Regulatory function of the Na,K-ATPase α2-isoform

Кривой, И. И.

doi:10.1134/s0006350912050119

Cited by 6 publications

(10 citation statements)

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“…The α 1 and α 2 isoforms of Na,K-ATPase are coexpressed in the skeletal muscles [ 18 ]. The α 2 isoform is the major α subunit and displays marked adaptability compared to the α 1 isoform [ 14 , 16 , 17 ]. Recent studies of the role of the α 2 Na,K-ATPase suggest that the α 2 isoform is essential for the contractile function of skeletal muscle and that its specific transport activity can be acutely regulated by muscle activity [ 25 , 28 , 35 – 37 ].…”

Section: Discussionmentioning

confidence: 99%

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Isoform-Specific Na,K-ATPase Alterations Precede Disuse-Induced Atrophy of Rat Soleus Muscle

Кравцова

Matchkov

Bouzinova

et al. 2015

BioMed Research International

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This study examines the isoform-specific effects of short-term hindlimb suspension (HS) on the Na,K-ATPase in rat soleus muscle. Rats were exposed to 24–72 h of HS and we analyzed the consequences on soleus muscle mass and contractile parameters; excitability and the resting membrane potential (RMP) of muscle fibers; the electrogenic activity, protein, and mRNA content of the α1 and α2 Na,K-ATPase; the functional activity and plasma membrane localization of the α2 Na,K-ATPase. Our results indicate that 24–72 h of HS specifically decreases the electrogenic activity of the Na,K-ATPase α2 isozyme and the RMP of soleus muscle fibers. This decrease occurs prior to muscle atrophy or any change in contractile parameters. The α2 mRNA and protein content increased after 24 h of HS and returned to initial levels at 72 h; however, even the increased content was not able to restore α2 enzyme activity in the disused soleus muscle. There was no change in the membrane localization of α2 Na,K-ATPase. The α1 Na,K-ATPase electrogenic activity, protein and mRNA content did not change. Our findings suggest that skeletal muscle use is absolutely required for α2 Na,K-ATPase transport activity and provide the first evidence that Na,K-ATPase alterations precede HS-induced muscle atrophy.

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Section: Discussionmentioning

confidence: 99%

“…Four isoforms of the α subunit are known to exist in tissues of vertebrates. It is generally accepted that the ubiquitous α 1 isoform plays the main “house-keeping” role while the other isoforms are expressed in a cell- and tissue-specific manner and possesses additional regulatory functions [ 12 – 14 ].…”

Section: Introductionmentioning

confidence: 99%

Isoform-Specific Na,K-ATPase Alterations Precede Disuse-Induced Atrophy of Rat Soleus Muscle

Кравцова

Matchkov

Bouzinova

et al. 2015

BioMed Research International

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“…In some tissues, e.g., erythrocytes, kidney epithelia and liver, the α1 isoform is the only isoform expressed, while the majority of other cell types co-expressed other α isoforms serving additional regulatory functions that often are poorly understood. Thus, the α2 isoform is principally expressed in skeletal, cardiac and smooth muscles as well as in glial cells while the α3 isoform is characteristic for neuronal tissues (Blanco and Mercer, 1998 ; Mobasheri et al, 2000 ; Dobretsov and Stimers, 2005 ; Krivoi, 2012 ; Li and Langhans, 2015 ). The α4 isoform has been found only in testis (Woo et al, 2000 ).…”

Section: Molecular Diversity Of Nak-atpasementioning

confidence: 99%

Specialized Functional Diversity and Interactions of the Na,K-ATPase

Matchkov

Кривой

2016

Front. Physiol.

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Na,K-ATPase is a protein ubiquitously expressed in the plasma membrane of all animal cells and vitally essential for their functions. A specialized functional diversity of the Na,K-ATPase isozymes is provided by molecular heterogeneity, distinct subcellular localizations, and functional interactions with molecular environment. Studies over the last decades clearly demonstrated complex and isoform-specific reciprocal functional interactions between the Na,K-ATPase and neighboring proteins and lipids. These interactions are enabled by a spatially restricted ion homeostasis, direct protein-protein/lipid interactions, and protein kinase signaling pathways. In addition to its “classical” function in ion translocation, the Na,K-ATPase is now considered as one of the most important signaling molecules in neuronal, epithelial, skeletal, cardiac and vascular tissues. Accordingly, the Na,K-ATPase forms specialized sub-cellular multimolecular microdomains which act as receptors to circulating endogenous cardiotonic steroids (CTS) triggering a number of signaling pathways. Changes in these endogenous cardiotonic steroid levels and initiated signaling responses have significant adaptive values for tissues and whole organisms under numerous physiological and pathophysiological conditions. This review discusses recent progress in the studies of functional interactions between the Na,K-ATPase and molecular microenvironment, the Na,K-ATPase-dependent signaling pathways and their significance for diversity of cell function.

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“…Four isoforms of the α-subunit are known to exist in tissues of vertebrates. It is generally accepted that the ubiquitous α1 isoform plays the main housekeeping role, whereas the other isoforms are expressed in a cell- and tissue-specific manner and possess additional regulatory functions that are still poorly understood ( Blanco and Mercer, 1998 ; Geering, 2008 ; Krivoĭ, 2012 ).…”

Section: Introductionmentioning

confidence: 99%