Bacterial cytotoxins, amphotericin B and local anesthetics enhance transbilayer mobility of phospholipids in erythrocyte membranes. Consequences for phospholipid asymmetry.

@article{Schneider1986BacterialCA,
  title={Bacterial cytotoxins, amphotericin B and local anesthetics enhance transbilayer mobility of phospholipids in erythrocyte membranes. Consequences for phospholipid asymmetry.},
  author={Erasmus Schneider and Cees W. M. Haest and Gunther Plasa and Bernhard Deuticke},
  journal={Biochimica et biophysica acta},
  year={1986},
  volume={855 3},
  pages={
          325-36
        }
}
Amphotericin B Membrane Action: Role for Two Types of Ion Channels in Eliciting Cell Survival and Lethal Effects
TLDR
A cell model is developed that serves as a framework for understanding how the intracellular K+ and Na+ concentration changes induced by the cation-selective AmB channels enhance multiple survival response pathways before they are overcome by the more sustained ion fluxes, Ca2+-dependent apoptotic events and cell lysis effects that are associated with the formation of AmB aqueous pores.
Gramicidin-induced enhancement of transbilayer reorientation of lipids in the erythrocyte membrane.
Incorporation of the channel-forming antibiotic gramicidin into the membrane of human erythrocytes highly (up to 30-fold) enhances rates of reorientation (flip) of lysophosphatidylcholine and
Nonmediated flip-flop of phospholipid analogues in the erythrocyte membrane as probed by palmitoylcarnitine: Basic properties and influence of membrane modification
TLDR
The flip is enhanced by lowering the pH and exhibits interindividual variability, phenomena not observed for the flip-flop of lysophosphatidylcholine, suggesting that generalizations on the kinetics of nonmediated flip-Flop of membrane-intercalated amphiphiles may not be justified.
On the mechanism of drug-induced acceleration of phospholipid translocation in the human erythrocyte membrane
TLDR
An unspecific bilayer perturbation is proposed to enhance the probability of formation of hydrophobic defects in the bilayer, facilitating penetration of the polar head group of the phospholipid into the apolar membrane core.
The Lantibiotic Nisin Induces Transmembrane Movement of a Fluorescent Phospholipid
TLDR
The data indicate that nisin transiently disturbs the phospholipid organization of the target membrane.
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It is suggested that cationic drugs in general may alter the protein-lipid interaction of the membrane and thus release the inner layer phospholipid PE from possible locational restriction under the influence of certain proteins.
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The results indicate that the accumulation of the transferable ("loose") form of cytochrome b5 on the outer surface of a vesicle causes a transient, global destabilization of the bilayer that is relieved by lipid flip-flop.
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