The Journal of Membrane Biology

, Volume 237, Issue 2–3, pp 93–106 | Cite as

Inhibition of Cation Channels in Human Erythrocytes by Spermine

Article
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Abstract

In erythrocytes, spermine concentration decreases gradually with age, which is paralleled by increases of cytosolic Ca2+ concentration, with subsequent cell shrinkage and cell membrane scrambling. Cytosolic Ca2+ was estimated from Fluo-3 fluorescence, cell volume from forward scatter, cell membrane scrambling from annexin V binding and cation channel activity with whole-cell patch-clamp in human erythrocytes. Extracellular spermine exerted a dual effect on erythrocyte survival. At 200 μM spermine blunted the increase of intracellular Ca2+, cell shrinkage and annexin V binding following 48 h exposure of cells at +37°C. In contrast, short exposure (10–30 min) of cells to 2 mM spermine was accompanied by increased cytosolic Ca2+ and annexin binding. Intracellular addition of spermine at subphysiological concentration (0.2 μM) significantly decreased the conductance of monovalent cations (Na+, K+, NMDG+) and of Ca2+. Moreover, spermine (0.2 μM) blunted the stimulation of voltage-independent cation channels by Cl− removal. Spermine (0.2 and 200 μM) added to the extracellular bath solution similarly inhibited the cation conductance in Cl−-containing bath solution. The effect of 0.2 μM spermine, but not the effect of 200 μM, was rapidly reversible. Acute addition (250 μM) of a naphthyl acetyl derivative of spermine (200 μM) again significantly decreased basal cation conductance in NaCl bath solution and inhibited voltage-independent cation channels. Spermine is a powerful regulator of erythrocyte cation channel cytosolic Ca2+ activity and, thus, cell survival.

Keywords

Red blood cell Ca2+ Phosphatidylserine exposure Cell volume Spermine NASPM Aging Channel 
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Notes

Acknowledgements

The authors acknowledge the meticulous preparation of the manuscript by Lejla Subasic and Tanja Loch. This study was supported by the Deutsche Forschungsgemeinschaft (La 315/13-3).

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© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  1. 1.Department of Physiology Institute IEberhard-Karls Universität TübingenTübingenGermany
  2. 2.Institute for Problems of Cryobiology and CryomedicineUkrainian National Academy of SciencesKharkovUkraine

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