Identification of the β-subunit for nongastric H-K-ATPase in rat anterior prostate Article (Web of Science)


  • 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 α-subunit (αng) is expressed in apical membranes of rodent prostate. Its highest level, as well as relative abundance, with respect to α1-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 β-subunits in rat anterior prostate (AP). RT-PCR detects transcripts of β-subunits of Na-K-ATPase only. Measurement of absolute protein content of these three β-subunit isoforms, with the use of quantitative Western blotting of AP membrane proteins, indicates that the abundance order is β1> β3≫ β2. Immunohistochemical experiments demonstrate that β1is present predominantly in apical membranes, coinciding with αng, whereas β3is localized in the basolateral compartment, coinciding with α1. This is the first direct demonstration of the αng1colocalization in situ indicating that, in rat AP, αngassociates only with β1. The existence of αng-β1complex has been confirmed by immunoprecipitation experiments. These results indicate that β1-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.


  • Pestov, Nikolay B.
  • Korneenko, Tatyana V.
  • Radkov, Rossen
  • Zhao, Hao
  • Shakhparonov, Mikhail I.
  • Modyanov, Nikolai

publication date

  • 2004

start page

  • C1229

end page

  • C1237


  • 286


  • 6