Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we will assume that you are happy to receive all cookies and you will not see this message again. Click 'Find out more' for information on how to change your cookie settings.

In rat arterial chemoreceptors, background potassium channels play an important role in maintaining resting membrane potential and promoting depolarization and excitation in response to hypoxia or acidosis. It has been suggested that these channels are a heterodimer of TASK-1 and TASK-3 based on their similarity to heterologously expressed TASK-1/3 fusion proteins. In this study, we sought to confirm the identity of these channels through germline ablation of Task-1 (Kcnk3) and Task-3 (Kcnk9) in mice. Background K-channels were abundant in carotid body type-1 cells from wild-type mice and comparable to those previously described in rat type-1 cells with a main conductance state of 33 pS. This channel was absent from both Task-1(-/-) and Task-3(-/-) cells. In its place we observed a larger (38 pS) K(+)-channel in Task-1(-/-) cells and a smaller (18 pS) K(+)-channel in Task-3(-/-) cells. None of these channels were observed in Task-1(-/-)/Task-3(-/-) double knock-out mice. We therefore conclude that the predominant background K-channel in wild-type mice is a TASK-1/TASK-3 heterodimer, whereas that in Task-1(-/-) mice is TASK-3 and, conversely, that in Task-3(-/-) mice is TASK-1. All three forms of TASK channel in type-1 cells were inhibited by hypoxia, cyanide and the uncoupler FCCP, but the greatest sensitivity was seen in TASK-1 and TASK-1/TASK-3 channels. In summary, the background K-channel in type-1 cells is predominantly a TASK-1/TASK-3 heterodimer. Although both TASK-1 and TASK-3 are able to couple to the oxygen and metabolism sensing pathways present in type-1 cells, channels containing TASK-1 appear to be more sensitive.

Original publication

DOI

10.1113/jphysiol.2013.262022

Type

Journal article

Journal

J Physiol

Publication Date

01/12/2013

Volume

591

Pages

5977 - 5998

Keywords

Animals, Calcium, Calcium Signaling, Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone, Carotid Body, Mice, Mice, Knockout, Mitochondria, Nerve Tissue Proteins, Oxygen, Potassium Channels, Potassium Channels, Tandem Pore Domain, Rotenone, Sodium Cyanide