Renal Na-K-ATPase: its role in tubular sodium and potassium transport.

Abstract

Na-K-ATPase, the enzymatic equivalent of the sodium:potassium pump, is found in large amounts in the kidney, and this organ has figured prominently both as a source for the purification of the enzyme and as a target for the study of its properties. Located on the basolateral aspect of tubule cells, renal Na-K-ATPase plays a key role in the active translocation of Na and K across this membrane as well as in the "secondary active" transport of a number of other solutes. The activity of renal Na-K-ATPase varies in parallel with sustained changes in Na or K transport, indicating the participation of this enzyme in the chronic adaptation of the kidney to altered Na reabsorption or K secretory load. Because of its slow turnover, however, the role of Na-K-ATPase in the modulation of acute changes in cation transport is unclear. Several hormones and vanadate influence renal Na-K-ATPase activity, and their importance as potential physiologic regulators of this enzyme is examined. Most of the information on the renal enzyme has been obtained from studies using homogenates or subcellular fractions thereof, but more recently the development of tubule microdissection and microanalytic methods has made possible the study of Na-K-ATPase in single nephron segments. This approach has opened new possibilities for evaluating the role of this enzyme in kidney function by facilitating correlation of enzyme activity with transport events in the same structure and by enabling us to focus the study of Na-K-ATPase on discrete anatomic subdivisions of the functionally heterogeneous nephron.