Source:http://linkedlifedata.com/resource/pubmed/id/12063289
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2002-6-13
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| pubmed:abstractText |
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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Tandem Pore...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Wheat Germ Agglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/potassium channel subfamily K...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0363-6135
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
283
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
H181-5
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| pubmed:dateRevised |
2006-10-26
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| pubmed:meshHeading |
pubmed-meshheading:12063289-Animals,
pubmed-meshheading:12063289-Antibody Specificity,
pubmed-meshheading:12063289-Blotting, Western,
pubmed-meshheading:12063289-CHO Cells,
pubmed-meshheading:12063289-Cell Separation,
pubmed-meshheading:12063289-Cricetinae,
pubmed-meshheading:12063289-Fluorescent Antibody Technique,
pubmed-meshheading:12063289-Heart Atria,
pubmed-meshheading:12063289-Heart Ventricles,
pubmed-meshheading:12063289-Hydrogen-Ion Concentration,
pubmed-meshheading:12063289-Myocardium,
pubmed-meshheading:12063289-Nerve Tissue Proteins,
pubmed-meshheading:12063289-Potassium Channels,
pubmed-meshheading:12063289-Potassium Channels, Tandem Pore Domain,
pubmed-meshheading:12063289-RNA, Messenger,
pubmed-meshheading:12063289-Rats,
pubmed-meshheading:12063289-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12063289-Transfection,
pubmed-meshheading:12063289-Wheat Germ Agglutinins
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| pubmed:year |
2002
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| pubmed:articleTitle |
Expression of TASK-1, a pH-sensitive twin-pore domain K(+) channel, in rat myocytes.
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| pubmed:affiliation |
School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom. s.a.jones@leeds.ac.uk
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| pubmed:publicationType |
Journal Article
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