ArticleEuropean journal of oral sciences2014
Gene-expression profile and localization of Na+/K(+)-ATPase in rat enamel organ cells.
Article in European journal of oral sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Prenatal exposure to gestational diabetes mellitus increases developmental defects in the enamel of offspring.PloS one · 2019Trial
- Article
- Review
- The Importance of Connexin 43 in Enamel Development and Mineralization.Frontiers in physiology · 2018Article
- Enamel: Molecular identity of its transepithelial ion transport system.Cell calcium · 2017Review
- Cytotoxic effect of zinc oxide nanoparticles on murine photoreceptor cells via potassium channel block and NaCell proliferation · 2017Article
- Multiple Calcium Export Exchangers and Pumps Are a Prominent Feature of Enamel Organ Cells.Frontiers in physiology · 2017Article
- NBCe1 (SLC4A4) a potential pH regulator in enamel organ cells during enamel development in the mouse.Cell and tissue research · 2014Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The sodium pump Na(+)/K(+)-ATPase, expressed in virtually all cells of higher organisms, is involved in establishing a resting membrane potential and in creating a sodium gradient to facilitate a number of membrane-associated transport activities. Na(+)/K(+)-ATPase is an oligomer of α, β, and γ subunits. Four unique genes encode each of the α and β subunits. In dental enamel cells, the spatiotemporal expression of Na(+)/K(+)-ATPase is poorly characterized. Using the rat incisor as a model, this study provides a comprehensive expression profile of all four α and all four β Na(+)/K(+)-ATPase subunits throughout all stages of amelogenesis. Real-time PCR, western blot analysis, and immunolocalization revealed that α1, β1, and β3 are expressed in the enamel organ and that all three are most highly expressed during late-maturation-stage amelogenesis. Expression of β3 was significantly higher than expression of β1, suggesting that the dominant Na(+)/K(+)-ATPase consists of an α1β3 dimer. Localization of α1, β1, and β3 subunits in ameloblasts was primarily to the cytoplasm and occasionally along the basolateral membranes. Weaker expression was also noted in papillary layer cells during early maturation. Our data support that Na(+)/K(+)-ATPase is functional in maturation-stage ameloblasts.
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