ArticleThe Journal of membrane biology2010
Regulation of human and pig renal Na(+),K (+)-ATPase activity by tyrosine phosphorylation of their alpha(1)-subunits.
Article in The Journal of membrane biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Phosphorylation of NaThe Journal of membrane biology · 2021Article
- Regulation of Neuronal NaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Unique Regulation of Na-K-ATPase during Growth and Maturation of Intestinal Epithelial Cells.Cells · 2019Article
- The effect of endothelin-1 on Src-family tyrosine kinases and Na,K-ATPase activity in porcine lens epithelium.Journal of cellular physiology · 2011Article
- Regulation and identification of Na,K-ATPase alpha1 subunit phosphorylation in rat parotid acinar cells.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modulation of the physiologically influential Na(+),K(+)-ATPase is a complex process involving a wide variety of factors. To determine the possible effects of the protein tyrosine phosphatase (PTP) inhibitors dephostatin and Et-3,4-dephostatin on human and pig, renal cells and enzymatic extracts, we treated our samples (15 min-24 h) with those PTP inhibitors (0-100 microM). PTP inhibitors were found to possess a concentration-dependent inhibition of Na(+),K(+)-ATPase activity in both human and pig samples. The inhibition was similarly demonstrated on all cellular, microsomal fraction and purified Na(+),K(+)-ATPase levels. Despite rigorous activity recovery attempts, the PTP inhibitors' effects were sustained on Na(+),K(+)-ATPase activity. Western blotting experiments revealed the expression of both alpha(1)- and beta(1)-subunits in both human and pig tissues. alpha(1)-Subunits possessed higher tyrosine phosphorylation levels with higher concentrations of PTP inhibitors. Meanwhile, serine/threonine residues of both alpha(1)- and beta(1)-subunits demonstrated diminished phosphorylation levels upon dephostatin treatment. Accordingly, we provide evidence that Na(+),K(+)-ATPase can be regulated through tyrosine phosphorylation of primarily their alpha(1)-subunits, using PTP inhibitors.
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