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)

Enzymatic properties of a canine cardiac muscle microsomal fraction were determined to localize in situ a "basic," divalent cation dependent adenosine triphosphatase (ATPase) by ultrastructural cytochemistry. The microsomal fraction had a buoyant density of 1.08--1.13 (20--30% [w/w] sucrose) and hydrolyzed adenosine triphosphate in the presence of Mg2+, Ca2+, Mn2+, or Co2+, but not in that of Sr2+ or Ni2+, under conditions that inhibited interfering (Na+ + K+)-ATPase and sarcoplasmic reticulum Ca2+-ATPase activities. "Basic" ATPase was localized in paraformaldehyde-fixed tissue in a medium containing Mg2+ or a high Ca2+ concentration (4 mM). A free Pb2+ concentration of less than 1 microM was used to capture enzymatically released phosphate anions. Electron-dense lead precipitates were present at the plasmalemma, T-system, and intercalated disc membranes with the exception of the nexus. These studies suggest that "basic" ATPase activity is associated with surface membrane structures of canine cardiac muscle.
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PMID:Cytochemical localization of a "basic" ATPase to canine myocardial surface membrane. 645 53

The ATPase activity of purified coupling factor 1 (CF1) of spinach chloroplasts [EC 3.6.1.3] was reversibly enhanced in some aqueous organic solvents, notably methanol, ethanol, and acetone. Pretreatment of CF1 with 20% (v/v) methanol did not affect the subsequent activity. The activity depended entirely on the final concentration of methanol in the reaction mixture. In the presence of 20% methanol, the Km of Ca2+-ATPase from ATP was lowered from 0.4 mM to 0.2 mM. Not only Ca2+, but also Cd2+, Mg2+, Mn2+, and Zn2+ supported the ATPase activity at rates of higher than 7 mumol.mg protein-1 . min-1. Co2+, Ni2+, and Pb2+ supported the activity at rates of 0.5-1.0 mumol.mg protein-1 . min-1. The activities supported by the following cations, if any, were less than 0.2 mumol.mg protein-1 . min-1; Ba2+, Cu2+, Fe2+, Hg2+, Sn2+, and Sr2+. The optimum concentration of methanol for Ca2+-ATPase and Mg2+-ATPase activities was about 30% (v/v). The optimum pH values for Ca2+-ATPase and Mg2+-ATPase activities were about 8.0 and 8.8, respectively. The enhancing effect of organic solvents appears to be associated with their relative lipophilic character as defined by the octanol-water partition coefficient. The Ca2+-ATPase activities of th trypsin-activated and the heat-activated CF1 were inhibited and their Mg2+-ATPase activities were enhanced by the presence of methanol in the reaction mixture.
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PMID:Enhancement of adenosine triphosphatase activity of purified chloroplast coupling factor 1 in aqueous organic solvent. 645 34

We describe a new technique for immunohistochemical and enzyme-histochemical double staining using confocal laser scanning microscopy in the reflection mode. As an example, we investigated the immunoreactivity for Spot 35-calbindin-D28K, a vitamin D-dependent calcium binding protein, and the enzyme activity for Ca(2+)-ATPase in the rat kidney. The lead precipitation method for Ca(2+)-ATPase was initially used to process kidney slices. Each specimen was then dehydrated and embedded in a water soluble resin. Thin sections were cut from the resin block, and an indirect immunocolloidal gold method with silver enhancement for Spot 35-calbindin-D28K antigen was carried out on the glass slides. Results were then observed by confocal laser scanning microscopy in the reflection mode. The three-dimensional distribution of the reaction products was detected by serial optic slice images. Lead phosphate particles, which represented the location of Ca(2+)-ATPase, were distributed deep in the section. The most intense signals from the silver particles were detected from the surface slice of the section. A stereoscopic image generated from the serial optic slices clearly showed the differences in their distribution.
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PMID:A new histochemical double-stain method using three-dimensional analysis with confocal laser scanning microscopy. 753 68

Lead, zinc and copper were administered i.p singly or in combination as acetate salts to rats for 14 consecutive days. It was observed that lead induced drastic changes, copper induced moderate changes but zinc did not cause any significant change in the cholesterol and phospholipid content, hexose, hexosamine and sialic acid levels and activities of the erythrocyte membrane enzymes--acetylcholinesterase (AChE), NADH dehydrogenase and Na(+)-K+ ATPase. In the combined metal treatment the presence of zinc considerably reduced the changes induced by lead and copper.
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PMID:Metal induced changes in the erythrocyte membrane of rats. 761 77

The different effects of lead exposure in young children and adults, and inconsistencies between in vivo and in vitro studies as well as between experimental and clinical data suggest that lead toxicity may have different mechanisms. During the developmental phase, lead neurotoxicity results in permanent dysfunction, but its neuropharmacological toxicity as seen in adults might involve its interaction with micronutrients such as calcium and zinc. Lead administered orally in a dose of 20 mg/kg for 8 weeks was found to inhibit the enzyme activity of succinic dehydrogenase, acetylcholine esterase and Na+/K+ ATPase both in the cerebrum and in the cerebellum. Selenium also affected these enzymes when administered in a dose of 0.5 ppm for 8 weeks. When lead and selenium were administered simultaneously the inhibition of the three enzyme activities was considerably alleviated. However, when selenium (0.5 ppm) was given only for 15 days after exposure to lead, the activity of the enzymes was much reduced when compared with control.
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PMID:Effect of selenium on lead-induced neurotoxicity in different brain regions of adult rats. 765 36

Exposure of rainbow trout to lead chloride (PbCl2, 1 ppm) in fresh water killed all animals within 16 days. Exposure to this lethal dose for 6 days only showed a significant increase in the haematocrit. Calcium, sodium and chloride concentrations in plasma were not notably modified. Both the influx and the net flux of sodium fluctuated much less than the diffusional water fluxes through secondary lamellae in gills. Branchial Na,K-ATPase, Ca-ATPase and HCO3-ATPase activities were not sensitive to lead toxicity. Lead caused a cellular 'wave-shaped' degeneration and renewal with modification in the number and morphology of chloride cells. Results are discussed in relation to the hydromineral balance of the trout.
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PMID:Effects of lead loads on branchial osmoregulatory mechanisms in the rainbow trout Oncorhynchus mykiss. 782 83

Bacterial plasmids contain specific genes for resistances to toxic heavy metal ions including Ag+, AsO2-, AsO4(3-), Cd2+, Co2+, CrO4(2-), Cu2+, Hg2+, Ni2+, Pb2+, Sb3+, and Zn2+. Recent progress with plasmid copper-resistance systems in Escherichia coli and Pseudomonas syringae show a system of four gene products, an inner membrane protein (PcoD), an outer membrane protein (PcoB), and two periplasmic Cu(2+)-binding proteins (PcoA and PcoC). Synthesis of this system is governed by two regulatory proteins (the membrane sensor PcoS and the soluble responder PcoR, probably a DNA-binding protein), homologous to other bacterial two-component regulatory systems. Chromosomally encoded Cu2+ P-type ATPases have recently been recognized in Enterococcus hirae and these are closely homologous to the bacterial cadmium efflux ATPase and the human copper-deficiency disease Menkes gene product. The Cd(2+)-efflux ATPase of gram-positive bacteria is a large P-type ATPase, homologous to the muscle Ca2+ ATPase and the Na+/K+ ATPases of animals. The arsenic-resistance system of gram-negative bacteria functions as an oxyanion efflux ATPase for arsenite and presumably antimonite. However, the structure of the arsenic ATPase is fundamentally different from that of P-type ATPases. The absence of the arsA gene (for the ATPase subunit) in gram-positive bacteria raises questions of energy-coupling for arsenite efflux. The ArsC protein product of the arsenic-resistance operons of both gram-positive and gram-negative bacteria is an intracellular enzyme that reduces arsenate [As(V)] to arsenite [As(III)], the substrate for the transport pump. Newly studied cation efflux systems for Cd2+, Zn2+, and Co2+ (Czc) or Co2+ and Ni2+ resistance (Cnr) lack ATPase motifs in their predicted polypeptide sequences. Therefore, not all plasmid-resistance systems that function through toxic ion efflux are ATPases. The first well-defined bacterial metallothionein was found in the cyanobacterium Synechococcus. Bacterial metallothionein is encoded by the smtA gene and contains 56 amino acids, including nine cysteine residues (fewer than animal metallothioneins). The synthesis of Synechococcus metallothionein is regulated by a repressor protein, the product of the adjacent but separately transcribed smtB gene. Regulation of metallothionein synthesis occurs at different levels; quickly by derepression of repressor activity, or over a longer time by deletion of the repressor gene at fixed positions and by amplification of the metallothionein DNA region leading to multiple copies of the gene.
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PMID:Newer systems for bacterial resistances to toxic heavy metals. 784 81

1. Heavy metals (Hg2+, Cu2+, Cd2+, Zn2+, Pb2+) at micromolar concentrations strongly inhibit the Ca(2+)-ATPase activity present in the plasma-membrane obtained from the gill cells of Mytilus galloprovincialis Lam. Heavy metals act through inhibition of the formation of the phosphorylated intermediate. 2. All the heavy metals tested inhibit the Ca(2+)-ATPase activity, the effect following the order: Hg2+ > Pb2+ > Cu2+ > Cd2+ > Zn2+; the simultaneous addition of different heavy metals causes a summatory inhibition of the enzyme activity; addition to the reaction mixture of GSH at a final concentration of 0.5 mM, reverses inhibitory effects of heavy metals. 3. The inhibitory effects of Cu2+ on Ca(2+)-ATPase are highly enhanced by addition of ascorbate to the reaction mixture. In the presence of ascorbate (100 microM), copper strongly stimulates the lipid peroxidation damage of the gill plasma-membranes, a result that may explain the high copper cytotoxicity.
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PMID:Effects of heavy metals on the Ca(2+)-ATPase activity present in gill cell plasma-membrane of mussels (Mytilus galloprovincialis Lam.). 790 5

The effects of lead on Ca2+ homeostasis in nerve terminals was studied. Incubation with lead in vitro stimulated the activity of calmodulin and the maximum effect was observed at 30 microM lead, higher concentrations had an inhibitory effect. In vivo exposure to lead increased the activity of calmodulin by 45%. Lead had an inhibitory effect on Ca2+ ATPase activity in both calmodulin-rich and calmodulin-depleted synaptic plasma membranes, the IC50 values for inhibition being 13.34 and 16.69 microM respectively. Exogenous addition of calmodulin (5 micrograms) and glutathione (1 mM) to calmodulin rich synaptic plasma membranes reversed the inhibition by IC50 concentration of lead. In vivo exposure of lead also significantly reduced the Ca2+ ATPase activity, resulting in an increase in intrasynaptosomal calcium. Concomitant with the increase in intrasynaptosomal calcium, lipid peroxidation values also increased significantly in lead-treated animals. In addition lead also had an inhibitory effect on depolarization induced Ca2+ uptake and the inhibition was found to be a competitive one. The results suggest that lead exerts its toxic effects by modifications of the intracellular calcium messenger system which would have serious consequences on neuronal functioning.
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PMID:Alterations in calcium homeostasis on lead exposure in rat synaptosomes. 804 62

Inhibition of Na+/K+-ATPase and Mg2+-ATPase activities by in vitro exposure to Cd2+, Pb2+ and Mn2+ was investigated in rat brain synaptic plasma membranes (SPMs). Cd2+ and Pb2+ produced a larger maximal inhibition of Na+/K+-ATPase than of Mg2+-ATPase activity. Metal concentrations causing 50% inhibition of Na+/K+-ATPase activity (IC50 values) were Cd2+ (0.6 microM) < Pb2+ (2.1 microM) < Mn2+ (approximately 3 mM), and the former two metals were substantially more potent in inhibiting SPM versus synaptosomal Na+/K+-ATPase. Dixon plots of SPM data indicated that equilibrium binding of metals occurs at sites causing enzyme inhibition. In addition, IC50 values for SPM K+-dependent p-nitrophenylphosphatase inhibition followed the same order and were Cd2+ (0.4 microM) < Pb2+ (1.2 microM) < Mn2+ (300 microM). Simultaneous exposure to the combinations Cd2+/Mn2+ or Pb2+/Mn2+ inhibited SPM Na+/K+-ATPase activity synergistically (i.e., greater than the sum of the metal-induced inhibitions assayed separately), while Cd2+/Pb2+ caused additive inhibition. Simultaneous exposure to Cd2+/Pb2+ antagonistically inhibited Mg2+-ATPase activity while Cd2+/Mn2+ or Pb2+/Mn2+ additively inhibited Mg2+-ATPase activity at low Mn2+ concentrations, but inhibited antagonistically at higher concentrations. The similar IC50 values for Cd2+ and Pb2+ versus Mn2+ inhibition of Na+/K+-ATPase and the pattern of inhibition/activation upon exposure to two metals simultaneously support similar modes of interaction of Cd2+ and Pb2+ with this enzyme, in agreement with their chemical reactivities.
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PMID:Inhibition of ATPase activity in rat synaptic plasma membranes by simultaneous exposure to metals. 859 55


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