Ouabain‐sensitive H,K‐ATPase: tissue‐specific expression of the mammalian genes encoding the catalytic α subunit 1

  title={Ouabain‐sensitive H,K‐ATPase: tissue‐specific expression of the mammalian genes encoding the catalytic $\alpha$ subunit
  author={Nikolay B. Pestov and Ludmila G Romanova and Tatyana V. Korneenko and Maxim V. Egorov and Maria B Kostina and Vladimir E. Sverdlov and Amir Askari and Mikhail I. Shakhparonov and Nikolai N. Modyanov},
  journal={FEBS Letters},
The βm protein, a member of the X, K-ATPase β-subunits family, is located intracellularly in pig skeletal muscle
Abstract The sequence of the pig cDNA encoding the muscle-specific βm-protein, a member of the X,K-ATPase β-subunits family, was determined. Two alternatively spliced transcripts encoding polypeptide
Nongastric H,K‐ATPase: Structure and Functional Properties
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.
Identification of the beta-subunit for nongastric H-K-ATPase in rat anterior prostate.
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.
Immunochemical demonstration of a novel beta-subunit isoform of X, K-ATPase in human skeletal muscle.
The existence of the predicted protein, designated as beta(m) (beta(muscle), in human adult skeletal muscle membranes is demonstrated using immunoblotting withbeta(m)-specific antibodies generated against recombinant polypeptide formed by extramembrane beta( m) domains.
Loss of acidification of anterior prostate fluids in Atp12a-null mutant mice indicates that nongastric H-K-ATPase functions as proton pump in vivo.
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.
Human Nongastric H,K-ATPase: Current View On Structure And Functional Properties
The recently discovered catalytic a-subunits of nongastric H,K-ATPases encoded by the human ATP1 AL1 (alternative name ATP12A) gene and its animal homologues represent the third distinct group.
The Putative Role of the Non-Gastric H+/K+-ATPase ATP12A (ATP1AL1) as Anti-Apoptotic Ion Transporter: Effect of the H+/K+ ATPase Inhibitor SCH28080 on Butyrate-Stimulated Myelomonocytic HL-60 Cells
It is found by RT-PCR, intracellular pH measurements, MCV measurements and flow cytometry that ATP12A is expressed in human myelomonocytic HL-60 cells and is a functionally active H+/K+ ATPase that may counteract events during early apoptosis like intrACEllular acidosis, loss of intrace cellular K+ ions and apoptotic volume decrease.


Human ATP1AL1 gene encodes a ouabain-sensitive H-K-ATPase.
It is argued that ATP1AL1 is the catalytic alpha-subunit of a human nongastric P-type ATPase capable of exchanging extracellular potassium for intracellular protons.
Genomic organization of the human ATP1AL1 gene encoding a ouabain-sensitive H,K-ATPase.
It is suggested that the ATP1AL1 gene contains two poly(A) addition sites that may function in a tissue-specific manner that meets the structural criteria of a CpG island.
Functional expression of putative H+-K+-ATPase from guinea pig distal colon.
It is concluded that the cDNA encodes the catalytic subunit (α-subunit) of the colonic H+-K+-ATPase, which is found to act as a surrogate for the Colonic β-sub unit for the functional expression of the ATPase.
H+, K(+)-ATPASE in the kidney: localization and function in the nephron.
Data is summarized with a special emphasis on those which demonstrate the existence along the mammalian nephron of several forms of H+, K(+)-ATPase displaying distinct biochemical, pharmacological and functional properties.
Increased sensitivity to K+ deprivation in colonic H,K-ATPase-deficient mice.
Results demonstrate that, during K+ deprivation, cHKA plays a critical role in the maintenance of K+ homeostasis in vivo.
Microglia generate external proton and potassium ion gradients utilizing a member of the H/K ATPase family
This is a first report of an H+/K+ transporter in microglia cells with a Kd in the physiological range of [K+]out, and it is suggested that a K/H ATPase is the major generator of both the potassium and the proton gradients.
Extracellular potassium in the mammalian central nervous system.
  • G. Somjen
  • Biology
    Annual review of physiology
  • 1979
There has been a new surge of interest in the functional significance of potassium distribution in the nervous system and the recent development of potassium-selective microelectrodes is supplemented by consulting more general reviews on brain electrolytes.