The family of human Na+,K+-ATPase genes No less than five genes and/or pseudogenes related to the α-subunit
E.D. Sverdlov,Galina S. Monastyrskaya,N.E. Broude,Yu.A. Ushkaryov,R.L. Allikmets,A.M. Melkov,Yu. V. Smirnov,I.V. Malyshev,I.E. Dulobova,Konstantin Petrukhin,A. V. Grishin,N.I. Kijatkin,M. B. Kostina,V.E. Sverdlov,Nikolai N. Modyanov,Yu.A. Ovchnikov +15 more
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TLDR
Five different nucleotide sequences have been found in the human genome homologous to the gene of the α‐subunit of Na+,K+‐ATPase, and a comparative analysis of the primary structure of these genes in the region 749–1328 is presented.About:
This article is published in FEBS Letters.The article was published on 1987-06-15 and is currently open access. It has received 74 citations till now. The article focuses on the topics: Gene cluster & Gene family.read more
Citations
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Journal ArticleDOI
Isozymes of the Na-K-ATPase: heterogeneity in structure, diversity in function
Gustavo Blanco,Robert W. Mercer +1 more
TL;DR: The regulation of specific Na pump isozymes gives cells the ability to precisely coordinate Na-K-ATPase activity to their physiological requirements.
Journal ArticleDOI
Endogenous Cardiotonic Steroids: Physiology, Pharmacology, and Novel Therapeutic Targets
TL;DR: The physiological interactions between CTS and other regulatory systems that may be important in the pathophysiology of essential hypertension, preeclampsia, end-stage renal disease, congestive heart failure, and diabetes mellitus are focused on.
Journal ArticleDOI
Tissue-specific and developmental regulation of rat Na,K-ATPase catalytic alpha isoform and beta subunit mRNAs.
John Orlowski,Jerry B. Lingrel +1 more
TL;DR: Each tissue examined exhibits a distinct pattern of expression for the Na,K-ATPase catalytic alpha isoforms during ontogenesis, with maximum expression occurring between 15 and 25 days of age for brain, heart, kidney, and skeletal muscle.
Book ChapterDOI
Molecular genetics of Na,K-ATPase.
TL;DR: The complex structural and functional features of this protein indicate that extensive research is necessary before a clear understanding of the molecular basis of active cation transport is achieved, and the proposed model and functional hypotheses should be considered judiciously.
References
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Amino-acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence.
TL;DR: A model of the Ca2+-ATPase of rabbit muscle sarcoplasmic reticulum which has 3 cytoplasmic domains joined to a set of 10 transmembrane helices by a narrow, penta-helical stalk is proposed.
Journal ArticleDOI
Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain.
TL;DR: A lysine-rich sequence that may function as a movable, ion-selective gate during cation binding and occlusion and several amino acid sequence variations that appear to explain some of the well-known species and tissue differences in cardiac glycoside sensitivity are identified.
Journal ArticleDOI
Pig kidney Na+,K+-ATPase. Primary structure and spatial organization.
Yu.A. Ovchinnikov,Nikolai N. Modyanov,N.E. Broude,Konstantin Petrukhin,A. V. Grishin,N.M. Arzamazova,N.A. Aldanova,Galina S. Monastyrskaya,E.D. Sverdlov +8 more
TL;DR: (Na+ + K+)‐ATPase α‐Sub Unit β‐Subunit β-Subunit cDNA nucleotide sequence Primary structure Glycopeptide Transmembrane arrangement
Journal ArticleDOI
The family of human Na+K+-ATPase genes: A partial nucleotide sequence related to the α-subunit
Yu.A. Ovchinnikov,Galina S. Monastyrskaya,N.E. Broude,R.L. Allikmets,Yu.A. Ushkaryov,A.M. Melkov,Yu. V. Smirnov,I.V. Malyshev,I.E. Dulubova,Konstantin Petrukhin,A.V. Gryshin,V.E. Sverdlov,N.I. Kiyatkin,M. B. Kostina,Nikolai N. Modyanov,Eugene D. Sverdlov +15 more
TL;DR: This report describes the isolation, mapping and partial sequencing of the fourth gene (ATP1AL1) that was demonstrated here to be functionally active and expressed in human brain and kidney and suggests that the gene probably encodes a new ion transport ATPase rather than an isoform of the Na,K-ATPase or the closely related H, K- ATPase.