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Am J Physiol Heart Circ Physiol 283: H181-H185, 2002. First published March 14, 2002; doi:10.1152/ajpheart.00963.2001
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Vol. 283, Issue 1, H181-H185, July 2002

Expression of TASK-1, a pH-sensitive twin-pore domain K+ channel, in rat myocytes

Sandra A. Jones, Michael J. Morton, Malcolm Hunter, and Mark R. Boyett

School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom

We have investigated the expression of TASK-1, a pH-sensitive, twin-pore domain K+ channel in the rat heart. A mammalian cell line of Chinese hamster ovary cells (CHO), transfected with a plasmid containing mouse TASK-1, demonstrated the specificity of the anti-TASK-1 antibody. TASK-1 expression in cardiac tissue was initially demonstrated by Western blot and then localized by immunofluorescence. In single rat ventricular myocytes, strong staining of the TASK-1 protein was located at the intercalated disks and across the cell in a striated pattern, corresponding to the transverse axial tubular network (T tubules). In contrast, single rat atrial myocytes were stained at the intercalated disks with a weak punctate, striated pattern corresponding to underdeveloped T tubules. Also, formamide was used to induce the detubulation of ventricular myocytes, which enabled confirmation that TASK-1 protein expression occurs in T tubules. Consistent with this, RT-PCR revealed the expression of TASK-1 mRNA in total RNA from both the ventricles and atria. In this study, we conclusively demonstrated that TASK-1 protein and mRNA were expressed in rat atrial and ventricular tissue. The extensive distribution of TASK-1 shown to exist within myocyte membranes may provide a potential future target for antiarrhythmic drugs.

protein; immunofluorescence; ribonucleic acid; distribution; transfection


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