| pubmed-article:19196986 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0007158 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0032214 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0600138 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0005529 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19196986 | lifeskim:mentions | umls-concept:C1879648 | lld:lifeskim |
| pubmed-article:19196986 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:19196986 | pubmed:dateCreated | 2009-2-25 | lld:pubmed |
| pubmed-article:19196986 | pubmed:abstractText | The physiological significance of the cardiac glycoside-binding site on the Na,K-ATPase remains incompletely understood. This study used a gene-targeted mouse (alpha2(R/R)) which expresses a ouabain-insensitive alpha2 isoform of the Na,K-ATPase to investigate whether the cardiac glycoside-binding site plays any physiological role in active Na(+)/K(+) transport in skeletal muscles or in exercise performance. Skeletal muscles express the Na,K-ATPase alpha2 isoform at high abundance and regulate its transport over a wide dynamic range under control of muscle activity. Na,K-ATPase active transport in the isolated extensor digitorum longus (EDL) muscle of alpha2(R/R) mice was lower at rest and significantly enhanced after muscle contraction, compared with WT. During the first 60 s after a 30-s contraction, the EDL of alpha2(R/R) mice transported 70.0 nmol/g.min more (86)Rb than WT. Acute sequestration of endogenous ligand(s) in WT mice infused with Digibind to sequester endogenous cardiac glycoside(s) produced similar effects on both resting and contraction-induced (86)Rb transport. Additionally, the alpha2(R/R) mice exhibit an enhanced ability to perform physical exercise, showing a 2.1- to 2.8-fold lower failure rate than WT within minutes of the onset of moderate-intensity treadmill running. Their enhanced exercise performance is consistent with their enhanced contraction-induced Na,K-ATPase transport in the skeletal muscles. These results demonstrate that the Na,K-ATPase alpha2 isozyme in skeletal muscle is regulated dynamically by a mechanism that utilizes the cardiac glycoside-binding site and an endogenous ligand(s) and that its cardiac glycoside-binding site can play a physiological role in the dynamic adaptations to exercise. | lld:pubmed |
| pubmed-article:19196986 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19196986 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19196986 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19196986 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19196986 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19196986 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:19196986 | pubmed:author | pubmed-author:LingrelJ BJB | lld:pubmed |
| pubmed-article:19196986 | pubmed:author | pubmed-author:HeinyJ AJA | lld:pubmed |
| pubmed-article:19196986 | pubmed:author | pubmed-author:RadzyukevichT... | lld:pubmed |
| pubmed-article:19196986 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19196986 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:19196986 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:19196986 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19196986 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19196986 | pubmed:pagination | 2565-70 | lld:pubmed |
| pubmed-article:19196986 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:meshHeading | pubmed-meshheading:19196986... | lld:pubmed |
| pubmed-article:19196986 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19196986 | pubmed:articleTitle | The cardiac glycoside binding site on the Na,K-ATPase alpha2 isoform plays a role in the dynamic regulation of active transport in skeletal muscle. | lld:pubmed |
| pubmed-article:19196986 | pubmed:affiliation | Department of Molecular and Cellular Physiology, University of Cincinnati College of Medicine, Cincinnati, OH 45267-0576, USA. | lld:pubmed |
| pubmed-article:19196986 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19196986 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19196986 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:98660 | entrezgene:pubmed | pubmed-article:19196986 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19196986 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19196986 | lld:pubmed |
