Bufo marinus bladder H-K-ATPase carries out electroneutral ion transport

Abstract

Bufo marinus bladder H-K-ATPase belongs to the Na-K-ATPase and H-K-ATPase subfamily of oligomeric P-type ATPases and is closely related to rat and human nongastric H-K-ATPases. It has been demonstrated that this ATPase transports K+ into the cell in exchange for protons and sodium ions, but the stoichiometry of this cation exchange is not yet known. We studied the electrogenic properties of B. marinus bladder H-K-ATPase expressed in Xenopus laevis oocytes. In a HEPES-buffered solution, K+ activation of the H-K-ATPase induced a slow-onset inward current that reached an amplitude of ∼20 nA after 1–2 min. When measurements were performed in a solution containing 25 mM HCO[Formula: see text] at a Pco 2 of 40 Torr, the negative current activated by K+ was reduced. In noninjected oocytes, intracellular alkalization activated an inward current similar to that due to B. marinus H-K-ATPase. We conclude that the transport activity of the nongastric B. marinus H-K-ATPase is not intrinsically electrogenic but that the inward current observed in oocytes expressing this ion pump is secondary to intracellular alkalization induced by proton transport.