FXYD3 facilitates Na+ and liquid absorption across human airway epithelia by increasing the transport capacity of the Na/K ATPase

Am J Physiol Cell Physiol. 2022 Oct 1;323(4):C1044-C1051. doi: 10.1152/ajpcell.00047.2022. Epub 2022 Aug 22.

Abstract

Na/K ATPase activity is essential for ion transport across epithelia. FXYD3, a γ subunit of the Na/K ATPase, is expressed in the airway, but its function remains undetermined. Single-cell RNA sequencing and immunohistochemistry revealed that FXYD3 localizes within the basolateral membrane of all airway epithelial cells. To study FXYD3 function, we reduced FXYD3 expression using siRNA. After permeabilizing the apical membrane with nystatin, epithelia pretreated with FXYD3-targeting siRNA had lower ouabain-sensitive short-circuit currents than control epithelia. FXYD3-targeting siRNA also reduced amiloride-sensitive short-circuit currents and liquid absorption across intact epithelia. These data are consistent with FXYD3 facilitating Na+ and liquid absorption. FXYD3 may be needed to maintain the high rates of Na+ and fluid absorption observed for airway and other FXYD3-expressing epithelia.

Keywords: airway; epithelia; ion transport.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, N.I.H., Extramural

MeSH terms

  • Amiloride*
  • Humans
  • Membrane Proteins / metabolism
  • Neoplasm Proteins / metabolism
  • Nystatin
  • Ouabain*
  • RNA, Small Interfering / genetics
  • Sodium / metabolism
  • Sodium-Potassium-Exchanging ATPase / genetics
  • Sodium-Potassium-Exchanging ATPase / metabolism

Substances

  • FXYD3 protein, human
  • Membrane Proteins
  • Neoplasm Proteins
  • RNA, Small Interfering
  • Nystatin
  • Ouabain
  • Amiloride
  • Sodium
  • Sodium-Potassium-Exchanging ATPase