Nongastric H-K-ATPase in rodent prostate: lobe-specific expression and apical localization.

@article{Pestov2002NongastricHI,
  title={Nongastric H-K-ATPase in rodent prostate: lobe-specific expression and apical localization.},
  author={Nikolay B. Pestov and Tatyana V. Korneenko and Gail Adams and Manoranjani P M Tillekeratne and Mikhail I. Shakhparonov and Nikolai N. Modyanov},
  journal={American journal of physiology. Cell physiology},
  year={2002},
  volume={282 4},
  pages={
          C907-16
        }
}
The molecular basis of active ion transport in secretory glands such as the prostate is not well characterized. Rat nongastric H-K-ATPase is expressed at high levels in distal colon surface cell apical membranes and thus is referred to as "colonic." Here we show that the ATPase is expressed in rodent prostate complex in a lobe-specific manner. RT-PCR and Western blot analyses indicate that rat nongastric H-K-ATPase alpha-subunit (alpha(ng)) mRNA and protein are present in coagulating gland… 
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TLDR
Results indicate that beta(1)-isoform functions as the authentic subunit of Na-K-ATPase and nongastric H-K -ATPases and that, in rat AP, alpha(ng) associates only with alpha(1), indicating that the intracellular polarization of X-k-atPase depends on interaction with other proteins.
Loss of acidification of anterior prostate fluids in Atp12a-null mutant mice indicates that nongastric H-K-ATPase functions as proton pump in vivo.
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Results show that nongastric H-K-ATPase is required for acidification of luminal prostate fluids, thereby providing a strong in vivo correlate of previous functional expression studies demonstrating that it operates as a proton pump.
An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization
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This work shows in transfected Madin-Darby canine kidney (MDCK) cells that the related non-gastric H,KATPase, ATP1AL1, does contain similar sorting motifs in close proximity to TM4, providing further evidence that the cellular distribution of P-type ATPases is determined by conformational sorted motifs.
Nongastric H,K‐ATPase: Structure and Functional Properties
TLDR
Analysis of human nongastric H,K‐ATPase expressed in Sf‐21 insect cells revealed that AL1/βHK exhibits substantial enzymatic activities in K‐free medium and K stimulates, but Na has inhibitory effect on ATP hydrolysis.
Regulation and hysiology of the H , K-ATPases in Kidney
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It is proposed that the gastric and colonic H ,K -ATPase participates importantly in the maintenance of chronic metabolic alkalosis.
Lobe-specific expression of phosphodiesterase 5 in rat prostate.
H-K-ATPase type 2: relevance for renal physiology and beyond.
  • G. Crambert
  • Biology
    American journal of physiology. Renal physiology
  • 2014
TLDR
The findings discussed in this review suggest that, as in the famous story, the ugly duckling of the X-K-ATPase family is actually a swan.
The Non-Gastric H+/K+ ATPase (ATP12A) Is Expressed in Mammalian Spermatozoa
TLDR
Results are consistent with those observed for the β1 subunit of Na+/K+ ATPase, suggesting that the latter may assemble with the α subunit to produce a functional ATP12A dimer in sperm cells, and hypothesize that ATP 12A may play a role in acrosome reactions.
Expression of the Non-gastric H+/K+ ATPase ATP12A in Normal and Pathological Human Prostate Tissue
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No significantly different expression levels could be detected in the various disease states compared to normal tissue, which contrasts the findings from immunohistochemistry and points to the possibility of altered post-translational processing and/or sorting of the protein.
Molecular regulation and physiology of the H+,K+ -ATPases in kidney.
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