ArticleThe Journal of biological chemistry2013
Tissue-specific role of the Na,K-ATPase α2 isozyme in skeletal muscle.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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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.
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Who cites it
52 citing papers in PubMed, 85 citations in OpenAlex.
- Digoxin and exercise effects on skeletal muscle NaExperimental physiology · 2024Trial
- Six weeks of high-load resistance and low-load blood flow restricted training increase Na/K-ATPase sub-units α2 and β1 equally, but does not alter ClC-1 abundance in untrained human skeletal muscle.Journal of muscle research and cell motility · 2023Trial
- Oral digoxin effects on exercise performance, KThe Journal of physiology · 2022Trial
- Intense interval training in healthy older adults increases skeletal muscle [Physiological reports · 2017Trial
- Pathophysiological Roles of Two Intracellular P-Type ATPases: The Cancer-Associated NaInternational journal of molecular sciences · 2026Review
- Associations between skeletal muscle phenotype, positional role, and on-ice performance in elite male ice hockey players.Physiological reports · 2024Article
- AMPK and glucose deprivation exert an isoform-specific effect on the expression of NaJournal of muscle research and cell motility · 2024Article
- Inhibition of GSK3α,β rescues cognitive phenotypes in a preclinical mouse model of CTNNB1 syndrome.EMBO molecular medicine · 2024Article
- Sensational site: the sodium pump ouabain-binding site and its ligands.American journal of physiology. Cell physiology · 2024Review
- A century of exercise physiology: effects of muscle contraction and exercise on skeletal muscle NaEuropean journal of applied physiology · 2024Review
- Specific ATPases drive compartmentalized glycogen utilization in rat skeletal muscle.The Journal of general physiology · 2022Article
- Excitability properties of mouse and human skeletal muscle fibres compared by muscle velocity recovery cycles.Neuromuscular disorders : NMD · 2022Article
- Regulation of Cardiac Contractility by the Alpha 2 Subunit of the NaFrontiers in physiology · 2022Review
- The Na/K-ATPase α1/Src interaction regulates metabolic reserve and Western diet intolerance.Acta physiologica (Oxford, England) · 2021Article
- Tissue-specific regulatory mechanism of LncRNAs and methylation in sheep adipose and muscle induced by Allium mongolicum Regel extracts.Scientific reports · 2021Article
- Chronic Ouabain Prevents Na,K-ATPase Dysfunction and Targets AMPK and IL-6 in Disused Rat Soleus Muscle.International journal of molecular sciences · 2021Article
- NaMolecules (Basel, Switzerland) · 2021Review
- The role of AMPK in regulation of NaJournal of muscle research and cell motility · 2021Review
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Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The Na,K-ATPase α2 isozyme is the major Na,K-ATPase of mammalian skeletal muscle. This distribution is unique compared with most other cells, which express mainly the Na,K-ATPase α1 isoform, but its functional significance is not known. We developed a gene-targeted mouse (skα2(-/-)) in which the α2 gene (Atp1a2) is knocked out in the skeletal muscles, and examined the consequences for exercise performance, membrane potentials, contractility, and muscle fatigue. Targeted knockout was confirmed by genotyping, Western blot, and immunohistochemistry. Skeletal muscle cells of skα2(-/-) mice completely lack α2 protein and have no α2 in the transverse tubules, where its expression is normally enhanced. The α1 isoform, which is normally enhanced on the outer sarcolemma, is up-regulated 2.5-fold without change in subcellular targeting. skα2(-/-) mice are apparently normal under basal conditions but show significantly reduced exercise capacity when challenged to run. Their skeletal muscles produce less force, are unable to increase force to match demand, and show significantly increased susceptibility to fatigue. The impairments affect both fast and slow muscle types. The subcellular targeting of α2 to the transverse tubules is important for this role. Increasing Na,K-ATPase α1 content cannot fully compensate for the loss of α2. The increased fatigability of skα2(-/-) muscles is reproduced in control extensor digitorum longus muscles by selectively inhibiting α2 enzyme activity with ouabain. These results demonstrate that the Na,K-ATPase α2 isoform performs an acute, isoform-specific role in skeletal muscle. Its activity is regulated by muscle use and enables working muscles to maintain contraction and resist fatigue.
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Registered trials
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.