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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-5-18
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pubmed:abstractText |
Using the two-microelectrode voltage clamp technique in Xenopus laevis oocytes, we estimated Na(+)-K(+)-ATPase activity from the dihydroouabain-sensitive current (IDHO) in the presence of increasing concentrations of tetraethylammonium (TEA+; 0, 5, 10, 20, 40 mM), a well-known blocker of K+ channels. The effects of TEA+ on the total oocyte currents could be separated into two distinct parts: generation of a nonsaturating inward current increasing with negative membrane potentials (VM) and a saturable inhibitory component affecting an outward current easily detectable at positive VM. The nonsaturating component appears to be a barium-sensitive electrodiffusion of TEA+ which can be described by the Goldman-Hodgkin-Katz equation, while the saturating component is consistent with the expected blocking effect of TEA+ on K+ channels. Interestingly, this latter component disappears when the Na(+)-K(+)-ATPase is inhibited by 10 microM DHO. Conversely, TEA+ inhibits a component of IDHO with a KD of 25 +/- 4 mM at +50 mV. As the TEA(+)-sensitive current present in IDHO reversed at -75 mV, we hypothesized that it could come from an inhibition of K+ channels whose activity varies in parallel with the Na(+)-K(+)-ATPase activity. Supporting this hypothesis, the inward portion of this TEA(+)-sensitive current can be completely abolished by the addition of 1 mM Ba2+ to the bath. This study suggests that, in X. laevis oocytes, a close link exists between the Na-K-ATPase activity and TEA(+)-sensitive K+ currents and indicates that, in the absence of effective K+ channel inhibitors, IDHO does not exclusively represent the Na(+)-K(+)-ATPase-generated current.
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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/Ouabain,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channel Blockers,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Tetraethylammonium,
http://linkedlifedata.com/resource/pubmed/chemical/Tetraethylammonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/dihydroouabain
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-2631
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
143
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29-35
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7714886-Animals,
pubmed-meshheading:7714886-Cell Membrane,
pubmed-meshheading:7714886-Electrophysiology,
pubmed-meshheading:7714886-Female,
pubmed-meshheading:7714886-Membrane Potentials,
pubmed-meshheading:7714886-Oocytes,
pubmed-meshheading:7714886-Ouabain,
pubmed-meshheading:7714886-Patch-Clamp Techniques,
pubmed-meshheading:7714886-Potassium Channel Blockers,
pubmed-meshheading:7714886-Potassium Channels,
pubmed-meshheading:7714886-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:7714886-Tetraethylammonium,
pubmed-meshheading:7714886-Tetraethylammonium Compounds,
pubmed-meshheading:7714886-Xenopus laevis
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pubmed:year |
1995
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pubmed:articleTitle |
Evidence for coupling between Na+ pump activity and TEA-sensitive K+ currents in Xenopus laevis oocytes.
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pubmed:affiliation |
Groupe de recherche en transport membranaire, University of Montreal, Quebec.
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pubmed:publicationType |
Journal Article
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