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

被引:46
作者
Jones, SA [1 ]
Morton, MJ [1 ]
Hunter, M [1 ]
Boyett, MR [1 ]
机构
[1] Univ Leeds, Sch Biomed Sci, Leeds LS2 9JT, W Yorkshire, England
来源
AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY | 2002年 / 283卷 / 01期
关键词
protein; immunofluorescence; ribonucleic acid; distribution; transfection;
D O I
10.1152/ajpheart.00963.2001
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
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.
引用
收藏
页码:H181 / H185
页数:5
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