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J Biol Chem, Vol. 273, Issue 43, 27772-27778, October 23, 1998

ATP1AL1, a Member of the Non-gastric H,K-ATPase Family, Functions as a Sodium Pump

From the Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06520

The human ATP1AL1-encoded protein (an  subunit of the human non-gastric H,K-ATPase) has previously been shown to assemble with the gastric H,K-ATPase  subunit (gH,K) to form a functionally active ionic pump in HEK 293 cells. This pump has been found to be sensitive to both SCH 28080 and ouabain. However, the ⁸⁶Rb⁺-influx mediated by the ATP1AL1-gH,K heterodimer in HEK 293 cells is at least 1 order of magnitude larger than the maximum ouabain-sensitive proton efflux detected in the same cells. In this study we find that the intracellular Na⁺ content in cells expressing ATP1AL1 and gH,K is two times lower than that in control HEK 293 cells in response to incubation for 3 h in the presence of 1 µM ouabain. Moreover, analysis of net Na⁺ efflux in HEK 293 expressing the ATP1AL1-gH,K heterodimer reveals the presence of Na⁺ extrusion activity that is not sensitive to 1 µM ouabain but can be inhibited by 1 mM of this drug. In contrast, ouabain-inhibitable Na⁺ efflux in control HEK 293 cells is similarly sensitive to either 1 µM or 1 mM ouabain. Finally, ⁸⁶Rb⁺ influx through the ATP1AL1-gH,K complex is comparable to the 1 mM ouabain-sensitive Na⁺ efflux in the same cells. The data presented here suggest that the enzyme formed by ATP1AL1 and the gastric H,K-ATPase  subunit in HEK 293 cells mediates primarily Na⁺,K⁺ rather than H⁺,K⁺ exchange.

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