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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6 Pt 1
|
| pubmed:dateCreated |
1995-8-15
|
| pubmed:abstractText |
We have previously cloned a bovine renal epithelial channel homologue (alpha-bENaC) belonging to the epithelial Na+ channel (ENaC) family. With the use of a rabbit nuclease-treated in vitro translation system, mRNA coding for alpha-bENaC was translated and the polypeptide products were reconstituted into liposomes. On incorporation into planar lipid bilayers, in vitro-translated alpha-bENaC protein 1) displayed voltage-independent Na+ channel activity with a single-channel conductance of 40 pS, 2) was mechanosensitive in that the single-channel open probability was maximally activated with a hydrostatic pressure gradient of 0.26 mmHg across the bilayer, 3) was blocked by low concentrations of amiloride [apparent inhibitory constant of amiloride (K(i)amil approximately 150 nM], and 4) was cation selective with a Li+:Na+:K+ permselectivity of 2:1:0.14 under nonstretched conditions. These pharmacological and selectivity characteristics were altered to a lower amiloride affinity (K(i)amil > 25 microM) and a lack of monovalent cation selectivity in the presence of a hydrostatic pressure gradient. This observation of stretch activation (SA) of alpha-bENaC was confirmed in dual electrode recordings of heterologously expressed alpha-bENaC whole cell currents in Xenopus oocytes swelled by the injection of 15 nl of a 100 mM KCl solution. We conclude that alpha-bENaC, and by analogy other ENaCs, represent a novel family of cloned SA channels.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amiloride,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Proteolipids,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/proteoliposomes
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0002-9513
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
268
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
C1450-9
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7611365-Amiloride,
pubmed-meshheading:7611365-Animals,
pubmed-meshheading:7611365-Cattle,
pubmed-meshheading:7611365-Cloning, Molecular,
pubmed-meshheading:7611365-Epithelium,
pubmed-meshheading:7611365-Hydrostatic Pressure,
pubmed-meshheading:7611365-Ion Channel Gating,
pubmed-meshheading:7611365-Kidney Medulla,
pubmed-meshheading:7611365-Kidney Tubules, Collecting,
pubmed-meshheading:7611365-Lipid Bilayers,
pubmed-meshheading:7611365-Membrane Potentials,
pubmed-meshheading:7611365-Probability,
pubmed-meshheading:7611365-Protein Biosynthesis,
pubmed-meshheading:7611365-Proteolipids,
pubmed-meshheading:7611365-RNA, Messenger,
pubmed-meshheading:7611365-Rabbits,
pubmed-meshheading:7611365-Recombinant Proteins,
pubmed-meshheading:7611365-Sodium Channels
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
A cloned renal epithelial Na+ channel protein displays stretch activation in planar lipid bilayers.
|
| pubmed:affiliation |
Department of Physiology and Biophysics, University of Alabama at Birmingham 35294, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|