The family of human Na,K‐ATPase genesATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase
@article{Modyanov1991TheFO, title={The family of human Na,K‐ATPase genesATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase}, author={Nikolai N. Modyanov and K. E. Petrukhin and Vladimir E. Sverdlov and Grishin Av and Marianna Orlova and Maria B Kostina and O I Makarevich and Natalia E. Broude and Galina Sergeevna Monastyrskaya and Eugene D. Sverdlov}, journal={FEBS Letters}, year={1991}, volume={278} }
19 Citations
Cloning and characterization of the entire cDNA encoded by ATP1AL1 — a member of the human Na,K/H,K‐ATPase gene family
- Biology, ChemistryFEBS letters
- 1994
Cloning and Characterization of a New Member of the Family of Na + /K + -ATPase Genes
- Biology
- 1994
The data on cloning and characterization of a new Na+/K+-ATPase α subunit related gene from rabbit is reported and two additional genes with high similarity to the α genes have been cloned and partly sequenced.
Human Nongastric H,K-ATPase: Current View On Structure And Functional Properties
- Biology, Chemistry
- 2002
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.
Human nongastric H+-K+-ATPase: transport properties of ATP1al1 assembled with different beta-subunits.
- BiologyAmerican journal of physiology. Cell physiology
- 2002
Results provide new evidence that the human nongastric H+-K+-ATPase interacts with and transports Na+ in exchange for K+ and that beta-isoforms have a distinct effect on the overall structural integrity of AL1 but influence its transport properties less than those of the Na+- K+- ATPase alpha-subunit.
Acid/Base Regulation in Renal Epithelia by H,K-ATPases
- Biology
- 2010
A recent report using a genetic approach to quantify the contribution of two a-subunit isoforms of the H,K-ATPase to acid secretion has confirmed years of pharmacological studies from many laboratories and demonstrates that both iso forms of this enzyme are normally active in the CD.
Renal expression of the gene encoding the gastric H(+)-K(+)-ATPase beta-subunit.
- Biology, ChemistryThe American journal of physiology
- 1995
Analysis of RNA hybridizations, polymerase chain reaction analysis of kidney RNA, and sequence analysis of cDNAs indicate that gastric H(+)-K( +)-ATPase beta-subunit mRNA is present in kidney and probably associates with the gastric K(+-K(+)ATPases alpha-subunits and/or other P-type ATPase alpha- Subunits, thus contributing to acid-base and potassium homeostasis.
PROTON AND POTASSIUM TRANSPORT BY H+/K+‐ATPases
- Biology, ChemistryClinical and experimental pharmacology & physiology
- 1995
The physiological and pharmacological significance of the prototypical H+/K+‐ATPase is the protein that acidifies gastric luminal contents and has led to a detailed investigation of its biochemistry and molecular and cell biology.
Non-gastric H+/K+ ATPase is present in the microvillous membrane of the human placental syncytiotrophoblast.
- Biology, MedicinePlacenta
- 2004
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Family of human Na+,K+‐ATPase genes Structure of the gene for the catalytic subunit (αIII‐form) and its relationship with structural features of the protein
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The family of human Na+,K+‐ATPase genes No less than five genes and/or pseudogenes related to the α‐subunit
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Multiple genes encode the human Na+,K+-ATPase catalytic subunit.
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A human genomic library was constructed and screened with hybridization probes derived from sheep and rat cDNAs encoding the alpha and alpha(+) isoforms, respectively, of the Na+,K+-ATPase catalytic subunit cDNA sequences but do not correspond to any previously identified isoforms.
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Total genomic Southern hybridization indicated the existence of at most two copies, possibly only one, of the gene encoding the Na,K-ATPase alpha-subunit in the human genome.
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