| pubmed-article:2538714 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2538714 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:2538714 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:2538714 | lifeskim:mentions | umls-concept:C0441800 | lld:lifeskim |
| pubmed-article:2538714 | lifeskim:mentions | umls-concept:C0205463 | lld:lifeskim |
| pubmed-article:2538714 | lifeskim:mentions | umls-concept:C0205549 | lld:lifeskim |
| pubmed-article:2538714 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2538714 | pubmed:dateCreated | 1989-5-1 | lld:pubmed |
| pubmed-article:2538714 | pubmed:abstractText | Measurements of internal ion concentrations, amino acid pools, and membrane potential were made across a series of HeLa subclones which are amplified for the genes for the sodium- and potassium-activated ATPase (Na,K-ATPase). These subclones expressed heterogeneous levels of ouabain-binding sites, allowing us to construct a graded amplification series. While [K+]i levels did not vary systematically across the series studied, [Na+]i ranged from 9 to 20 mM as a function of Na,K-ATPase expression. Steady-state accumulation of tetraphenylphosphonium in low versus high potassium was used to measure membrane potential. Values for [Na+]i and the membrane potential were used to calculate the sodium electrochemical potential, which was also found to be a function of Na,K-ATPase expression. Measurements of acid-soluble amino acid pools in cell lysates demonstrated that amino acids which are substrates for sodium-dependent transport systems, or which can potentially exchange through system L for a substrate of a sodium-dependent system, varied as a function of the sodium electrochemical potential. This confirmed our prediction of increased amino acid pool sizes in Na,K-ATPase-amplified lines based on observations of elevated flux through the sodium-independent system L. Finally, we measured lactate production and glycolytic potential in a subset of clones and found that both were reduced in subclones with elevated Na,K-ATPase. | lld:pubmed |
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| pubmed-article:2538714 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2538714 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2538714 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2538714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2538714 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2538714 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2538714 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:2538714 | pubmed:author | pubmed-author:AshJ FJF | lld:pubmed |
| pubmed-article:2538714 | pubmed:author | pubmed-author:PauwP GPG | lld:pubmed |
| pubmed-article:2538714 | pubmed:author | pubmed-author:SheckR NRN | lld:pubmed |
| pubmed-article:2538714 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2538714 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:2538714 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2538714 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2538714 | pubmed:pagination | 116-23 | lld:pubmed |
| pubmed-article:2538714 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2538714 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2538714 | pubmed:articleTitle | Steady-state physiological variations across a graded series of Na,K-ATPase-amplified cells. | lld:pubmed |
| pubmed-article:2538714 | pubmed:affiliation | Department of Anatomy, University of Utah School of Medicine, Salt Lake City 84132. | lld:pubmed |
| pubmed-article:2538714 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2538714 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2538714 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
