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This Article Full Text Full Text (PDF) All Versions of this Article: 286/6/C1229    most recent 00393.2003v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (5) Citing Articles via Google Scholar Google Scholar Articles by Pestov, N. B. Articles by Modyanov, N. N. Search for Related Content PubMed PubMed Citation Articles by Pestov, N. B. Articles by Modyanov, N. N.

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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