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Oxidation induces ClC‐3‐dependent anion channels in human leukaemia cells
Author(s) -
Kasinathan Ravi S.,
Föller Michael,
Lang Camelia,
Koka Saisudha,
Lang Florian,
Huber Stephan M.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.10.042
Subject(s) - chemistry , biophysics , permeability (electromagnetism) , intracellular , redox , k562 cells , biotinylation , membrane , patch clamp , membrane permeability , transmembrane protein , microbiology and biotechnology , biochemistry , cell , biology , inorganic chemistry , receptor
To test for redox regulation of anion channels in erythroid cells, we exposed K562 cells to oxidants and measured changes in transmembrane Cl − currents using patch‐clamp, and in intracellular Cl − content using the Cl − selective dye MQAE. Oxidation with tert ‐butylhydroperoxide or H 2 O 2 produced a plasma membrane anion permeability with a permselectivity ofNO 3 ‐ > lactate ‐ > gluconate ‐ .The permeability increase was paralleled by insertion of ClC‐3 protein into the plasma membrane as evident from immunofluorescence microscopy and surface biotinylation. Down‐regulation of ClC‐3 protein by RNA interference as assessed by immunoblotting decreased the oxidation‐stimulated permeability. In conclusion, oxidation induces surface expression of ClC‐3 and activation of a ClC‐3‐dependent anion permeability in K562 cells.