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)

Vanadium in the 4+ (vanadyl-ion) and 5+ (vanadate-ion) oxidation state stimulates furosemide-sensitive electrogenic Cl- secretion in isolated epithelia of rabbit descending colon. This effect is associated with an increased release of prostaglandin E2 from the tissue. Inhibitors of phospholipase A2 or cyclooxygenase abolish both vanadium-induced release of prostaglandin E2 and Cl- secretion. Neuronal mechanisms are not likely to be involved, as tetrodotoxin does not affect the vanadate induced Cl- secretion. Although vanadate is known to inhibit Na+,K(+)-ATPase activity, no inhibition of active Na+ transport was observed in intact colonic epithelia suggesting a rapid intracellular reduction of vanadate ions to vanadyl ions which have no inhibitory effect on the Na+,K(+)-ATPase. The present findings therefore indicate that vanadate stimulated colonic Cl- secretion involves intracellular conversion of vanadate to vanadyl and release of prostaglandin E2.
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PMID:Vanadium-induced Cl(-)-secretion in rabbit descending colon is mediated by prostaglandins. 161 17

Beta-Bungarotoxin (beta-BuTX) and notexin are phospholipase A2 (PLA2) neurotoxins which cause an irreversible blockade of neurotransmitter release through specific and potent effects at the presynaptic nerve terminal; however, their mechanism of action is uncertain. We examined the effects of beta-BuTX and notexin on Na+/K+ ATPase activity using Sprague-Dawley rat brain synaptosomes in order to determine if alterations in activity might modulate neurotoxin-induced depolarization. Treatment of synaptosomes with 0.05 to 5 nM beta-BuTX, notexin, and Naja naja atra and Naja nigricollis PLA2 (PLA2 enzymes without selective presynaptic actions) caused a dose-dependent depolarization of synaptosomes with no differences being observed between the effects of the PLA2 neurotoxins and enzymes. N. nigricollis PLA2 (0.5 nM; 20 min) slightly stimulated Na+/K+ ATPase activity while beta-BuTX and notexin (0.5 nM: 10 and 20 min) were without effect. With 50 nM concentrations beta-BuTX and notexin stimulated Na+/K+ ATPase activity, while N. nigricollis and N. n. atra PLA2 inhibited activity. The effects on membrane potential and Na+/K+ ATPase were antagonized or blocked by EDTA (10 mM) and bovine serum albumin (1 mg/ml), suggesting that PLA2 enzymatic activity is essential for their effects on membrane potential and Na+/K+ ATPase activity. Following neurotoxin and enzyme pretreatment, we found a biphasic correlation between synaptosomal free fatty acid (FFA) levels and Na+/K+ ATPase activity, where Na+/K+ ATPase is stimulated by low levels of FFA (0.13 to 0.22 mumol/mg protein) and antagonized by FFA levels in excess of 0.34 mumol/mg protein. In contrast there was a linear correlation between the extent of FFA production and membrane depolarization. We propose that the presynaptic depolarizing actions of beta-BuTX and notexin are not mediated through modulation of Na+/K+ ATPase activity and that the changes observed in ATPase activity and possibly membrane potential are directly due to PLA2 enzymatic activity and the production of FFA.
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PMID:Comparative effects of phospholipase A2 neurotoxins and enzymes on membrane potential and Na+/K+ ATPase activity in rat brain synaptosomes. 164 1

Treatment of rat brain slices with veratrine and monensin decreased (Na+ + K+)-ATPase activity in the membranes in a dose-dependent manner. The effect of monensin, like that of veratrine, was accompanied by a decrease of maximal binding sites for ouabain. The inhibitory effect of monensin on the enzyme activity was dependent on external Ca2+ at low concentrations, but not at a high concentration. The decreased enzyme activity induced by monensin was restored by subsequent incubation of the slices in a Ca(2+)-free medium containing 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetraacetoxymethyl ester (BAPTA-AM), a chelator of intracellular Ca2+. The effect of monensin at a low concentration on enzyme activity was antagonized by amiloride (1 mM), bepridil (5 microM), quinacrine (30 microM) or verapamil (30 microM), but not by nifedipine (1 microM) or omega-conotoxin (1 microM). Furthermore, the inhibitory effect of monensin at a high concentration under Ca(2+)-free conditions was blocked by BAPTA-AM (30 microM) and by bepridil (100 microM) or diazepam (500 microM), inhibitors of mitochondrial Na(+)-Ca2+ exchange. Inhibitors of calmodulin, protein kinase C, phospholipase A2 and calpain did not affect the monensin-induced decrease of enzyme activity. Dithiothreitol (10 mM) blocked the effect of monensin on enzyme activity but did not affect the ionophore-induced influx of Ca2+ in the slices.
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PMID:Na+ influx-induced decrease of (Na+ + K+)-ATPase activity in rat brain slices: role of Ca2+. 166 55

Treatment of purified preparations of porcine Na+,K(+)-ATPase with phospholipase A2, MgCl2 and NaVO3 leads to the formation of two-dimensional crystals exclusively in a dimeric configuration. Two-dimensional computer-averaged projections of the electron microscopy images of the crystalline enzyme with bound Fab fragments of monoclonal antibody M10-P5-C11 were accomplished using image enhancement software and showed that the antibody fragments caused only a modest increase in the unit cell size, while reducing the extent of asymmetry of the two promoters in each unit cell. The digital imaging also showed that the antibody's epitope on the alpha subunit resides on the 'lobe' or 'hook' region of the intracellular portion of the enzyme. Since functional studies indicate that M10-P5-C11 binds near or between the ATP binding site and the phosphorylation site, this visualized 'lobe' region of alpha may comprise the catalytic site. In addition, the binding of another inhibitory antibody, 9-A5, has been found to prevent crystal formation and the presence of the carbohydrate sugars on the enzyme's beta subunit shown to be required for crystal formation.
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PMID:Identification of monoclonal antibody binding domains of Na+,K(+)-ATPase by immunoelectron microscopy. 169 81

Exercise for which a skeletal muscle is not adequately conditioned results in focal sites of injury distributed within and among the fibres. Exercise with eccentric contractions is particularly damaging. The injury process can be hypothesised to occur in several stages. First, an initial phase serves to inaugurate the sequence. Hypotheses for the initial event can be categorised as either physical or metabolic in nature. We argue that the initial event is physical, that stresses imposed on sarcolemma by sarcomere length inhomogeneities occurring during eccentric contractions cause disruption of the normal permeability barrier provided by the cell membrane and basal lamina. This structural disturbance allows Ca++ to enter the fibre down its electrochemical gradient, precipitating the Ca++ overload phase. If the breaks in the sarcolemma are relatively minor, the entering Ca++ may be adequately handled by ATPase pumps that sequester and extrude Ca++ from the cytoplasm ('reversible' injury). However, if the Ca++ influx overwhelms the Ca++ pumps and free cytosolic Ca++ concentration rises, the injury becomes 'irreversible'. Elevations in intracellular Ca++ levels activate a number of Ca(++)-dependent proteolytic and phospholipolytic pathways that are indigenous to the muscle fibres, which respectively degrade structural and contractile proteins and membrane phospholipids; for instance, it has been demonstrated that elevation of intracellular Ca++ levels with Ca++ ionophores results in loss of creatine kinase activity from the fibres through activation of phospholipase A2 and subsequent production of leukotrienes. This autogenetic phase occurs prior to arrival of phagocytic cells, and continues during the inflammatory period when macrophages and other phagocytic cells are active at the damage site. The phagocytic phase is in evidence by 2 to 6 hours after the injury, and proceeds for several days. The regenerative phase then restores the muscle fibre to its normal condition. Repair of the muscle fibres appears to be complete; the fibres adapt during this process so that future bouts of exercise of similar type, intensity, and duration cause less injury to the muscle.
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PMID:Mechanisms of exercise-induced muscle fibre injury. 178 73

The effect of long-term ethanol intake on the structural and functional characteristics of rat skeletal-muscle mitochondria and sarcoplasmic reticulum was investigated. Functionally, skeletal-muscle mitochondria were characterized by a high respiratory control index and ADP/O ratio and a high State-3 respiration rate with different substrates. These parameters were not significantly different in preparations from control and ethanol-fed rats, except for a small increase in the rate of oxidation of alpha-oxoglutarate/malate in the latter. In submitochondrial particles from the two groups of animals there was no significant difference in cytochrome content, ATPase activity or the activity of respiratory-chain complexes. Mitochondrial membranes from untreated and ethanol-fed rats showed no difference in the baseline e.s.r. order parameter, and both preparations were equally sensitive to disordering by ethanol in vitro. Similarly, sarcoplasmic-reticulum preparations were not significantly affected by long-term ethanol feeding with respect to Ca2(+)-ATPase activity or in baseline order parameter and susceptibility to membrane disordering by ethanol in vitro. These membranes were also equally sensitive to degradation by exogenous phospholipase A2. Ethanol feeding did not alter the class composition of mitochondrial or sarcoplasmic-reticulum membrane phospholipids, nor the acyl composition of individual phospholipid classes. Specifically, the changes in acyl composition that characteristically occur in liver microsomal phosphatidylinositol and liver mitochondrial cardiolipin were not observed in the corresponding phospholipids from skeletal-muscle membranes. In experiments where membrane preparations from liver and skeletal muscle from the same ethanol-fed animals were compared, the liver membranes developed membrane tolerance, with the muscle membranes retaining normal sensitivity to disordering effects by ethanol. It is concluded that: (a) different tissues from the same animals differ in their susceptibility to ethanol; (b) the tissue-specific lack of development of membrane tolerance correlates with a lack of chemical changes in the phospholipids and with a retention of normal function of mitochondria and sarcoplasmic reticulum; (c) effects of chronic ethanol intake on muscle function are not due to a defect in the mitochondrial energy supply.
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PMID:Maintenance of structural and functional characteristics of skeletal-muscle mitochondria and sarcoplasmic-reticular membranes after chronic ethanol treatment. 184 61

The presence, distribution, and levels of phospholipase A2 and ATPases activities in those structures of the guinea pig spermatozoa that participate in the acrosome reaction were studied, both before and after capacitation, as well as during the acrosome reaction induced in vitro. Spermatozoa were collected from the cauda epididymis and incubated in the absence and presence of 1.15 mmol/L calcium, with and without the addition of 1 mumol/L A23187. Membrane fractions were recovered by vortexing and discontinuous sucrose density gradient centrifugation. Most of the Na+, K(+)-ATPase was recovered in the acrosome-free spermatozoa, but a clear, distinct presence of this enzyme was observed in the plasma membrane (25 against 101 nmoles Pi released per milligram of protein, respectively). The activity of this enzyme in the periacrosomal plasma and in the outer acrosomal membrane increased during calcium incubation. Ca2(+)-dependent ATPase was found in both membrane fractions, being higher in the periacrosomal plasma membrane. The addition of calcium induced a significant inhibition of this acrosomal ATPase, whereas the activity in the acrosome-free spermatozoa increased. The activity of phospholipase A2, under all experimental conditions, was found to be restricted to the soluble fraction.
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PMID:Subcellular distribution of phospholipase A2 and ATPases during capacitation and acrosome reaction in guinea pig spermatozoa. 185 52

Endogenous activities of phospholipases A and C in Ureaplasma urealyticum were assayed in cellular fractions of exponential-phase cells. Enzymatic studies indicated that ATPase activity was localized in the plasma membrane fraction and NADH and NADPH dehydrogenase activities were localized in the cytosol fraction. Studies with purified ureaplasma membranes demonstrated that, of three serovars tested, endogenous phospholipase A1, A2, and C activities were localized in the plasma membrane. Very low levels of activity were observed in the cytosol fractions. Phospholipase A2 activity in the plasma membrane was 3- to 5-fold higher than the activity in the lysates and 60- to 300-fold higher than the activity of phospholipase A1. Phospholipase C was localized mainly in the plasma membrane, with 20% found in the cytosol fraction. The levels of activity were comparable among the three serovars. There was a significantly lower level of activity in cells from the stationary growth phase than in the exponential phase. Significant differences were observed in the phospholipase A activities among the U. urealyticum serovars 3, 4, and 8. Phospholipase A2 activity was twofold higher in serovar 8 membranes, and phospholipase A1 activity was twofold higher in serovar 3 membranes. These results demonstrate that endogenous activities of phospholipase A and C are localized primarily in the plasma membrane fraction of U. urealyticum. The specific activities in the membranes of the phospholipases varied among the three serovars. Phospholipase enzymes may function as virulence factors in U. urealyticum and may vary among the serovars.
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PMID:Localization of endogenous activity of phospholipases A and C in Ureaplasma urealyticum. 188 45

Stimulation of macrophages with platelet-activating factor (PAF) elicits an increase of intracellular calcium concentration, Ca2+i, which was monitored here at the single cell level with the calcium-sensitive dye Fura-2. The sustained component of this Ca2+i increase reflects the dynamic balance achieved between enhanced Ca2+ influx and efflux. In macrophages where a steady increase of Ca2+i has been evoked by 50 nM thapsigargin (a molecule known to empty Ca2+ stores and elevate Ca2+i in various cell types), PAF activates Ca2+ efflux, without causing a preceding increase in Ca2+i. This result shows that in this case, Ca2+ extrusion is not merely a consequence of a Ca2+i increase. PAF-evoked Ca2+ extrusion does not result from the activation of the Na+/Ca2+ exchanger. Exogenous arachidonic acid (10-100 microM) elicits Ca2+ efflux in macrophages where Ca2+i has been previously elevated by either PAF or thapsigargin. PAF-induced Ca2+ extrusion is blocked by 4-bromophenacylbromide, an inhibitor of arachidonic acid production by phospholipase A2. Together, these results suggest that arachidonic acid, which is produced in PAF-stimulated macrophages, contributes to the regulation of a Ca2+ extrusion system, which is presumably a Ca2(+)-ATPase.
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PMID:Arachidonic acid activates Ca2+ extrusion in macrophages. 214 78

Current progress in the studies of myocardial membrane alterations during endotoxin shock indicates that endotoxin administration impairs (Na(+) + K(+)-ATPase enzyme system by disrupting the coordination of the ouabain receptor subunit and the catalytic subunit of the enzyme system, and that the disruption is due to an alteration in the lipid microenvironment and a decrease in the phosphorylated intermediate of the enzyme cycle. Studies of the membrane lipid profile provide evidence that endotoxin administration modifies the molecular structure of cardiac membrane lipids in association with the activation of phospholipases A1 and A2 and with the inhibition of phospholipid methylating enzymes. Using liposomes as a membrane model for investigation, endotoxin was found to be capable of modifying the physical property of membrane phospholipids by altering the molecular packing and the phase transition temperature of lipid bilayers. Further studies with Na(+)-Ca2+ exchange system in cardiac sarcolemma have established the roles of phospholipase A2 and protein phosphorylation on the endotoxin-induced derangement in myocardial Na(+)-Ca2+ exchange. Based on these studies, it is concluded that endotoxin administration exerts multiple injuries in different membrane-associated enzyme/receptor systems and that the mechanisms responsible for the endotoxin-induced membrane damage can be categorized into two conceptual frameworks: namely, changes in membrane lipid microenvironment in response to phospholipase A activation and alterations in the phosphorylation of the enzyme/receptor proteins.
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PMID:Mechanisms of myocardial membrane alterations in endotoxin shock: roles of phospholipase and phosphorylation. 215 41


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