Biophysical and Pharmacological Characteristics of Native Two-Pore Domain TASK Channels in Rat Adrenal Glomerulosa Cells

Biophysical and Pharmacological Characteristics of Native Two-Pore Domain TASK Channels in Rat... Multiple genes of the TASK subfamily of two-pore domain K+ channels are reported to be expressed in rat glomerulosa cells. To determine which TASK isoforms contribute to native leak channels controlling resting membrane potential, patch-clamp studies were performed to identify biophysical and pharmacological characteristics of macroscopic and unitary K+ currents diagnostic of recombinant TASK channel isoforms. Results indicate K+ conductance (gK+) is mediated almost exclusively by a weakly voltage-dependent (leak) K+ channel closely resembling TASK-3. Leak channels exhibited a unitary conductance approximating that expected for TASK-3 under the recording conditions employed, brief mean open times and a voltage-dependent open probability. Extracellular H+ induced voltage-independent inhibition of gK+, exhibiting an IC50 of 56 nM (pH 7.25) and a Hill coefficient of 0.75. Protons inhibited leak channel open probability (Po) by promoting a long-lived closed state (τ > 500 ms). Extracellular Zn2+ mimicked the effects of H+; inhibition of gK+ exhibited an IC50 of 41 μM with a Hill coefficient of 1.26, inhibiting channel gating by promoting a long-lived closed state. Ruthenium red (5 μM) inhibited gK+ by 75.6% at 0 mV. Extracellular Mg2+ induced voltage-dependent block of gK+, inhibiting unitary current amplitude without affecting mean open time. Bupivacaine induced voltage-dependent block of gK+, exhibiting IC50 values of 116 μM at −100 mV and 28 μM at 40 mV with Hill coefficients of 1 at both potentials. Halothane induced a voltage-independent stimulation of gK+ primarily by decreasing the leak channel closed-state dwell time. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Biophysical and Pharmacological Characteristics of Native Two-Pore Domain TASK Channels in Rat Adrenal Glomerulosa Cells

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Publisher
Springer-Verlag
Copyright
Copyright © 2006 by Springer Science+Business Media, Inc.
Subject
Life Sciences; Human Physiology; Biochemistry, general
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-005-7012-x
Publisher site
See Article on Publisher Site

Abstract

Multiple genes of the TASK subfamily of two-pore domain K+ channels are reported to be expressed in rat glomerulosa cells. To determine which TASK isoforms contribute to native leak channels controlling resting membrane potential, patch-clamp studies were performed to identify biophysical and pharmacological characteristics of macroscopic and unitary K+ currents diagnostic of recombinant TASK channel isoforms. Results indicate K+ conductance (gK+) is mediated almost exclusively by a weakly voltage-dependent (leak) K+ channel closely resembling TASK-3. Leak channels exhibited a unitary conductance approximating that expected for TASK-3 under the recording conditions employed, brief mean open times and a voltage-dependent open probability. Extracellular H+ induced voltage-independent inhibition of gK+, exhibiting an IC50 of 56 nM (pH 7.25) and a Hill coefficient of 0.75. Protons inhibited leak channel open probability (Po) by promoting a long-lived closed state (τ > 500 ms). Extracellular Zn2+ mimicked the effects of H+; inhibition of gK+ exhibited an IC50 of 41 μM with a Hill coefficient of 1.26, inhibiting channel gating by promoting a long-lived closed state. Ruthenium red (5 μM) inhibited gK+ by 75.6% at 0 mV. Extracellular Mg2+ induced voltage-dependent block of gK+, inhibiting unitary current amplitude without affecting mean open time. Bupivacaine induced voltage-dependent block of gK+, exhibiting IC50 values of 116 μM at −100 mV and 28 μM at 40 mV with Hill coefficients of 1 at both potentials. Halothane induced a voltage-independent stimulation of gK+ primarily by decreasing the leak channel closed-state dwell time.

Journal

The Journal of Membrane BiologySpringer Journals

Published: Jun 22, 2006

References

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