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)

The aim of this study was to investigate whether in vitro cholesterol enrichment of human erythrocytes affects transmembrane cation transport systems by changes induced in the membrane microviscosity of these cells. Human erythrocytes in suspension were incubated with cholesterol-lecithin dispersions to obtain an enrichment of their membrane cholesterol. The ouabain-sensitive Na+ efflux, the Na+, Li+(-)countertransport activity, the Na+, K+(-)cotransport activity, the basal transmembrane leakage of Na+ and K+, and the enzymatic activity of ATPases were determined in these cholesterol-rich cells and compared with control cells. Membrane core and surface microviscosity was also measured in the control and cholesterol-enriched cells, using the fluorescent probes, 1,6-diphenyl-1,3,5-hexatriene (DPH) and trimethylammonium (TMA)-DPH, respectively. The cholesterol content of the erythrocytes incubated in the presence of cholesterol-rich dispersions increased gradually over time. A 47% increase membrane cholesterol content was obtained after 16 h of incubation, while no change in the erythrocyte phospholipid content was found. High membrane cholesterol in the human erythrocyte phospholipid content was found. High membrane cholesterol in the human erythrocyte, obtained by in vitro enrichment of the cells with cholesterol-lecithin dispersion, inhibited in intact cell suspensions the ouabain-sensitive Na+ efflux, an estimate of the Na+(-)pump activity, and in isolated erythrocyte membranes the enzymatic activity of Na+, K+(-)ATPase, and Mg2+(-)ATPase. The dissociation constant for internal sodium and the maximal rate of ouabain-sensitive Na+ efflux is decreased in cholesterol-rich erythrocytes compared to control cells. The elevated erythrocyte membrane cholesterol content was also accompanied by a decrease in the Na+,K+(-)cotransport activity, the Na+, Li+(-)countertransport activity, and the transmembrane basal leakage of Na+ and K+. Microviscosity, measured in the erythrocyte membrane core with the fluorescence probe DPH, was increased in the cholesterol-rich cells compared to the control cells. However, the membrane surface microviscosity, measured with the probe TMA-DPH, was not different between the control cell and the cholesterol-rich cells. The present data show that enrichment of the human erythrocyte membrane with cholesterol results in an increase of membrane core microviscosity, resulting in an inhibition of transmembrane cation transport systems in erythrocytes in suspensions and of erythrocyte membrane Na+,K+(-)ATPase, Ca2+(-)ATPase, and Mg2+(-)ATPase.
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PMID:Cholesterol modulation of transmembrane cation transport systems in human erythrocytes. 859 38

The in vivo anesthetic activity of monoketones in mice was examined in relation to their hydrophobicity and to the in vivo effects on Na+/K+ -adenosine triphosphatase (Na+/K+ -ATPase) activity and membrane fluidity. Anesthetic potency (AD50) of monoketones was determined; AD50 implys the dose required to anesthetize 50% of the animals from the treated group. The n-octanol/water partition coefficient (P) was used as an index of hydrophobicity. Membrane fluidity was determined by using 1,6-diphenyl-1,3,5-hexatriene (DPH) or 1-(4-trimethylammoniumphenyl)-6-phenyl-1,3,5-hexatriene (TMA-DPH as fluorescence probes. Log (1/AD50) was the parabolic function of log P, log ((1/AD50) = -0.167(log P)2 + 0.698 log P - 1.365, and the log P that corresponds to the minimum AD50 was estimated to be 2.09. Brain synaptosomes were prepared from mice that were considered anesthetized with each of the 4 monoketones (1.5-fold AD50), methyl n-propyl, methyl n-amyl, methyl 3-methylhexyl and methyl n-octyl ketone. The Na+/K+ -ATPase activity was inhibited by methyl n-propyl ketone alone, membrane DPH fluidity was decreased by each of the 4 monoketones, and membrane TMA-DPH fluidity was decreased by methyl n-propylketone alone. These results suggest an involvement of the decreased DPH fluidity in monoketone-induced anesthesia.
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PMID:Anesthetic activity of monoketones in mice: relationship to hydrophobicity and in vivo effects on Na+/K+ -ATPase activity and membrane fluidity. 861 59

Free radical-induced physiopathologies are generally thought to be mediated by membrane injuries. Using a pro-oxidant model induced by dietary magnesium deficiency, we have recently shown that skeletal muscle lesions occurred with a rise in the calcium level and enhanced free radical production. In this study, we investigated the physicochemical and biochemical properties of sarcoplasmic reticulum membranes isolated from hind limb muscles of weanling male rats pair fed magnesium-deficient or control diets for 12 d. The calcium-induced calcium efflux from preloaded vesicles was increased in membranes isolated from Mg-deficient rat muscle. In agreement with this latter observation, we demonstrated increased ryanodine binding affinity of the calcium channel. The Ca2(+)-ATPase activity of the pump was shown to be reduced. The viscosity state of the membranes, assessed by 1,6-diphenyl-1,3,5-hexatriene fluorescence anisotropy, was significantly increased in Mg-deficient membranes. Moreover, these membranes demonstrated an increased content of protein carbonyls as compared with controls. These functional as well as structural changes are closed to those described in sarcoplasmic reticulum membranes oxidatively modified in vitro. Together, these data fitted well with the concept that free radical-induced membrane damages resulting in calcium overload may be at the origin of skeletal muscle lesion during Mg-deficiency.
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PMID:Functional alterations in sarcoplasmic reticulum membranes of magnesium-deficient rat skeletal muscle as consequences of free radical-mediated process. 872 13

Decanoic acid, a lipophilic agent, inhibited in vitro the plasma membrane H(+)-ATPase of Saccharomyces cerevisiae grown in YPD medium. Conversely, when decanoic acid (35 microM) was present in the growth medium, the measured H(+)-ATPase activity was four times higher than that of control cells. Km, and pH and orthovanadate sensitivity were the same for the two growth conditions, which indicated that H(+)-ATPase activation was not due to conformational changes in the enzyme. The activation process was not entirely reversible which showed that plasma membrane H(+)-ATPase activation is due to several mechanisms. 1,6-diphenyl-1,3,5-hexatriene anisotropy performed on protoplasts from cells grown in YPD revealed that as decanoic acid concentration was increased, anisotropy significantly decreased, i.e. membrance fluidity increased. Cells grown in media containing decanoic acid exhibited greater membrane fluidity compared with control cells. Furthermore, these cells did not show any fluidifying effect when increased concentrations of decanoic acid were added. Chemical analysis of cell membrane lipid composition revealed a modification in the distribution of the phospholipid fatty acids and sterols in cells grown in the presence of 35 microM decanoic acid compared with control cells. Our results support the view that the plasma membrane H(+)-ATPase activation induced by decanoic acid is correlated with an alteration in membrane lipid constituents.
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PMID:Alteration in membrane fluidity and lipid composition, and modulation of H(+)-ATPase activity in Saccharomyces cerevisiae caused by decanoic acid. 886 21

In the present study we demonstrated that human erythrocytes under normal conditions release small amounts of peroxynitrite (ONOO-) that can be considerably increased by the tumour promoter t-butylhydroperoxide (t-BHP), with a subsequent increase in lipid peroxidation and inhibition of Ca2+ pump ATPase activity. By causing oxidative stress in human erythrocytes with t-BHP, ONOO- release was increased approximately ten fold. N-monomethyl-L-arginine (L-NMMA) inhibited ONOO- release by approximately 90% while D-NMMA had no effect. The interaction of t-BHP with hemoglobin (Hb) and methemoglobin (MetHb) caused the production of superoxide (O2-) and hydrogen peroxide (H2O2). The differential direct effect of t-BHP on Hb and MetHb was investigated by taking their spectra in the presence or absence of cytochrome C. Erythrocyte membranes treated either with t-BHP or with ONOO- were subjected to oxidative stress with a subsequent increase in malondialdehyde (MDA) production and decrease in membrane fluidity, as estimated by the fluorescence polarization of 1,6,diphenyl-1,3,5-hexatriene (DPH). Ca2+ pump ATPase activity was decreased in t-BHP and/or ONOO-(-)treated erythrocytes, indicating that the subsequent intracellular calcium increase promoted ONOO- production by activating the Ca(2+)-calmodulin-dependent NO-synthase activity. These results suggest that hemoglobin oxidation by the tumour promoters play a key role in oxidative damage to erythrocytes and that the t-BHP/ Hb redox system could be a useful tool for investigating the tumour promoting efficacy of organic hydroperoxides.
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PMID:Tumour promoter tert-butyl-hydroperoxide induces peroxynitrite formation in human erythrocytes. 891 15

The purpose of the present study is to analyze membrane fluidity, enzyme, phospholipid and fatty acid composition and cholesterol content in the brush border (BBM) and basolateral (BLM) membranes obtained from the renal cortex of normal dogs. All measurements were carried out in samples from the same kidney in order to correlate membrane fluidity with membrane composition. BBM and BLM were obtained separately by MgCl precipitation and gradient centrifugation. The order parameter of membrane fluidity was measured by 1,6-dimethyl-1,3,5-hexatriene (DPH) and 1-trimethylammoniophenyl-DPH. (TMA-DPH) steady-state polarization fluorescence. Total lipids, phospholipids and phospholipid classes, cholesterol content, and fatty acid classes were also measured. Data from BLM enzymatic activity revealed an 11-fold enrichment in Na,K-ATPase, whereas the enrichment factors for the other enzymatic markers were well below the unit, demonstrating the high purity of the preparation obtained. Similarly, BBM showed a 9 times increase in alkaline phosphatase and gamma-glutamyltranspeptidase enrichment, and values of enrichment factors for the other enzymatic markers of about 1. BBM exhibited a higher value of steady-state fluorescence anisotropy and thus a lower fluidity than BLM using either of the fluorescent probes DPH or TMA-DPH. This lower fluidity in both the central hydrophobic zone, and the fluorescent probes DPH or TMA-DPH. This lower fluidity in both the central hydrophobic zone, and the external, more hydrophilic leaflet of BBM in comparison with BLM was consistent with the findings of: (a) a higher cholesterol/protein ratio; (b) a lower phospholipid protein ratio; (c) a higher sphingomyelin/choline glycerophospholipid ratio, and (d) a lower unsaturation degree of the fatty acids.
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PMID:Biochemical and functional characterization of renal cortical brush border and basolateral membranes in dogs. 895 34

1. Na+,K(+)-ATPase is the membrane enzyme catalysing the active transport of Na+ and K+ across the plasma membrane of animal cells. A reduced activity of Na+,K(+)-ATPase has been described in gestational hypertension in a variety of cell types, in agreement with the hypothesis that gestational hypertension can induce membrane transport modifications similar to those reported for essential hypertension. The causes of the reduced Na+,K(+)-ATPase activity are still debated. 2. The aim of the present work was to investigate the molecular mechanism of the reduced enzymic activity in gestational hypertension using as a model Na+,K(+)-ATPase purified from human placenta. Na+,K(+)-ATPase obtained from term placentas of eight healthy pregnant women and eight age-matched women with gestational hypertension was purified as previously described. 3. We observed in gestational hypertension: (i) a significant increase in the activation energies above transition temperature; (ii) a significant decrease in the fluorescence polarization of 1-(4-trimethylaminophenyl)-6-phenyl-1,3,5-hexatriene (i.e. increased fluidity) and an increase in the mean lifetime (modified hydrophobicity); (iii) a lower Kq, suggesting an enzymic structural modification; and (iv) an increased mean lifetime and rotational relaxation time of pyrene isothiocyanate, indicating a modified ATP binding site.
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PMID:Na+,K(+)-ATPase of human placenta during gestational hypertension: a biochemical-biophysical study. 897 7

Photodynamic action of merocyanine 540 (MC540) on the plasma membrane of human glioblastoma(U-87MG) cells has been investigated. Plasma membrane was labeled with lipid specific probe 1,(4-trimethylammonium),6-diphenyl-1,3,5-hexatriene. Steady-state anisotropy, decay time and time-dependent anisotropy of TMA-DPH in U-87MG cells have been measured as a function of light dose. A decrease in the steady-state anisotropy and decay time of TMA-DPH in MC540-treated cells was observed upon light irradiation. The time-dependent anisotropy measurements showed a decrease in the limiting anisotropy (r infinity) and an increase in the rotational relaxation time (phi) of the probe upon photosensitization of cells. Analysis of these data using wobbling in cone model for probe rotation in the membrane indicated an increase in the cone angle (theta c) and a decrease in the order parameter (S). Protein specific probe N-(1-pyrene)-maleimide was used to study the effect of photosensitization on the plasma membrane proteins. An increase in the rotational relaxation time and a decrease in the ratio of excimer to monomer fluorescence intensity of PM was observed on photosensitization. Photodynamic action of MC540 also caused an inhibition of protein SH groups and Na(+)-K(+)-ATPase activity of plasma membrane. Our results demonstrate that the photodynamic action of MC540 decreases the order of the lipid bilayer and reduces the mobility of the proteins in the plasma membrane of cells.
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PMID:Alterations in plasma membrane of glioblastoma cells by photodynamic action of merocyanine 540. 904 49

The effect of oxidative stress, induced by Fe(2+)-EDTA system, on Na+,K(+)-ATPase, Na+/CA2+ exchanger and membrane fluidity of synaptosomes was investigated. Synaptosomes isolated from gerbil whole forebrain were incubated in the presence of 200 microM FeSO4-EDTA per mg of protein at 37 degrees C for 30 min. The oxidative insult reduced Na+,K(+)-ATPase activity by 50.7 +/- 5.0% and Na+/Ca2+ exchanger activity measured in potassium and choline media by 47.1 +/- 7.2% and 46.7 +/- 8.6%, respectively. Membrane fluidity was also significantly reduced as observed with the 1,6-diphenyl-1,3,5-hexatriene probe. Stobadine, a pyridoindole derivative, prevented the decrease in membrane fluidity and in Na+/Ca2+ exchanger activity. The Na+,K(+)-ATPase activity was only partially protected by this lipid antioxidant, indicating a more complex mechanism of inhibition of this protein. The results of the present study suggest that the Na+/Ca2+ exchanger and the Na+,K(+)-ATPase are involved in oxidation stress-mediated disturbances of intracellular ion homeostasis and may contribute to cell injury.
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PMID:Iron-induced inhibition of Na+, K(+)-ATPase and Na+/Ca2+ exchanger in synaptosomes: protection by the pyridoindole stobadine. 935 20

The causes of the reduced activity of Na+/K+-adenosine triphosphatase (ATPase) in human diabetes are still the object of controversy. The aim of this work was to investigate the mechanisms of inhibition by means of the study of the Na+/K+-ATPase purified from human placenta. We purified Na+/K+-ATPase from term placentas of six healthy women and six age-matched women with insulin-dependent diabetes mellitus (IDDM) in good metabolic control. The enzymatic activity was reduced in both the microsomal fraction and the purified Na+/K+-ATPase obtained from diabetic women, whereas no difference was found in the number of active molecules determined by anthroyl ouabain binding. The Na+/K+-ATPase purified from women with IDDM did not show any modification in the ouabain affinity or changes in the physicochemical structure of the ouabain binding site investigated by dynamic fluorescence or alterations in lateral diffusion. The activation energy of the enzyme was increased, whereas the tryptophan accessibility of the enzyme was lower in women with IDDM. The fluidity of the lipid anulus of the enzyme was higher in women with IDDM than in control women, as suggested by fluorescence polarization of 1-(4-trimethylaminophenyl)-6-phenyl-1,3,5-hexatriene. The adenosine triphosphate-binding site, investigated by anisotropy decay studies of the fluorescent probe pyrene isothiocyanate, was modified in women with IDDM. It appears that the Na+/K+-ATPase of human placenta is altered in its disposition in IDDM.
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PMID:Modifications induced by insulin-dependent diabetes mellitus on human placental Na+/K+-adenosine triphosphatase. 935 71


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