Evidence map›Paper›PMID 19196986›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

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.

T L Radzyukevich, J B Lingrel, J A Heiny

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.1field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Sensational site: the sodium pump ouabain-binding site and its ligands.American journal of physiology. Cell physiology · 2024
    Review
  2. Exercise and fatigue: integrating the role of KEuropean journal of applied physiology · 2023
    Review
  3. Identification of the NAJournal of chemical ecology · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Skeletal Muscle Na,K-ATPase as a Target for Circulating Ouabain.International journal of molecular sciences · 2020
    Article
  9. Article
  10. Review
  11. Isoform-specific role of Na/K-ATPase α1 in skeletal muscle.American journal of physiology. Endocrinology and metabolism · 2018
    Article
  12. Review
  13. Pivotal role of α2 NaThe Journal of physiology · 2016
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Na+/Ca2+ exchange and Na+/K+-ATPase in the heart.The Journal of physiology · 2015
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

T L RadzyukevichDepartment of Molecular and Cellular Physiology, University of Cincinnati College of Medicine, Cincinnati, OH 45267-0576, USA.
J B Lingrel
J A Heiny
University of Cincinnati Medical Center · US

Funding

SODIUM/POTASSIUM ATPASE AND ITS GENESR01HL028573 · NHLBI · UNIVERSITY OF CINCINNATI · PI LINGREL, JERRY B · 1986 to 2011
$3.9M
FUNCTIONAL STUDIES OF THE NA,K-ATPASER01HL066062 · NHLBI · UNIVERSITY OF CINCINNATI · PI LINGREL, JERRY B · 2001 to 2009
$3.4M
NHLBI NIH HHS HL28573NHLBI NIH HHS HL66062NHLBI NIH HHS R01 HL028573NHLBI NIH HHS R01 HL066062
6 · The paper itself

Abstract

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.

Indexed as

AnimalsBinding SitesBiological Transport, ActiveCardiac GlycosidesIsoenzymesMiceMuscle, SkeletalPhysical Conditioning, AnimalSodium-Potassium-Exchanging ATPaseCardiac GlycosidesIsoenzymesSodium-Potassium-Exchanging ATPase

Identifiers

PMID19196986
PMCPMC2650304
OpenAlexW1972829652

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.