pubmed-article:1653250 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C0018873 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C1979844 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C1979845 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
pubmed-article:1653250 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:1653250 | pubmed:issue | 25 | lld:pubmed |
pubmed-article:1653250 | pubmed:dateCreated | 1991-10-4 | lld:pubmed |
pubmed-article:1653250 | pubmed:abstractText | The role of multiple isoforms for the alpha subunit of Na,K-ATPase is essentially unknown. To examine the functional properties of the three alpha subunit isoforms, we developed a system for the heterologous expression of Na,K-ATPase in which the enzymatic activity of each isoform can be independently analyzed. Ouabain-resistant forms of the rat alpha 2 and alpha 3 subunits were constructed by site-directed mutagenesis of amino acid residues at the extracellular borders of the first and second transmembrane domains (L111R and N122D for alpha 2 and Q108R and N119D for alpha 3). cDNAs encoding the rat alpha 1 subunit, which is naturally ouabain-resistant, and rat alpha 2 and alpha 3, which were mutated to ouabain resistance (designated rat alpha 2* and rat alpha 3*, respectively) were cloned into an expression vector and transfected into HeLa cells. Resistant clones were isolated and analyzed for ouabain-inhibitable ATPase activity in the presence of 1 microM ouabain, which inhibits the endogenous Na,K-ATPase present in HeLa cells (I50 approximately equal to 10 nM). The remaining activity corresponds to Na,K-ATPase molecules containing the transfected rat alpha 1, rat alpha 2*, or rat alpha 3* isoforms. Utilizing this system, we examined Na+, K+, and ATP dependence of enzyme activity. Na,K-ATPase molecules containing rat alpha 1 and rat alpha 2* exhibited a 2-3-fold higher apparent affinity for Na+ than those containing rat alpha 3* (apparent KNa+ (millimolar): rat alpha 1 = 1.15 +/- 0.13; rat alpha 2* = 1.05 +/- 0.11; rat alpha 3* = 3.08 +/- 0.06). Additionally, rat alpha 3* had a slightly higher apparent affinity for ATP (in the millimolar concentration range) compared with rat alpha 1 or rat alpha 2* (apparent K0.5 (millimolar): rat alpha 1 = 0.43 +/- 0.12; rat alpha 2* = 0.54 +/- 0.15; rat alpha 3* = 0.21 +/- 0.04) and all three isoforms has similar apparent affinities for K+ (apparent KK+: rat alpha 1 = 0.45 +/- 0.01; rat alpha 2* = 0.43 +/- 0.004; rat alpha 3* = 0.27 +/- 0.01). This study represents the first comparison of the functional properties of the three Na,K-ATPase alpha isoforms expressed in the same cell type. | lld:pubmed |
pubmed-article:1653250 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1653250 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1653250 | pubmed:language | eng | lld:pubmed |
pubmed-article:1653250 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1653250 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1653250 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1653250 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:1653250 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1653250 | pubmed:month | Sep | lld:pubmed |
pubmed-article:1653250 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1653250 | pubmed:author | pubmed-author:LingrelJ BJB | lld:pubmed |
pubmed-article:1653250 | pubmed:author | pubmed-author:JewellE AEA | lld:pubmed |
pubmed-article:1653250 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1653250 | pubmed:day | 5 | lld:pubmed |
pubmed-article:1653250 | pubmed:volume | 266 | lld:pubmed |
pubmed-article:1653250 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1653250 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1653250 | pubmed:pagination | 16925-30 | lld:pubmed |
pubmed-article:1653250 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:1653250 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1653250 | pubmed:articleTitle | Comparison of the substrate dependence properties of the rat Na,K-ATPase alpha 1, alpha 2, and alpha 3 isoforms expressed in HeLa cells. | lld:pubmed |
pubmed-article:1653250 | pubmed:affiliation | Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, Ohio 45267-0524. | lld:pubmed |
pubmed-article:1653250 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1653250 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:1653250 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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