ArticleMolecular and cellular biochemistry2007
Fiber specific differential phosphorylation of the alpha1-subunit of the Na(+),K (+)-ATPase in rat skeletal muscle: the effect of aging.
Article in Molecular and cellular biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Aging in the Skeletal Muscle Revealed by Molecular Immunohistochemical Imaging.International journal of molecular sciences · 2025Review
- Impaired AQP2 trafficking in Fxyd1 knockout mice: A role for FXYD1 in regulated vesicular transport.PloS one · 2017Article
- Effects of Age on Na(+),K(+)-ATPase Expression in Human and Rodent Skeletal Muscle.Frontiers in physiology · 2016Review
- Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1α.The Journal of membrane biology · 2011Article
- The alpha1 isoform of the Na+/K+ ATPase is up-regulated in dedifferentiated progenitor cells that mediate lens and retina regeneration in adult newts.Experimental eye research · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In skeletal muscle, the Na(+),K(+)-ATPase maintains the Na(+) and K(+) gradients and modulates contractile functions. The different fibers of the skeletal muscle possess diverse properties and functions, and thus, the demands for the Na-pump activity might be different. Because phosphorylation of the alpha1-subunit of the Na(+),K(+)-ATPase appears to serve a regulatory role in the activity of Na(+),K(+)-ATPase, we postulated that a difference in the phosphorylation of the alpha1-subunit may be found among the fibers. We utilized two well-characterized specific antibodies for the alpha1-subunit, namely the McK1 and alpha6F, to determine, by immunofluorescence, if the alpha1-subunit in rat skeletal muscle fiber is differentially phosphorylated. McK1 has the unique property that its binding to the alpha1-subunit is greatly reduced when Ser-18 is phosphorylated. Our data show that, in red gastrocnemius muscle, only a small number of the fibers were stained on the sarcolemmal membrane by McK1, while other fibers were almost completely devoid of any staining. By contrast, the staining pattern by McK1 in the white gastrocnemius muscle was mostly uniform. Immunostaining of serial sections using the alpha6F antibody showed that the alpha1-subunit is expressed in all fibers. Dephosphorylation of the tissue sections by phosphatase partially restored immunostaining of the alpha1-subunit by McK1. Fiber typing results showed that, in red gastrocnemius, those fibers stained positive for alpha1-subunit by McK1 are the Type I fibers, whereas those stained negative are the Type IIA, IID, and IIB fibers. With age, the number of fibers in red gastrocnemius stained positive for McK1 increased markedly in 30-month old rats compared to 6-month old rats. In conclusion, our result suggests that, in rats, the alpha1-subunit of the Na(+),K(+)-ATPase is differentially phosphorylated in the fibers of the red gastrocnemius muscle. Furthermore, advanced age is associated with an apparent decrease in the phosphorylation of the alpha1-subunit, in addition to the previously demonstrated increase in the levels of expression of the subunit.
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