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)

Simultaneous assay of blood lead (Pb-B) and red cell lead (Pb-Rbc) in 123 samples from 104 urban and suburban students, ages 10-18, shows the ratio of concentration (Pb-Rbc)/(Pb-B) to increase as the hematocrit decreases. On direct assay in 40 samples, plasma lead (Pb-P) was fixed in a narrow range. In 28 students with Pb-Rbc >40 mug/100 ml, the mean red cell 2,3-diphosphoglycerate (2,3-DPG) was 6.05+/-0.28 (+/-S.E.), significantly higher (P<.025) than the 5.25+/-0.18 of 51 students with Pb-Rbc<40 mug/100 ml, although hemoglobin values were comparable (13.83+/-0.31 versus 13.55+/-0.20). Analysis of the individual population groups showed this correlation of Pb-Rbc with 2,3-DPG to be primarily related to the intercorrelation of each parameter with hemoglobin.Rbc membrane Na/K ATPase, as per cent of total membrane ATPase, had a median value of 60% in 48 subjects. Na/K ATPase below 60% was found in 10 (77%) of the 13 students with Pb-Rbc>/=40 mug/100 ml, but in only 14 of the 35 with Pb-Rbc<40 mug/100 ml (chi(2)=5.1, df=1, P<0.05). Correlation of significant enzyme changes with Pb-Rbc, but not with Pb-B in the normal urban range of Pb-B<35 mug/100 ml suggests Pb-Rbc, increased in anemia, to be a critical factor in the hematotoxicity of lead.
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PMID:Red cell lead, whole blood lead, and red cell enzymes. 436 46

Two dogs were diagnosed as malignant hyperthermia susceptible based on increased susceptibility (P less than 0.001) of biopsied muscle to caffeine-induced contracture. Erythrocytes from malignant hyperthermia and normal dogs were then examined for an antioxidant system deficiency. Values for serum muscle enzymes, reticulocytes and corpuscular hemoglobin were mildly elevated. Osmotic fragility was increased: hemolysis occurred at a NaCl concentration 10 mM higher than for normal dogs (P less than 0.001). A 35% glucose-6-phosphate dehydrogenase deficiency (P less than 0.001) with a 40% compensatory increase (P less than 0.01) in 6-phosphogluconate dehydrogenase activity was found. The membrane Ca2+-activated ATPase activity was abnormal: 100% increased with a 40% decreased Arrhenius activation energy (P less than 0.005) and increased thermostability. A 40% increased intracellular accumulation of total Ca2+ occurred in response to in vitro energy depletion in erythrocytes from one malignant hyperthermia dog (P less than 0.01). The multifactorial pattern of inheritance and the broad spectrum of malignant hyperthermia susceptibility are proposed to result from an antioxidant system deficit unmasking or aggravating an intrinsic muscle membrane anomaly. An individual from a family with a history of malignant hyperthermia or unexplained anesthetic death should be considered malignant hyperthermia susceptible if erythrocyte osmotic fragility is abnormal and there is a mild, unexplained elevation in serum creatine kinase.
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PMID:Canine malignant hyperthermia susceptibility: erythrocytic defects--osmotic fragility, glucose-6-phosphate dehydrogenase deficiency and abnormal Ca2+ homeostasis. 615 Jul 53

The rate constant for erythrocyte "total" sodium efflux was significantly decreased in patients with essential hypertension compared with normotensive controls due to a reduced "ouabain-sensitive" (active) sodium transport. The rate constants for "ouabain-insensitive", "ouabain-insensitive furosemide-sensitive" and "ouabain-insensitive furosemide-insensitive" sodium efflux were not different between hypertensives and normotensives. Ouabain inhibited sodium efflux by 74% and furosemide by a further 13%, both in hypertensives and in normotensives. The reduced rate constant for active erythrocyte transport in patients with essential hypertension was due to a diminished Na-K-ATPase activity demonstrable in hemolyzed and dialyzed erythrocytes. In contrast, in hemoglobin-free red blood cell membranes Na-K-ATPase activity was not different between both groups. Apparently the centrifugation procedure, which is necessary for preparation of hemoglobin-free membranes, leads to a loss of non-hemoglobin proteins, including ouabain-sensitive and ouabain-insensitive ATPase and/or a Na-K-ATPase inhibiting factor. Thus, the results obtained in hemolyzed and dialyzed red blood cells reflect probably better the conditions in the intact erythrocyte than do measurements on hemoglobin-free membranes, suggesting a decreased Na-K-ATPase activity in erythrocytes of essential hypertensives. However, the diminished rate constant for ouabain-sensitive sodium efflux did not result in a measurable increase in erythrocyte sodium indicating that this biochemical abnormality can fully be compensated in moderate essential hypertension without excess salt intake. The cause of the reduced rate constant for ouabain-sensitive sodium efflux is not clear. However, as suggested for sodium-potassium cotransport and for sodium-lithium countertransport it might be determined genetically.
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PMID:[ATPase activity and sodium transport in erythrocytes of patients with essential hypertension (author's transl)]. 621 10

The energy requirement for protein breakdown in Escherichia coli results from an ATP requirement for the function of protease La, the product of the lon gene. This novel serine protease contains an ATPase activity that is essential for proteolysis. ATP and protein hydrolysis show the same Km for ATP (30-40 muM) and are affected similarly by various inhibitors, activators, and ATP analogs. Vanadate inhibited ATP cleavage and caused a proportionate reduction in casein hydrolysis, and inhibitors of serine proteases reduced ATP cleavage. Thus, ATP and protein hydrolysis appear to be linked stoichiometrically. Furthermore, ATP hydrolysis is stimulated two- to threefold by polypeptides that are substrates for the protease (casein, glucagon) but not by nonhydrolyzed polypeptides (insulin, RNase). Unlike hemoglobin or native albumin, globin and denatured albumin stimulated ATP hydrolysis and were substrates for proteolysis. It is suggested that the stimulation of ATP hydrolysis by potential substrates triggers activation of the proteolytic function.
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PMID:Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion. 621 87

The components of the nitrogenase complex, MoFe-protein and FeMo-cofactor, possessing no ATPase or nitrogen-fixing activity, maintain the 18O-exchange at the level of 1 atom of 18O per molecule of Pi, which is inhibited by ATP. The Fe-protein complex does not catalyze the 18O-exchange. The nitrogenase components do not hydrolyze the substrates for phosphatase (p-nitrophenylphosphate, beta-glycerophosphate, glucose 1-phosphate and ribose 5-phosphate). The artificial albumin-containing MoFe- and Fe-proteins and the carboxyl group-containing proteins (albumin, hemoglobin, lysozyme) as well as sodium molibdate do not catalyze the 18O-exchange. It is assumed that the site of the ATPase center which is subjected to phosphorylation, is located on the MoFe-protein.
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PMID:[Localization of the ATPase site of nitrogenase by isotopic oxygen exchange [180]-Pi in equilibrium with H20]. 621 20

The mechanism by which cells reduce cytoplasmic vanadium(V) (vanadate) to vanadium(IV) was investigated using the human red cell as a model system. Vanadate uptake by red cells occurs with a rapid phase involving chemical equilibration across the plasma membrane and a slower phase resulting in a high concentration of bound vanadium(IV). The slow phase was inhibited in glucose-starved cells and restored upon addition of glucose indicating an energy requirement for this process. The time course of vanadium(IV) appearance (monitored by EPR spectroscopy of intact cells) paralleled the slow phase of uptake indicating that this phase involves vanadium reduction. The reduction of intracellular vanadate to vanadium(IV) was nearly quantitative after 23 h. The intracellular reduction is not enzymatic, since a similar time course of vanadium reduction and binding to hemoglobin was observed when glutathione was added to a hemoglobin + vanadate solution in vitro. Vanadium(IV) binding to hemoglobin was reduced by addition of ATP, 2,3-diphosphoglycerate or EDTA, probably through chelation of the cation. The stability constant of the ATP-vanadium (IV) complex was determined to be 150 M-1 at pH 4.9. The time course of red cell vanadate uptake and reduction was followed in the concentration range in which approximately 60% inhibition of the (Na+ + K+)-ATPase is observed. It is concluded that vanadate is reduced by cytoplasmic glutathione in this concentration range and that the reduction explains the resistance of the (Na+ + K+)-ATPase to vanadium in intact cells.
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PMID:Glutathione reduces cytoplasmic vanadate. Mechanism and physiological implications. 624 16

We have studied the effects of adriamycin (doxorubicin HCl) on human red blood cells. The peroxidizing effect of adriamycin on the thiols of red cell constituents resulted in decreased glutathione stability, and oxidation of hemoglobin and membrane protein components 1, 2, and 3, forming large molecular weight complexes. Membrane lipids were also peroxidized. Adriamycin itself did not inhibit the enzymes of the reductions system (glucose-6-phosphate dehydrogenase, 6-phosphogluconic dehydrogenase, glutathione reductase, glutathione peroxidase, catalase, superoxide dismutase) of the red cells. Because adriamycin has the potential of inhibiting ATPase, including both Na-K-dependent ATPase and ouabain insensitive ATPase, at concentrations not inhibitory to other enzymes, the net sodium content increased, and potassium content decreased after incubation of red cells with adriamycin at high concentrations. The experimental results described with adriamycin may serve as a model for the possible mechanism of cardiotoxicity observed in its clinical use, and also explain the potential hemolyzing effect on red cells. There was greater oxidizing effect on glucose-6-phosphate dehydrogenase (G-6-PD) deficient than on normal erythrocytes. It is suggested that adriamycin be used with caution in individuals with G-6-PD deficient red cells.
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PMID:The effects of adriamycin (doxorubicin HCl) on human red blood cells. 625 23

Membrane Na+,K+-adenosinetriphosphatase in erythrocytes from three groups of industrially exposed Pb workers (without toxicity, with toxicity associated with high blood Pb levels, and with toxicity associated with low blood Pb levels) was inversely correlated with Pb in the membrane fraction but not significantly correlated with total erythrocyte Pb. This difference was attributable to the proportion of erythrocyte Pb bound to hemoglobin and a Pb-binding protein of molecular weight 10,000.
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PMID:Erythrocyte lead-binding protein after occupational exposure. II. Influence on lead inhibition of membrane Na+,K+-adenosinetriphosphatase. 627 Mar 42

This study on erythrocytes in hemoglobin H (Hb H) disease reveals that unstable Hb H is bound to membranes to a greater extent, especially when it forms methemoglobin or is precipitated as inclusion body. The methemoglobin content of these erythrocytes is elevated in spite of a higher activity of NADH-methemoglobin reductase. The ATPase activity is doubled, and the ATP is presumably used for phosphorylation of membrane proteins, which leads to cross-linking of membrane proteins. This assumption could be supported by the observed decrease in non-electrolyte permeability, by increased binding of hemoglobin to the membrane and by polymerisation of membrane proteins detected by SDS-polyacrylamide gel electrophoresis. By means of electron microscopy, it could also be shown that the inclusion bodies are bound to the inner surface of membrane and cause its protrusion. This linkage might be responsible for the observed inhibition of the lateral movement of intramembrane particles.
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PMID:Erythrocyte alterations in hemoglobin H disease. 627 17

An increase in pH decreases the Na+ concentration (Na+ +K+ = 150 mM) necessary for half-maximum activation of the (Na+ +K+)-ATPase at non-saturating concentrations of ATP just as an increase in the concentration of ATP at a given pH. It also decreases the concentration of Na+ necessary for transformation from the K+-form to the Na+-form at equilibrium conditions (Na+ +K+ = 150 mM). An increase in pH increases the rate of the transformation from the K+-form to the Na+-form of the system and decreases the rate of the reverse reaction. The pH effect on the conformation suggests that the K+-form is a protonated form and the Na+-form a deprotonated one. The similarity between the effect of an increase in pH with non-saturating concentrations of ATP and that of an increase in ATP at a given pH suggests that ATP exerts its effect on the transformation from the K+ - to the Na+-form by a decrease in pK values of the system, i.e., by releasing protons, a Bohr effect. Enzyme modified by reaction with pyridoxal 5-phosphate terminated by NaBH4 behaves at a given pH as if it were non-modified enzyme but at a higher pH. The 'pH effect' is seen after modification by pyridoxal 5-phosphate in the presence of ATP, of Na+ without and with ATP, of K+ with ATP but not in the presence of K+ alone. The modification has also a 'pH effect' on the rate of the transformation from the K+ -form to the Na+ -form and on the reverse reaction. There are at least two different pyridoxal 5-phosphate-reactive groups (amino groups), one which can be protected by ATP and which is of importance for activity and another which is not protected by ATP and which is of importance for the pH effect on the conformation. The effect of a protonation-deprotonation of amino groups on the conformation is explained by an involvement of the amino groups in salt bridge formation in between and inside the polypeptide chains, a hemoglobin-like situation. The protonated K+ -form is then a tense T-structure with a high K+, low Na+ affinity and the deprotonated Na+ -form a relaxed, R-structure with high Na+, low K+ affinity. ATP facilitates deprotonation by decreasing pK values. Oligomycin has 'pH effect' on the K0.5 for Na+ under equilibrium and steady-state conditions, but oligomycin has no effect on the rate of the transformation from the K+ -form to the Na+ -form, but gives a pronounced decrease of the rate of the reverse reaction, indicating that oligomycin does not react with the K+ -form but with the Na+ -form of the system and prevents the protonation, the E1 to E2 transformation.
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PMID:The effect of pH, of ATP and of modification with pyridoxal 5-phosphate on the conformational transition between the Na+-form and the K+-form of the (Na+ +K+)-ATPase. 628 65


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