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Am J Physiol Cell Physiol 282: C588-C594, 2002. First published September 21, 2001; doi:10.1152/ajpcell.00365.2001
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Vol. 282, Issue 3, C588-C594, March 2002

Apoptosis recruits two-pore domain potassium channels used for homeostatic volume regulation

James R. Trimarchi1,3, Lin Liu1,3, Peter J. S. Smith2, and David L. Keefe1,3

1 Laboratory for Reproductive Medicine and 2 BioCurrents Research Center, Marine Biological Laboratory, Woods Hole, Massachusetts 02543; and 3 Women and Infants Hospital, Brown University, Providence, Rhode Island 02905

Cell shrinkage is an incipient hallmark of apoptosis and is accompanied by potassium release that decreases the concentration of intracellular potassium and regulates apoptotic progression. The plasma membrane K+ channel recruited during apoptosis has not been characterized despite its importance as a potential therapeutic target. Here we provide evidence that two-pore domain K+ (K2P) channels underlie K+ efflux during apoptotic volume decreases (AVD) in mouse embryos. These K2P channels are inhibited by quinine but are not blocked by an array of pharmacological agents that antagonize other K+ channels. The K2P channels are uniquely suited to participate in the early phases of apoptosis because they are not modulated by common intracellular messengers such as calcium, ATP, and arachidonic acid, transmembrane voltage, or the cytoskeleton. A K+ channel with similar biophysical properties coordinates regulatory volume decreases (RVD) triggered by changing osmotic conditions. We propose that K2P channels are the pathway by which K+ effluxes during AVD and RVD and that apoptosis co-opts mechanisms more routinely employed for homeostatic cell volume regulation.

self-referencing electrode; cell volume; quinine; cell shrinkage


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