monoamine oxidase inhibitors) have been shown to catalyse the reduction of vanadate to the less active vanadyl ion. Therapies based on decreasing vanadate levels in the body (e.g. ascorbic acid, EDTA, methylene blue) have been reported to be effective in both depression and mania.
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PMID:Vanadium and manic depressive psychosis. 644 82

The effect of vanadium (as VO3-) on the uptake and release of tritiated noradrenaline ([3H]NA) was studied in vitro in rat cerebral cortex slices. Vanadate inhibited [3H]NA uptake and the inhibition was dependent upon concentration and on incubation time. The IC50 value (20 min incubation) was 8 X 10(-5) M of vanadate. Inhibition of Na+, K+ -ATPase activity by VO3-, chelation of noradrenaline or autooxidation of catecholamine by this oxyanion might contribute to the decrease of [3H]NA uptake. Vanadate inhibited also the release of [3H]NA in a time- and concentration-dependent fashion.
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PMID:Effect of metavanadate on the uptake and release of noradrenaline in rat brain cerebral cortex slices. 660 67


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