ArticleThe Journal of biological chemistry2012
Activation of AMP-activated protein kinase stimulates Na+,K+-ATPase activity in skeletal muscle cells.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 66 citations in OpenAlex.
- Exercise- and diet-induced glycogen depletion impairs performance during one-legged constant-load, high-intensity exercise in humans.Frontiers in physiology · 2025Article
- The Venom ofVeterinary sciences · 2024Article
- AMPK and glucose deprivation exert an isoform-specific effect on the expression of NaJournal of muscle research and cell motility · 2024Article
- A novel AMPK activator shows therapeutic potential in hepatocellular carcinoma by suppressing HIF1α-mediated aerobic glycolysis.Molecular oncology · 2022Article
- Phosphorylation of NaThe Journal of membrane biology · 2021Article
- Prenylflavonoids from fruit of Macaranga tanarius promote glucose uptake via AMPK activation in L6 myotubes.Journal of natural medicines · 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
- The role of AMPK in regulation of NaJournal of muscle research and cell motility · 2021Review
- Anti-NaScience advances · 2021Article
- MetforminFrontiers in physiology · 2021Article
- Article
- Critical Role for AMPK in Metabolic Disease-Induced Chronic Kidney Disease.International journal of molecular sciences · 2020Review
- AMPK controls the axonal regenerative ability of dorsal root ganglia sensory neurons after spinal cord injury.Nature metabolism · 2020Article
- AMPK alleviates high uric acid-induced NaExperimental & molecular medicine · 2019Article
- In vitro experimental models for examining the skeletal muscle cell biology of exercise: the possibilities, challenges and future developments.Pflugers Archiv : European journal of physiology · 2019Review
- Stimulation of NaOxidative medicine and cellular longevity · 2019Article
- AMP-Activated Protein Kinase as a Key Trigger for the Disuse-Induced Skeletal Muscle Remodeling.International journal of molecular sciences · 2018Review
- AMP-Activated Protein Kinase (AMPK)-Dependent Regulation of Renal Transport.International journal of molecular sciences · 2018Review
- DR region of NaScientific reports · 2018Article
- Regulation of hepatic NaMolecular and cellular biochemistry · 2018Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Contraction stimulates Na(+),K(+)-ATPase and AMP-activated protein kinase (AMPK) activity in skeletal muscle. Whether AMPK activation affects Na(+),K(+)-ATPase activity in skeletal muscle remains to be determined. Short term stimulation of rat L6 myotubes with the AMPK activator 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside (AICAR), activates AMPK and promotes translocation of the Na(+),K(+)-ATPase α(1)-subunit to the plasma membrane and increases Na(+),K(+)-ATPase activity as assessed by ouabain-sensitive (86)Rb(+) uptake. Cyanide-induced artificial anoxia, as well as a direct AMPK activator (A-769662) also increase AMPK phosphorylation and Na(+),K(+)-ATPase activity. Thus, different stimuli that target AMPK concomitantly increase Na(+),K(+)-ATPase activity. The effect of AICAR on Na(+),K(+)-ATPase in L6 myotubes was attenuated by Compound C, an AMPK inhibitor, as well as siRNA-mediated AMPK silencing. The effects of AICAR on Na(+),K(+)-ATPase were completely abolished in cultured primary mouse muscle cells lacking AMPK α-subunits. AMPK stimulation leads to Na(+),K(+)-ATPase α(1)-subunit dephosphorylation at Ser(18), which may prevent endocytosis of the sodium pump. AICAR stimulation leads to methylation and dephosphorylation of the catalytic subunit of the protein phosphatase (PP) 2A in L6 myotubes. Moreover, AICAR-triggered dephosphorylation of the Na(+),K(+)-ATPase was prevented in L6 myotubes deficient in PP2A-specific protein phosphatase methylesterase-1 (PME-1), indicating a role for the PP2A·PME-1 complex in AMPK-mediated regulation of Na(+),K(+)-ATPase. Thus contrary to the common paradigm, we report AMPK-dependent activation of an energy-consuming ion pumping process. This activation may be a potential mechanism by which exercise and metabolic stress activate the sodium pump in skeletal muscle.
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