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

@article{Pestov1998OuabainsensitiveHT,
  title={Ouabain‐sensitive H,K‐ATPase: tissue‐specific expression of the mammalian genes encoding the catalytic $\alpha$ subunit
1},
  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},
  year={1998},
  volume={440}
}
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38 Citations
Background Citations
5
Methods Citations
3

38 Citations

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
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.
Identification of a novel gene of the X,K‐ATPase β‐subunit family that is predominantly expressed in skeletal and heart muscles 1
Identification of the beta-subunit for nongastric H-K-ATPase in rat anterior prostate.
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.
Non-gastric H+/K+ ATPase is present in the microvillous membrane of the human placental syncytiotrophoblast.
Immunochemical demonstration of a novel beta-subunit isoform of X, K-ATPase in human skeletal muscle.
TLDR
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.
TLDR
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
TLDR
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.
Gastric proton pump is expressed in the inner ear and choroid plexus of the rat
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
TLDR
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.
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References

SHOWING 1-10 OF 25 REFERENCES
The family of human Na,K‐ATPase genesATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase
Human ATP1AL1 gene encodes a ouabain-sensitive H-K-ATPase.
TLDR
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.
TLDR
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.
Cloning and characterization of the entire cDNA encoded by ATP1AL1 — a member of the human Na,K/H,K‐ATPase gene family
Functional expression of putative H+-K+-ATPase from guinea pig distal colon.
TLDR
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.
TLDR
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.
Isolation and characterization of a cDNA encoding the putative distal colon H+,K(+)-ATPase. Similarity of deduced amino acid sequence to gastric H+,K(+)-ATPase and Na+,K(+)-ATPase and mRNA expression in distal colon, kidney, and uterus.
Increased sensitivity to K+ deprivation in colonic H,K-ATPase-deficient mice.
TLDR
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
TLDR
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
TLDR
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.
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