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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 649 (1981), S. 481-486 
    ISSN: 0005-2736
    Keywords: (Erythrocyte) ; Hemolysis ; K^+loss ; Palytoxin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 688 (1982), S. 486-494 
    ISSN: 0005-2736
    Keywords: (Erythrocyte) ; Amphotericin B ; Palytoxin ; Permeability
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 861 (1986), S. 165-176 
    ISSN: 0005-2736
    Keywords: (Erythrocyte membrane) ; (Na^+ + K^+)-ATPase ; Ligand binding ; Membrane permeability ; Ouabain ; Palytoxin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 319 (1982), S. 101-107 
    ISSN: 1432-1912
    Keywords: Palytoxin ; Ouabain ; Erythrocytes ; Permeability ; ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. Palytoxin in concentrations as low as 1 pM raises the potassium permeability of rat, human and sheep erythrocytes, and the sodium permeability of human erythrocytes. The release of potassium or sodium from human cells also occurs when extracellular sodium is replaced by choline. 2. Ouabain inhibits the release due to palytoxin of potassium ions from human, sheep and rat erythrocytes, and also the release of sodium ions from human cells. The glycoside effect is specific since a) it is already prominent with 5×10−8 M ouabain b) rat erythrocytes are less sensitive than human cells to ouabain c) potassium release due to amphotericin B or the Ca2+ ionophore A23187 is not influenced by ouabain and d) dog erythrocytes are resistant to palytoxin as well as to ouabain. 3. Palytoxin has no direct influence on the Na+, K+-ATPase. It inhibits the binding of [3H]ouabain to erythrocyte membranes within the same concentration range as unlabelled ouabain. It partially displaces bound [3H]ouabain, and partially inhibits the inactivation of erythrocyte ATPase by the glycoside. Depletion of ATP or of external Ca2+ renders the cells less sensitive to palytoxin. Nevertheless inhibition by ouabain can be still demonstrated with human cells whose ATP stores had been largely exhausted, and also in the absence of external Ca2+. 4. Palytoxin decreases the surface tension at the air-water interface. We assume that the formation of nonspecific pores by palytoxin is linked with its surface activity. Further experiments should demonstrate whether ouabain prevents the binding of palytoxin to erythrocytes (“receptor hypothesis”), or whether an ouabain-sensitive hydrolysis of trace amounts of ATP (“metabolic hypothesis”) promotes the palytoxin effect.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 323 (1983), S. 269-275 
    ISSN: 1432-1912
    Keywords: Palytoxin ; Tetraphenylphosphonium ; Depolarization ; Binding ; Borate ; Calcium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Palytoxin in concentrations as low as 10−11 to 10−12 M promotes the outflow of the lipophilic [3H]-tetraphenylphosphonium ion from particulate brain cortex of guinea-pigs and rats, and from preloaded crude synaptosomes of rats, which indicates depolarization. The outflow is not influenced by tetrodotoxin or the calcium channel blocker nimodipin, or by substitution of choline for Na+ ions. It is increased by Ca2+ and by borate, the latter interacting with the toxin itself. To assess the fixation of palytoxin to biological membranes, a binding step was installed before the depolarization step. Palytoxin binds to membranes from rat brain, liver, kidney, human and dog erythrocytes, and to a lesser degree to liposomes made from rat brain or erythrocyte lipids. Binding is reversible. It is decreased by mild physical pretreatments of crude synaptosomes. Palytoxin binding is increased in the presence of micromolar concentrations of Ca2+ or borate. It is concluded that the potentiation of palytoxin actions by Ca2+ or borate is at least partially due to the promotion of its binding.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 323 (1983), S. 261-268 
    ISSN: 1432-1912
    Keywords: Palytoxin ; Erythrocyte ; Membrane ; Na+, K+-ATPase ; Calcium ; Ouabain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Palytoxin increases the permeability of human erythrocytes and their resealed ghosts. To elucidate its mode of action the activation by ATP and Ca2+, the inhibition by ouabain, and the changes in permselectivity have been studied: 1. Depletion of cells from ATP considerably depresses their sensitivity towards palytoxin. Ouabain prevents the actions of the toxin, however, with different inhibition characteristics in normal and depleted cells. The concentration of palytoxin required to raise the K+ permeability is higher in ghosts than in erythrocytes. The sensitivity is restored by incorporating ATP which can be partially substituted by ADP and GTP but not by AMP, Pi, β-γ-methylene adenosine 5′-triphosphate or the chromium (III) complex of ATP. Ouabain inhibits the K+ release from resealed ghosts in the presence as well as absence of ATP. Ouabain also inhibits the palytoxin-triggered Na+ and choline efflux into Na+ medium, as well as the Na+, K+ and choline efflux into choline medium. Phosphate promotes the inhibitory action of ouabain. Incorporated vanadate or Mg2+ do not change the sensitivity of ghosts toward palytoxin. 2. External calcium down to 10 μM potentiates the action of palytoxin in ghosts resealed with or without ATP. In contrast to calcium ionophore A23187, palytoxin does not raise the influx of Ca2+. 3. Palytoxin triggers the formation of small pores in resealed ghosts. The efflux into Na+ medium decreases in the order K+≧Na+〉[3H]choline≫[14C]inositol〉[14C]sucrose, [3H]inulin≅0. Our data suggest that palytoxin, once bound to erythrocyte membranes, transforms the sodium pump, or its functional vicinity, into a pore allowing the passive transport of small ions. This process is assisted by ATP from inside whereas Ca2+ promotes from the outside the efficacy of palytoxin.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 325 (1984), S. 85-87 
    ISSN: 1432-1912
    Keywords: Na+, K+-ATPase ; Palytoxin ; Ouabain ; Kidney ; Erythrocyte
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Hog kidney Na+, K+-ATPase, purified to the microsomal stage and activated with detergent, binds palytoxin, as shown by the nearly complete competition of the toxin with 3H-ouabain. The K i-values of palytoxin, but not of ouabain, depend on the protein concentration; this indicates additional binding sites for the toxin on kidney membranes. — Palytoxin inhibits the enzymatic activity of the detergent-activated preparation nearly completely (IC50 8·10−7 mol/l). Inhibition of ATPase activity and of ouabain binding are promoted by borate, a known activator of palytoxin. — Palytoxin also inhibits the Na+, K+-ATPase of erythrocyte ghosts in the same dose range. The data are discussed in context with the hypothesis (Chhatwal et al. 1983) that palytoxin raises the cellular permeability by altering the state of Na+, K+-ATPase or its environment.
    Type of Medium: Electronic Resource
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