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PMID: 14600080 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Role of Ca2+-activated K+ channels in human erythrocyte apoptosis.

American journal of physiology. Cell physiology ·Vol. 285 ·No. 6 ·2003-12-00 ·Pages C1553-60

Lang PA, Kaiser S, Myssina S, Wieder T, Lang F, Huber SM

Abstract

Exposure of erythrocytes to the Ca2+ ionophore ionomycin has recently been shown to induce cell shrinkage, cell membrane blebbing, and breakdown of phosphatidylserine asymmetry, all features typical of apoptosis of nucleated cells. Although breakdown of phosphatidylserine asymmetry is thought to result from activation of a Ca2+-sensitive scramblase, the mechanism and role of cell shrinkage have not been explored. The present study was performed to test whether ionomycin-induced activation of Ca2+-sensitive Gardos K+ channels and subsequent cell shrinkage participate in ionomycin-induced breakdown of phosphatidylserine asymmetry of human erythrocytes. According to on-cell patch-clamp experiments, ionomycin (1 microM) induces activation of inwardly rectifying K+-selective channels in the erythrocyte membrane. Fluorescence-activated cell sorter analysis reveals that ionomycin leads to a significant decrease of forward scatter, reflecting cell volume, an effect blunted by an increase of extracellular K+ concentration to 25 mM and exposure to the Gardos K+ channel blockers charybdotoxin (230 nM) and clotrimazole (5 microM). As reflected by annexin binding, breakdown of phosphatidylserine asymmetry is triggered by ionomycin, an effect again blunted, but not abolished, by an increase of extracellular K+ concentration and exposure to charybdotoxin (230 nM) and clotrimazole (5 microM). Similar to ionomycin, glucose depletion leads (within 55 h) to annexin binding of erythrocytes, an effect again partially reversed by an increase of extracellular K+ concentration and exposure to charybdotoxin. K-562 human erythroleukemia cells similarly respond to ionomycin with cell shrinkage and annexin binding, effects blunted by antisense, but not sense, oligonucleotides against the small-conductance Ca2+-activated K+ channel isoform hSK4 (KCNN4). The experiments disclose a novel functional role of Ca2+-sensitive K+ channels in erythrocytes, i.e., their participation in regulation of erythrocyte apoptosis.

MeSH Terms
Annexins/drug effects,metabolism Apoptosis/drug effects,physiology Calcium/chemistry,metabolism Cells, Cultured Erythrocytes/drug effects,metabolism,pathology Flow Cytometry Humans Intermediate-Conductance Calcium-Activated Potassium Channels Ionomycin/pharmacology Ionophores/pharmacology K562 Cells Oligodeoxyribonucleotides, Antisense Patch-Clamp Techniques Phosphatidylserines/metabolism Potassium/chemistry,metabolism Potassium Channels/genetics Potassium Channels, Calcium-Activated/physiology
Chemicals
Annexins Intermediate-Conductance Calcium-Activated Potassium Channels Ionophores KCNN4 protein, human Oligodeoxyribonucleotides, Antisense Phosphatidylserines Potassium Channels Potassium Channels, Calcium-Activated Ionomycin Potassium Calcium
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Lang Philipp A
Physiologisches Institut der Universität Tübingen, Gmelinstr. 5, D 72076 Tübingen, Germany.
Kaiser Stefanie
Myssina Swetlana
Wieder Thomas
Lang Florian
Huber Stephan M
Article Info
Journal
American journal of physiology. Cell physiology
Abbr.
Am J Physiol Cell Physiol
ISSN
0363-6143
Published
2003-12-00
Pages
C1553-60
Language
English
Region
United States
NLM ID
100901225
Subset
IM
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