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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1995-8-4
|
| pubmed:databankReference | |
| pubmed:abstractText |
The basophilic leucaemia cell line RBL-2H3 exhibits a robust inwardly rectifying potassium current, IKIR, which is likely to be modulated by G proteins. We examined the physiological and molecular properties of this KIR conductance to define the nature of the underlying channel species. The macroscopic conductance revealed characteristics typical of classical K+ inward rectifiers of the IRK type. Channel gating was rapid, first order (tau approximately 1 ms at -100 mV) and steeply voltage dependent. Both activation potential and slope conductance were dependent on extracellular K+ concentration ([K+]o) and inward rectification persisted in the absence of internal Mg2+. The current was susceptible to a concentration- and voltage-dependent block by extracellular Na+, Cs+ and Ba2+. Initial IKIR whole-cell amplitudes as well as current rundown were dependent on the presence of 1 mM internal ATP. Perfusion of intracellular guanosine 5'-Q-(3-thiotriphosphate) (GTP[gamma S]) suppressed IKIR with an average half-time of decline of approximately 400 s. It was demonstrated that the dominant IRK-type 25 pS conductance channel was indeed suppressed by 100 microM preloaded GTP[gamma S]. Reverse transcriptase-polymerase chain reactions (RT-PCR) with RBL cell poly(A)+ RNA identified a full length K+ inward rectifier with 94% base pair homology to the recently cloned mouse IRK1 channel. It is concluded that RBL cells express a classical voltage-dependent IRK-type K+ inward rectifier RBL-IRK1 which is negatively controlled by G proteins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Barium,
http://linkedlifedata.com/resource/pubmed/chemical/Cesium,
http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0031-6768
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
429
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
809-19
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7603835-Adenosine Triphosphate,
pubmed-meshheading:7603835-Amino Acid Sequence,
pubmed-meshheading:7603835-Animals,
pubmed-meshheading:7603835-Barium,
pubmed-meshheading:7603835-Base Sequence,
pubmed-meshheading:7603835-Cesium,
pubmed-meshheading:7603835-Edetic Acid,
pubmed-meshheading:7603835-Electric Conductivity,
pubmed-meshheading:7603835-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:7603835-Ion Channel Gating,
pubmed-meshheading:7603835-Kinetics,
pubmed-meshheading:7603835-Leukemia, Basophilic, Acute,
pubmed-meshheading:7603835-Magnesium,
pubmed-meshheading:7603835-Mast Cells,
pubmed-meshheading:7603835-Molecular Sequence Data,
pubmed-meshheading:7603835-Polymerase Chain Reaction,
pubmed-meshheading:7603835-Potassium,
pubmed-meshheading:7603835-Potassium Channels,
pubmed-meshheading:7603835-Rats,
pubmed-meshheading:7603835-Sodium,
pubmed-meshheading:7603835-Tumor Cells, Cultured
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Physiological and molecular characterization of an IRK-type inward rectifier K+ channel in a tumour mast cell line.
|
| pubmed:affiliation |
Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
|
| pubmed:publicationType |
Journal Article
|