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Volume 17, Number 13, Issue of July 1, 1997 pp. 4942-4955
Copyright ©1997 Society for Neuroscience

Redox Modulation of hslo Ca²⁺-Activated K⁺ Channels

Received Jan. 15, 1997; revised April 9, 1997; accepted April 14, 1997.

Timothy J. DiChiara and Peter H. Reinhart

Department of Neurobiology, Duke University Medical Center, Durham, North Carolina 27710

The modulation of ion channel proteins by cellular redox potential has emerged recently as a significant determinant of channel function. We have investigated the influence of sulfhydryl redox reagents on human brain Ca²⁺-activated K⁺ channels (hslo) expressed in both human embryonic kidney 293 cells and Xenopus oocytes using macropatch and single-channel analysis. Intracellular application of the reducing agent dithiothreitol (DTT): (1) shifts the voltage of half-maximal channel activation (V_0.5) 18 mV to more negative potentials without affecting the maximal conductance or the slope of the voltage dependence; (2) slows by 10-fold a time-dependent right-shift in V_0.5 values ("run-down"); (3) speeds macroscopic current activation kinetics by 33%; and (4) increases the single-channel open probability without affecting the unitary conductance. In contrast to DTT treatment, oxidation with hydrogen peroxide shifts macropatch V_0.5 values to more positive potentials, increases the rate of channel run-down, and decreases the single-channel open probability. K_Ca channels cloned from Drosophila differ from hslo channels in that they show very little run-down and are not modulated by the addition of DTT. These data indicate that hslo Ca²⁺-activated K⁺ channels may be modulated by changes in the cellular redox potential as well as by the transmembrane voltage and the cytoplasmic Ca²⁺ concentration.

Key words: calcium-activated potassium channel; hslo; dslo; HEK293 cells; redox; reduction; oxidation; dithiothreitol; hydrogen peroxide; cysteine; disulfide

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