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Am J Physiol Heart Circ Physiol (March 14, 2002). doi:10.1152/ajpheart.00963.2001
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Articles in PresS, published online ahead of print March 14, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00963.2001
Submitted on November 2, 2001
Accepted on March 13, 2002

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

Sandra A. Jones1*, Michael J. Morton1, Malcolm Hunter1, and Mark R. Boyett1

1 School of Biomedical Sciences, University of Leeds, Leeds, Yorkshire, United Kingdom

* To whom correspondence should be addressed. E-mail: s.a.jones{at}leeds.ac.uk.

We have investigated the expression of TASK-1, a pH-sensitive, twin pore-domain K+ channel in the rat heart. The mammalian cell line of 'Chinese Hamster ovary' (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 localised by immunofluorescence. In single rat ventricular myocytes, strong staining of the TASK-1 protein was located at the intercalated discs 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 discs 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 was 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 anti-arrhythmic drugs.




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