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)

Purified basolateral membrane vesicles (BLMVs) were prepared from Atlantic lobster (Homarus americanus) hepatopancreas using a Percoll density gradient technique. Enrichments of the Na+/K+-ATPase and alkaline phosphatase activities of these vesicles were 15.4- and 1.2-fold, respectively. The presence of amiloride-sensitive Na+/H+ exchange was demonstrated. Contrary to electrogenic 2Na+/1H+ exchange on apical membranes from the same tissue, kinetic studies of Na+ transport by these basolateral membranes indicate an electroneutral antiport with a Km of 28±1.7 mmol l-1 and a Jmax of 1.74±0.13 µmol mg-1 min-1. Amiloride interacted at a single binding site (Ki=39 µmol l-1) and external Li+ was shown to be an effective competitive inhibitor of the exchange process (Ki=493 µmol l-1). The presence of a membrane-potential-sensitive, Na+-accepting ion channel was also demonstrated. The basolateral Na+/H+ exchanger physiologically resembles members of the NHE family of Na+/H+ antiporters described in vertebrates and departs from the apical electrogenic system previously described in lobster. Whether or not the basolateral Na+/H+ antiporter is an NHE isoform remains to be determined.
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PMID:Characterization of a basolateral electroneutral Na+/H+ antiporter in Atlantic lobster (Homarus americanus) hepatopancreatic epithelial vesicles 931 72

Acidocalcisomes are acidic vacuoles present in trypanosomatids that contain a considerable fraction of intracellular Ca2+. They possess a vacuolar-type H+-ATPase for H+ uptake, a Ca2+/H+ countertransporting ATPase for Ca2+ uptake and a Ca2+/nH+ antiporter for Ca2+ release. Trypanosoma brucei procyclic trypomastigotes acidocalcisomes possess, in addition, an Na+/H+ antiporter that may participate in Ca2+ release from these organelles. In this work we show that the hydrophobic antioxidant 3,5-dibutyl-4-hydroxy toluene (BHT), at concentrations in the range 1-20 microM, inhibits Na+-induced Ca2+ release from the acidocalcisomes of digitonin-permeabilized procyclic trypomastigotes in a concentration-dependent manner. This effect supports the notion that Ca2+ release from this compartment is regulated by the activity of the Na+/H+ antiporter. In the presence of BHT, Ca2+ release could still be obtained by nigericin-mediated alkalinization of the acidocalcisomes, clearly demonstrating that the action of BHT is not at the level of the Ca2+/nH+ antiporter but on that of the Na+/H+ antiporter. In the same range of concentrations and depending on the preincubation time, BHT had an stimulatory or an inhibitory effect on the vacuolar H+-ATPase present in T. brucei acidocalcisomes. Since these effects of BHT were obtained at concentrations which are commonly used for its antioxidant properties, these results indicate that care should be exercised when attributing effects of BHT to only these properties.
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PMID:Inhibition of Ca2+ release from Trypanosoma brucei acidocalcisomes by 3,5-dibutyl-4-hydroxytoluene: role of the Na+/H+ exchanger. 937 4

Alkaliphilic Bacillus species that are isolated from nonmarine, moderate salt, and moderate temperature environments offer the opportunity to explore strategies that have developed for solving the energetic challenges of aerobic growth at pH values between 10 and 11. Such bacteria share many structural, metabolic, genomic, and regulatory features with nonextremophilic species such as Bacillus subtilis. Comparative studies can therefore illuminate the specific features of gene organization and special features of gene products that are homologs of those found in non-extremophiles, and potentially identify novel gene products of importance in alkaliphily. We have focused our studies on the facultative alkaliphile Bacillus firmus OF4, which is routinely grown on malate-containing medium at either pH 7.5 or 10.5. Current work is directed toward clarification of the characteristics and energetics of membrane-associated proteins that must catalyze inward proton movements. One group of such proteins are the Na+/H+ antiporters that enable cells to adapt to a sudden upward shift in pH and to maintain a cytoplasmic pH that is 2-2.3 units below the external pH in the most alkaline range of pH for growth. Another is the proton-translocating ATP synthase that catalyzes robust production of ATP under conditions in which the external proton concentration and the bulk chemiosmotic driving force are low. Three gene loci that are candidates for Na+/H+ antiporter encoding genes with roles in Na(+)-dependent pH homeostasis have been identified. All of them have homologs in B. subtilis, in which pH homeostasis can be carried out with either K+ or Na+. The physiological importance of one of the B. firmus OF4 loci, nhaC, has been studied by targeted gene disruption, and the same approach is being extended to the others. The atp genes that encode the alkaliphile's F1F0-ATP synthase are found to have interesting motifs in areas of putative importance for proton translocation. As an initial step in studies that will probe the importance and possible roles of these motifs, the entire atp operon from B. firmus OF4 has been cloned and functionally expressed in an Escherichia coli mutant that has a full deletion of its atp genes. The transformant does not exhibit growth on succinate, but shows reproducible, modest increases in the aerobic growth yields on glucose as well as membrane ATPase activity that exhibits characteristics of the alkaliphile enzyme.
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PMID:pH homeostasis and ATP synthesis: studies of two processes that necessitate inward proton translocation in extremely alkaliphilic Bacillus species. 978 68

This study was an investigation of the mechanisms for the regulation of intracellular pH (pHi) by hamster preimplantation embryos. The resting pH values of hamster embryos were similar at the 1-cell (7. 19 +/- 0.34), 2-cell (7.21 +/- 0.21), and 8-cell (7.22 +/- 0.41) stages. Cleavage-stage hamster embryos alleviated intracellular acidosis by activity of the Na+/H+ antiporter. The rate of recovery from acidosis was similar for embryos at 1-cell, 2-cell, and 8-cell stages. When Na+/H+ antiporter activity was inhibited by either incubation in Na+-free medium or the presence of an inhibitor, pHi was unable to recover to initial levels. Instead, pHi remained acidic. The Na+/H+ antiporter was also found to contribute to baseline pH regulation, as incubation in Na+-free medium resulted in an immediate intracellular acidification. The set point for Na+/H+ antiporter was pH 7.14. There was no evidence at any developmental stage for activity of either Na+-dependent HCO3-/Cl- exchanger or H+-ATPase in the regulation of pHi. Inhibition of the Na+/H+ antiporter by an amiloride derivative significantly reduced the ability of 2-cell embryos to develop in culture when challenged with acidosis, indicating that the Na+/H+ antiporter is an essential regulator of pHi.
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PMID:Regulation of intracellular pH in hamster preimplantation embryos by the sodium hydrogen (Na+/H+) antiporter. 982 96

Both Na+/H+ exchange and the electrogenic extrusion of H+ via an H+-ATPase have been postulated to drive acid excretion across the branchial epithelium of fishes. While the H+-ATPase/Na+ channel system appears to be the predominant mechanism in some freshwater species, it may play a reduced role in seawater and brackish-water animals, where high external Na+ concentrations may thermodynamically favor Na+/H+ exchange driven by a Na+/H+ antiporter (NHE). In this study, we used molecular and immunological methods to assess the role of NHE isoforms in the branchial epithelium of the marine long-horned sculpin (Myoxocephalus octodecimspinosus) and the euryhaline killifish (Fundulus heteroclitus). Northern blot analysis of RNA probed with the human NHE-1 BamHI fragment suggested the presence of homologous gill NHE mRNA in sculpin. RT-PCR on gill RNA isolated from sculpin recovering from metabolic acidosis provided evidence for two distinct NHE isoforms; one with 76 % amino acid homology to mammalian NHE-2, and another 92 % homologous to trout erythrocytic beta-NHE. Killifish also have transcripts with 91 % homology to beta-NHE. Immunological detection using monoclonal antibodies for mammalian NHE-1 revealed a protein antigenically similar to this isoform in the gills of both species. Metabolic acidosis caused an approximately 30-fold decrease in expression of the NHE-1-like protein in sculpin. We speculate that beta-NHE in the gills plays the intracellular 'housekeeping' roles described for mammalian NHE-1. During systemic acidosis, apical gill NHE-2 (which is sensitive to external amiloride and low [Na+]) in parallel with a dramatic suppression of basolateral NHE-1 activity enhances net capdelta H+ transfers to the water.
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PMID:A mechanism for branchial acid excretion in marine fish: identification of multiple Na+/H+ antiporter (NHE) isoforms in gills of two seawater teleosts. 988 43

In a series of experiments aimed to understand the signaling pathways that regulate intracellular pH (pHi) in rat mast cells, the effect of different intracellular mechanisms on the activity of the Na+/H+ exchanger was studied. After promoting an artificial acidification with sodium propionate we determined the variations on pHi rate recovery. pHi was measured with the dye 2, 7-bis(carboxyethyl)-5(6)-carboxyfluorescein acetoxymethyl ester. We studied the effect that the inhibition of some cellular exchangers with different drugs induced on pHi. When the Na+/H+ exchanger was inhibited in the presence of amiloride, the recovery rate constant was twofold smaller than the control value. After the recovery, the final pH was lower than the initial value when the cells were treated either with amiloride or with 4, 4'-diisothiocyanatostilbene-2,2'-disulfonic acid (an anionic antiport inhibitor). No effect was observed when the Na+/K+-ATPase or the Na+/Ca2+ exchanger were inhibited. The suppression of intracellular and extracellular calcium did not induced any change in pHi. The addition of thapsigargin, an activator of capacitative calcium influx, or the phorbol esther 12-O-tetradecanoylphorbol-13-acetate (PMA), a protein kinase C (PKC) activator, increased the activity of the antiporter. Both effects were abrogated by inhibition of the Na+/K+-ATPase with ouabain. The increase in cAMP levels did not affect the effect of PMA on pHi recovery, but it blocked the effect of thapsigargin. Our results indicate that rat mast cells regulate pHi by the combination of some anionic exchanger and the Na+/H+ antiporter. And also that the modulation of this exchanger is the consequence of the connection between different intracellular mechanisms, Na+/K+-ATPase-PKC-calcium, among which cAMP seems not to have a direct role.
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PMID:Sodium, PMA and calcium play an important role on intracellular pH modulation in rat mast cells. 994 57

Perturbations of the extracellular osmotic environment leads to cell volume changes. The aim of the present study was to evaluate the effects of hyperosmolality on cardiac contractile function and in particular the role of ionic mechanisms anticipated to be operative during hyperosmolal exposure. Paced rabbit hearts were perfused in the Langendorff mode and were exposed to 330, 370, 410, 450 and 600 mOsm kg-1 in 10 min. intervals intervened by 15 min. isosmolal buffer perfusion (by adding mannitol). Thereafter, 370 and 600 mOsm kg-1 perfusates were chosen for investigation of the effects of inhibition of the Na-K-2Cl co-transporter (bumetanide 1 microM and 10 microM), the Na+/H+ exchanger (5-(N-ethyl-N-isopropyl amiloride (EIPA) 100 nM) and the Na+/K(+)-ATPase (ouabain 50 nM). After a rapid and transient decrease in left ventricular developed pressure, all perfusates up to 450 mOsm kg-1 increased LVDP. The 600 mOsm kg-1 perfusate initially reduced LVDP by 50%, but LVDP increased to 85% of initial value at the end of the 10 min. perfusion. EIPA attenuated the recovery of LVDP during perfusion with 600 mOsm kg-1, whereas bumetanide did not affect cardiac contractile function. A net uptake of potassium was observed during hyperosmolal perfusion. Inhibition of the Na+/H+ exchanger resulted in a continued release of cardiac water throughout hyperosmolal perfusion. Isolated perfused rabbit hearts tolerate considerable elevations in perfusate osmolality. Our results suggest that the Na+/H+ antiporter is activated on hyperosmolal exposure with a secondary activation of the Na+/K(+)-ATPase. Since inhibition with bumetanide did not affect contractility or electrolyte movements, the Na-K-2Cl co-transporter does not seem to play an important role in cardiac response to hyperosmolality in rabbits.
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PMID:Cardiac contractile function and electrolyte regulation during hyperosmolal stress: an experimental study in the isolated rabbit heart. 1022 69

Enterococcus hirae grows in a broad pH range from 5 to 11. An E. hirae mutant 7683 lacking the activities of two sodium pumps, Na+-ATPase and Na+/H+ antiporter, does not grow in high Na+ medium at pH above 7.5. We found that 7683 grew normally in high Na+ medium at pH 5.5. Although an energy-dependent sodium extrusion at pH 5.5 was missing, the intracellular levels of Na+ and K+ were normal in this mutant. The Na+ influx rates of 7683 and two other strains at pH 5.5 were much slower than those at pH 7.5. These results suggest that Na+ elimination of this bacterium at acid pH is achieved by a decrease in Na+ entry and a normal K+ uptake.
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PMID:Sodium ATPase and sodium/proton antiporter are not obligatory for sodium homeostasis of Enterococcus hirae at acid pH. 1087 90

In the male reproductive tract, the epididymis plays an important role in mediating transepithelial bicarbonate transport and luminal acidification. In the proximal vas deferens, a significant component of luminal acidification is Na+-independent, and mediated by specific cells that possess apical vacuolar proton pumps. In contrast, luminal acidification in the cauda epididymidis is an Na+-dependent process. The specific apical Na+-dependent H+/base transport process(es) responsible for luminal acidification have not been identified. A potential clue as to the identity of these apical Na+-dependent H+/base transporter(s) is provided by similarities between the transport properties of the epididymis and the mammalian nephron. Specifically, the H+/base transport properties of caput epididymidis resemble the mammalian renal proximal tubule, whereas the distal epididymis and vas deferens have characteristics in common with renal collecting duct intercalated cells. Given the known expression of the Na+/H+ antiporter, NHE3, in the proximal tubule, and of the electroneutral sodium bicarbonate cotransporter, NBC3, in renal intercalated cells, we determined the localization of NHE3 and NBC3 in various regions of rat epididymis. NBC3 was highly expressed on the apical membrane of apical (narrow) cells in caput epididymidis, and light (clear) cells in corpus and cauda epididymidis. The number of cells expressing apical NBC3 was highest in cauda epididymidis. The localization of NBC3 in the epididymis was identical to the vacuolar H+-ATPase. The results indicate that colocalization of NBC3 and the vacuolar H+-ATPase is not restricted to kidney intercalated cells. Moreover, the close association of the two transporters appears to be a more generalized phenomenon in cells that express high levels of vacuolar H+-ATPase. Unlike NBC3, NHE3 was most highly expressed on the apical membrane of all epithelial cells in caput epididymidis, with less expression in the corpus, and no expression in the cauda. These results suggest that apical NBC3 and NHE3 potentially play an important role in mediating luminal H+/base transport in epididymis.
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PMID:Immunolocalization of NBC3 and NHE3 in the rat epididymis: colocalization of NBC3 and the vacuolar H+-ATPase. 1097 18

Transport of Na+ and K+ ions through the plasma membrane of intact cells of the halotolerant microalga Dunaliella maritima Massjuk was studied. Ion fluxes through the plasma membrane were induced by hyperosmotic shock (uptake of Na+ by the cells is transformed into extrusion of Na+) or by addition of K+ to a suspension of K+-deficient cells (uptake of K+ by the cells is associated with extrusion of Na+). The pathway of Na+ extrusion from the D. maritima cells does not depend on the direction or value of the proton gradient on the plasma membrane. In particular, the efficiency of Na+ extrusion was not changed at extracellular pH values varying from 6.0 to 8.0. The protonophore carbonyl cyanide m-chlorophenylhydrazone (CCCP) (20 microM) and the H+-ATPase inhibitor N,N-dicyclohexyl carbodiimide (DCCD) (25 and 100 microM) inhibited accumulation of K+ by the cells but did not influence Na+ extrusion. Significant acidification of the medium did not induce a net current of Na+ from the cells through a Na+/H+ antiporter. The data indicate that the Na+/H+ antiporter of the plasma membrane of D. maritima is not responsible for Na+ extrusion from the cells. These results can be explained by the involvement of a primary electrogenic Na+ pump (a Na+-transporting ATPase) in Na+ transfer through the plasma membrane of this alga.
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PMID:Export of Na+ from cells of the halotolerant microalga Dunaliella maritima: Na+/H+ antiporter or primary Na+-pump? 1100 84


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