Amphiphile-induced phosphatidylserine exposure in human erythrocytes

A1 Journal article (refereed)

Internal Authors/Editors

Publication Details

List of Authors: Hägerstrand, Holmström, Bobrowska-Hägerstrand, Eriksson, Isomaa
Publication year: 1998
Journal: Molecular Membrane Biology
Journal acronym: Mol Membr Biol
Volume number: 15
Issue number: 2
Start page: 89
End page: 95
ISSN: 0968-7688
eISSN: 1464-5203


Nonionic and anionic water-soluble amphiphiles were shown to increase strongly the binding of fluorescein isothiocyanate-conjugated annexin V (FITC-annexin V) in human erythrocytes pretreated with the aminophospholipid translocase (APLT) inhibitor n-ethylmaleimide (NEM). At high sublytic amphiphile-concentrations the binding of FITC-annexin V, monitored in a flow cytometer, was time- and temperature-dependent and occurred heterogeneously in the cell population, with 43-81% of cells being stained above background following incubation for 60 minutes at 37 degrees C. The increased FITC-annexin V binding apparently indicates an increased flop rate of phosphatidylserine (PS) to the outer membrane leaflet. When the NEM-pretreatment was omitted, the FITC-annexin V binding was markedly, but not completely, reduced. In erythrocytes incubated with a zwitter-ionic amphiphile, a small increase in FITC-annexin V binding was detected, while cationic amphiphiles did not induce an increased FITC-annexin V binding. The potency of amphiphiles to induce PS exposure was not related to the type of shape alteration or vesiculation induced. Our results indicate a significant role of the charge status of a membrane intercalated amphiphile for its capability to induce PS exposure.

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