Rapid resting ion fluxes in goldfish hair cells are balanced by (Na+,K+)-ATPase

Hear Res. 1993 Oct;70(1):22-30. doi: 10.1016/0378-5955(93)90049-7.

Abstract

Inhibition of sodium/potassium pumping by isolated goldfish hair cells led to a rapid gain of sodium and loss of potassium. Half-times for turnover were about 10 min, among the fastest of any cell type examined by electron-probe analysis. Pumping was inhibited by removal of extracellular potassium or by treatment with 1 mM ouabain, as expected of a classical (Na+,K+)-ATPase. The initial rate of entry of sodium after inhibition, about 4 mM/min, provided an estimate of resting sodium-entry and sodium-pumping rates. After return to control medium, cells loaded with sodium by removal of extracellular potassium could recover their normal high-potassium/low-sodium status. The initial rate of recovery (an estimate of the cells' maximum sodium-pumping rate) was sufficient to lower cell sodium by 10 mM/min. This functional estimate of hair-cell (Na+,K+)-ATPase activity was of the same order of magnitude as the biochemical activity of (Na+,K+)-ATPase previously reported for sensory epithelia of other species. The balance between sodium entry and sodium pumping determines hair-cell ionic composition, and thus the resting potential and the driving forces for sodium-coupled transport processes. Imbalance due to excess sodium entry or loss of pump capacity could have significant consequences for hair-cell function and integrity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Chlorides / metabolism
  • Goldfish / metabolism*
  • Hair Cells, Auditory / drug effects
  • Hair Cells, Auditory / metabolism*
  • Hair Cells, Auditory / physiology
  • In Vitro Techniques
  • Ion Transport
  • Kinetics
  • Ouabain / pharmacology
  • Sodium-Potassium-Exchanging ATPase / antagonists & inhibitors
  • Sodium-Potassium-Exchanging ATPase / drug effects
  • Sodium-Potassium-Exchanging ATPase / metabolism*
  • Sodium-Potassium-Exchanging ATPase / physiology

Substances

  • Chlorides
  • Ouabain
  • Adenosine Triphosphate
  • Sodium-Potassium-Exchanging ATPase