Distinct α2 Na,K-ATPase membrane pools are differently involved in early skeletal muscle remodeling during disuse
| Autor: | Elena V. Bouzinova, Alexander N. Vasiliev, Boubacar Benziane, Judith A. Heiny, Vladimir V. Matchkov, Alexey M. Petrov, Andrey L. Zefirov, Igor I. Krivoi, Alexander V. Chibalin, V. V. Kravtsova |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Male medicine.medical_specialty Physiology Phospholemman Biology Receptors Nicotinic Membrane Potentials 03 medical and health sciences Sarcolemma Membrane region Internal medicine medicine Animals Na+/K+-ATPase Phosphorylation Rats Wistar Muscle Skeletal Research Articles Membrane potential Soleus muscle Skeletal muscle Membrane Proteins Phosphoproteins Rats Isoenzymes 030104 developmental biology medicine.anatomical_structure Endocrinology medicine.symptom Sodium-Potassium-Exchanging ATPase Muscle contraction Muscle Contraction |
| Zdroj: | The Journal of General Physiology Kravtsova, V, Petrov, A M, Matchkov, V, Bouzinova, E, Vasiliev, A N, Benziane, B, Zefirov, A L, Chibalin, A V, Heiny, J A & Krivoi, II 2016, ' Distinct alpha2 Na,K-ATPase membrane pools are differently involved in early skeletal muscle remodeling during disuse ', Journal of General Physiology, vol. 147, no. 2, pp. 175-188 . https://doi.org/10.1085/jgp.201511494 |
| ISSN: | 1540-7748 0022-1295 |
| Popis: | Location, location, location. The Na-K pump of skeletal muscle is regulated differently at neuromuscular junctions. The Na,K-ATPase is essential for the contractile function of skeletal muscle, which expresses the α1 and α2 subunit isoforms of Na,K-ATPase. The α2 isozyme is predominant in adult skeletal muscles and makes a greater contribution in working compared with noncontracting muscles. Hindlimb suspension (HS) is a widely used model of muscle disuse that leads to progressive atrophy of postural skeletal muscles. This study examines the consequences of acute (6–12 h) HS on the functioning of the Na,K-ATPase α1 and α2 isozymes in rat soleus (disused) and diaphragm (contracting) muscles. Acute disuse dynamically and isoform-specifically regulates the electrogenic activity, protein, and mRNA content of Na,K-ATPase α2 isozyme in rat soleus muscle. Earlier disuse-induced remodeling events also include phospholemman phosphorylation as well as its increased abundance and association with α2 Na,K-ATPase. The loss of α2 Na,K-ATPase activity results in reduced electrogenic pump transport and depolarized resting membrane potential. The decreased α2 Na,K-ATPase activity is caused by a decrease in enzyme activity rather than by altered protein and mRNA content, localization in the sarcolemma, or functional interaction with the nicotinic acetylcholine receptors. The loss of extrajunctional α2 Na,K-ATPase activity depends strongly on muscle use, and even the increased protein and mRNA content as well as enhanced α2 Na,K-ATPase abundance at this membrane region after 12 h of HS cannot counteract this sustained inhibition. In contrast, additional factors may regulate the subset of junctional α2 Na,K-ATPase pool that is able to recover during HS. Notably, acute, low-intensity muscle workload restores functioning of both α2 Na,K-ATPase pools. These results demonstrate that the α2 Na,K-ATPase in rat skeletal muscle is dynamically and acutely regulated by muscle use and provide the first evidence that the junctional and extrajunctional pools of the α2 Na,K-ATPase are regulated differently. |
| Databáze: | OpenAIRE |
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