ArticlePloS one2014
Purinergic effects on Na,K-ATPase activity differ in rat and human skeletal muscle.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Vanillin modulates activities linked to dysmetabolism in psoas muscle of diabetic rats.Scientific reports · 2021Article
- Muscle Glycogen Metabolism and High-Intensity Exercise Performance: A Narrative Review.Sports medicine (Auckland, N.Z.) · 2021Review
- Limitations in intense exercise performance of athletes - effect of speed endurance training on ion handling and fatigue development.The Journal of physiology · 2017Review
- β-Adrenergic modulation of skeletal muscle contraction: key role of excitation-contraction coupling.The Journal of physiology · 2015Review
- The effect of exercise and beta2-adrenergic stimulation on glutathionylation and function of the Na,K-ATPase in human skeletal muscle.Physiological reports · 2015Article
- β2-adrenergic stimulation enhances Ca2+ release and contractile properties of skeletal muscles, and counteracts exercise-induced reductions in Na+-K+-ATPase Vmax in trained men.The Journal of physiology · 2014Article
- Oxidative stress (glutathionylation) and Na,K-ATPase activity in rat skeletal muscle.PloS one · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundP2Y receptor activation may link the effect of purines to increased maximal in vitro activity of the Na,K-ATPase in rat muscle. The hypothesis that a similar mechanism is present in human skeletal muscle was investigated with membranes from rat and human skeletal muscle.
resultsMembranes purified from rat and human muscles were used in the Na,K-ATPase assay. Incubation with ADP, the stable ADP analogue MeS-ADP and UDP increased the Na+ dependent Na,K-ATPase activity in rat muscle membranes, whereas similar treatments of human muscle membranes lowered the Na,K-ATPase activity. UTP incubation resulted in unchanged Na,K-ATPase activity in humans, but pre-incubation with the antagonist suramin resulted in inhibition with UTP, suggesting that P2Y receptors are involved. The Na,K-ATPase in membranes from both rat and human could be stimulated by protein kinase A and C activation. Thus, protein kinase A and C activation can increase Na,K-ATPase activity in human muscle but not via P2Y receptor stimulation.
conclusionThe inhibitory effects of most purines (with the exception of UTP) in human muscle membranes are probably due to mass law inhibition of ATP hydrolysis. This inhibition could be blurred in rat due to receptor mediated activation of the Na,K-ATPase. The different effects could be related to a high density of ADP sensitive P2Y1 and P2Y13 receptors in rat, whereas the UTP sensitive P2Y11 could be more abundant in human. Alternatively, rat could possesses a mechanism for protein-protein interaction between P2Y receptors and the Na,K-ATPase, and this mechanism could be absent in human skeletal muscle (perhaps with the exception of the UTP sensitive P2Y11 receptor). PERSPECTIVE: Rat muscle is not a reliable model for purinergic effects on Na,K-ATPase in human skeletal muscle.
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