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MEMBRANE TRANSPORTERS, ION CHANNELS, AND PUMPS

Identification of the -subunit for nongastric H-K-ATPase in rat anterior prostate

¹Department of Pharmacology, Medical College of Ohio, Toledo, Ohio 43614; and ²Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117871, Russia

Submitted 15 September 2003 ; accepted in final form 26 January 2004

The structural organization of nongastric H-K-ATPase, unlike that of closely related Na-K-ATPase and gastric H-K-ATPase, is not well characterized. Recently, we demonstrated that nongastric H-K-ATPase -subunit (_ng) is expressed in apical membranes of rodent prostate. Its highest level, as well as relative abundance, with respect to ₁-isoform of Na-K-ATPase, was observed in anterior lobe. Here, we aimed to determine the subunit composition of nongastric H-K-ATPase through the detailed analysis of the expression of all known X-K-ATPase -subunits in rat anterior prostate (AP). RT-PCR detects transcripts of -subunits of Na-K-ATPase only. Measurement of absolute protein content of these three -subunit isoforms, with the use of quantitative Western blotting of AP membrane proteins, indicates that the abundance order is ₁ > ₃ >> ₂. Immunohistochemical experiments demonstrate that ₁ is present predominantly in apical membranes, coinciding with _ng, whereas ₃ is localized in the basolateral compartment, coinciding with ₁. This is the first direct demonstration of the _ng-₁ colocalization in situ indicating that, in rat AP, _ng associates only with ₁. The existence of _ng-1 complex has been confirmed by immunoprecipitation experiments. These results indicate that ₁-isoform functions as the authentic subunit of Na-K-ATPase and nongastric H-K-ATPase. Putatively, the intracellular polarization of X-K-ATPase isoforms depends on interaction with other proteins.

ATP1AL1; ATP12A; ATP1B1; X-potassium-adenosine triphosphatase; hydrogen-potassium-adenosine triphosphatase; sodium-potassium-adenosine triphosphatase; male accessory glands; potassium transport

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