pubmed.ncbi.nlm.nih.gov

Transcriptional regulators of Na,K-ATPase subunits - PubMed

  • ️Thu Jan 01 2015

Review

Transcriptional regulators of Na,K-ATPase subunits

Zhiqin Li et al. Front Cell Dev Biol. 2015.

Abstract

The Na,K-ATPase classically serves as an ion pump creating an electrochemical gradient across the plasma membrane that is essential for transepithelial transport, nutrient uptake and membrane potential. In addition, Na,K-ATPase also functions as a receptor, a signal transducer and a cell adhesion molecule. With such diverse roles, it is understandable that the Na,K-ATPase subunits, the catalytic α-subunit, the β-subunit and the FXYD proteins, are controlled extensively during development and to accommodate physiological needs. The spatial and temporal expression of Na,K-ATPase is partially regulated at the transcriptional level. Numerous transcription factors, hormones, growth factors, lipids, and extracellular stimuli modulate the transcription of the Na,K-ATPase subunits. Moreover, epigenetic mechanisms also contribute to the regulation of Na,K-ATPase expression. With the ever growing knowledge about diseases associated with the malfunction of Na,K-ATPase, this review aims at summarizing the best-characterized transcription regulators that modulate Na,K-ATPase subunit levels. As abnormal expression of Na,K-ATPase subunits has been observed in many carcinoma, we will also discuss transcription factors that are associated with epithelial-mesenchymal transition, a crucial step in the progression of many tumors to malignant disease.

Keywords: Na,K-ATPase α-subunit; Na,K-ATPase β-subunit; cancer; epigenetics; promoter analysis; transcription.

PubMed Disclaimer

Figures

Figure 1
Figure 1

Regulatory elements in the promoter regions of human Na,K-ATPase subunits. The promoter regions of human Na,K-ATPase are shown in the direction from 5′ to 3′. The colored boxes indicate potential transcription factor binding sites. The colored ovals represent experimentally verified transcription factor binding sites.

Similar articles

Cited by

References

    1. Adachi S., Zelenin S., Matsuo Y., Holtback U. (2004). Cellular response to renal hypoxia is different in adolescent and infant rats. Pediatr. Res. 55, 485–491. 10.1203/01.PDR.0000106805.54926.2C - DOI - PubMed
    1. Alvarez de la Rosa D., Avila J., Martín-Vasallo P. (2002). Chromatin structure analysis of the rat Na,K-ATPase beta2 gene 5'-flanking region. Int. J. Biochem. Cell Biol. 34, 632–644. 10.1016/S1357-2725(02)00006-7 - DOI - PubMed
    1. Avila J., Alvarez de la Rosa D., González-Martínez L. M., Lecuona E., Martín-Vasallo P. (1998). Structure and expression of the human Na,K-ATPase beta 2-subunit gene. Gene 208, 221–227. 10.1016/S0378-1119(97)00661-6 - DOI - PubMed
    1. Azuma K. K., Hensley C. B., Tang M. J., McDonough A. A. (1993). Thyroid hormone specifically regulates skeletal muscle Na(+)-K(+)-ATPase alpha 2- and beta 2-isoforms. Am. J. Physiol. 265(3 Pt 1), C680–C687. - PubMed
    1. Bajpai M., Chaudhury S. (1999). Transcriptional and post-transcriptional regulation of Na+,K(+)-ATPase alpha isoforms by thyroid hormone in the developing rat brain. Neuroreport 10, 2325–2328. 10.1097/00001756-199908020-00019 - DOI - PubMed

Publication types