© 1998 American Heart Association, Inc.
Rapid Communication |
Cloning and Functional Expression of a Novel Cardiac Two-Pore Background K+ Channel (cTBAK-1)
From the Department of Pharmacology II (D.K., Y.H., Y.K.), Faculty of Medicine, Osaka University, Osaka, Japan, and the Department of Cell Biology and Signaling (A.F., Y.K.), Yamagata University School of Medicine, Yamagata, Japan.
Correspondence to Yoshihisa Kurachi, MD, PhD, Department of Pharmacology II, Faculty of Medicine, Osaka University, 2–2 Yamada-oka, Suita, Osaka 565, Japan. E-mail ykurachi{at}pharma2.med.osaka-u.ac.jp
Abstract
Abstract—We have cloned from a mouse
heart cDNA library a novel K+ channel subunit that has two
pore-forming domains and four transmembrane regions. Its amino acid
sequence shares 25% identity with mouse TWIK-1, 22% with mouse
TREK-1, and 33% with a putative K+ channel of
Caenorhabditis elegans (C40C9). Strikingly abundant mRNA
for this clone was expressed in the heart. The mRNA was also detected
in kidney, brain, skin, testis, lung, skeletal muscle, small intestine,
and stomach but not in liver, thymus, or spleen. Reverse
transcription–polymerase chain reaction analyses of single
cells showed that the mRNA of the clone was expressed in both atrial
and ventricular myocytes per se. Xenopus
oocytes injected with the cRNA of the clone expressed a
Ba2+-sensitive K+-selective current with an
almost linear steady-state current-voltage relationship. In
cell-attached patches, the expressed channel exhibited short-lasting
openings with a mean open time of 
2 milliseconds and a unitary
conductance of 16 pS (150 mmol/L
[K+]o). The K+ current was
insensitive to intracellular Na+ (50 mmol/L),
Ca2+ (0.1 mmol/L), H+ (pH 6.4), and
arachidonic acid (10 µmol/L) in inside-out
patches. Thus, the current flowing through the channel may contribute
to the cardiac cellular electrical activity as a linear background
K+ conductance. Therefore, we designated the clone cTBAK
(cardiac two-pore background K+ channel).
Key Words: two pore-domain K+ channel • molecular cloning • heart • cardiac myocyte • functional expression
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A. Barbuti, S. Ishii, T. Shimizu, R. B. Robinson, and S. J. Feinmark Block of the background K+ channel TASK-1 contributes to arrhythmogenic effects of platelet-activating factor Am J Physiol Heart Circ Physiol, June 1, 2002; 282(6): H2024 - H2030. [Abstract] [Full Text] [PDF]
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W. Gu, G. Schlichthorl, J. R Hirsch, H. Engels, C. Karschin, A. Karschin, C. Derst, O. K Steinlein, and J. Daut Expression pattern and functional characteristics of two novel splice variants of the two-pore-domain potassium channel TREK-2 J. Physiol., March 15, 2002; 539(3): 657 - 668. [Abstract] [Full Text] [PDF]
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A. Fujita, Y. Horio, K. Higashi, T. Mouri, F. Hata, N. Takeguchi, and Y. Kurachi Specific localization of an inwardly rectifying K+ channel, Kir4.1, at the apical membrane of rat gastric parietal cells; its possible involvement in K+ recycling for the H+-K+-pump J. Physiol., April 1, 2002; 540(1): 85 - 92. [Abstract] [Full Text] [PDF]
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