Coexpression of alpha 1 with putative beta 3 subunits results in functional Na+/K+ pumps in Xenopus oocytes

Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8397-400. doi: 10.1073/pnas.88.19.8397.

Abstract

The active Na+/K+ pump is composed of an alpha and a beta subunit. Until now, three putative isoforms of the beta subunit have been identified that share sequence similarity. We have expressed the beta 1 and beta 3 isoforms of Xenopus laevis Na+/K(+)-ATPase in Xenopus oocytes to compare functional properties of the Na+/K+ pump, including either of these two isoforms. Na+/K+ pump current, estimated as K(+)-induced outward current in voltage-clamped oocytes, was doubled by coexpression of alpha 1 subunits with either isoform of the beta subunit compared to expression of alpha 1 subunits alone. The kinetics of activation by external K+ and the voltage dependence of the electrogenic activity of the Na+/K+ pump were similar with both beta isoforms, indicating that both beta 1 and beta 3 isoforms can support expression at the oocyte surface of an active Na+/K+ pump with similar functional properties.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport, Active
  • Cell Membrane / enzymology
  • Electric Conductivity
  • In Vitro Techniques
  • Ion Channels / chemistry*
  • Ion Channels / physiology
  • Kinetics
  • Membrane Potentials
  • Oocytes
  • Potassium / pharmacology
  • Recombinant Proteins
  • Sodium-Potassium-Exchanging ATPase / chemistry*
  • Sodium-Potassium-Exchanging ATPase / physiology
  • Strophanthidin / pharmacology
  • Structure-Activity Relationship
  • Xenopus laevis

Substances

  • Ion Channels
  • Recombinant Proteins
  • Strophanthidin
  • Sodium-Potassium-Exchanging ATPase
  • Potassium