Amplification of DNA sequences coding for the Na,K-ATPase alpha-subunit in ouabain-resistant C+ cells.

Emanuel, Janet Rettig; Garetz, Susan; Schneider, Jay W.; Ash, John F.; Benz, EJ Jr; Levenson, Robert

doi:10.1128/mcb.6.7.2476

Cited by 32 publications

(16 citation statements)

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“…The largest amounts were found in kidney, the smallest in liver. Two or even three (r2 mRNAs (5.3-6, 3.4-4.5 and 2.4 kb) were found in different amounts in many rat tissues except for liver [61,62,64,65]. This variety could result from the differential use of the polyadenylation signals in the 3 '-untranslated region of cu2 mRNA [61].…”

Section: Tissue-specificity Of Expression Of Various Isoforms Of Na+mentioning

confidence: 99%

“…This variety could result from the differential use of the polyadenylation signals in the 3 '-untranslated region of cu2 mRNA [61]. But one cannot rule out some crosshybridization due to the high level of homology of different isoforms especially when large cDNA probes have been used [64,65]. Both main mRNAs of aI1 form have been shown to be expressed in brain, skeletal muscles and heart [61].…”

Section: Tissue-specificity Of Expression Of Various Isoforms Of Na+mentioning

confidence: 99%

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Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Broude¹,

Modyanov²,

Monastyrskaya³

1989

FEBS Letters

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Complete primary stators of both submit of Na',K+-ATPase from various sources have been ~~biisbed by a ~mbination of the methods for molecular cloning and protein chemistry. The gene family homologo~ to the a-subunit cDNA of animal Na+,K*-ATPases has been found in the human genome. Some genes of this family encode the known isoforms (aI and aI1) of the Na+,K+-ATPase catalytic subunit. The proteins coded by other genes can be either new isoforms of the Na+,K+-ATPase catalytic subunit or other ion-transporting ATPases. Expression of the genes of this family proceeds in a tissue-specific manner and changes during the postnatal development and neoplastic transformation. The complete exon-intron structure of one of the genes of this family has been established. This gene codes for the form of the catalytic subunit, the existence of which has been unknown. Apparently, all the genes of the discovered family have a similar intron-exon structure. There is certain correlation between the gene structure and the proposed domain a~angement of the a-subunit. The results obtained have become the basis for the experiments which prove the existence of the earlier unknown afI1 isoform of the Na+,K+-ATPase catalytic subunit and have made possible the study of its function.

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Section: Tissue-specificity Of Expression Of Various Isoforms Of Na+mentioning

confidence: 99%

Section: Tissue-specificity Of Expression Of Various Isoforms Of Na+mentioning

confidence: 99%

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Broude¹,

Modyanov²,

Monastyrskaya³

1989

FEBS Letters

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“…HeLa cells, an epithelial cell line derived from human cervix, have only one alpha isoform of around 3.7 kb (Cutler et al 1988), probably equivalent to al in rat (Emanuel et al, 1986), so that the phirmacological properties of the glycosideNa+, K+-ATPase interaction of these cells can be unambiguously related to this isoform. It is of particular interest to study this isoform for we had long noticed that the effect of cardiac glycosides on these and other cultured human cells under equilibrium conditions (see e.g.…”

Section: Introductionmentioning

confidence: 99%

Discrepancy between the short and long term effects of ouabain on the sodium pumps of human cells grown in culture

Griffiths

Ogden

Cormack

et al. 1991

British J Pharmacology

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1 Human cells (HeLa) were cultured for periods up to 48 h in growth medium in the absence or presence of a range of concentrations of cardiac glycosides. In some experiments the potassium concentration of the medium was varied between 0.3 mm and the usual 5 mm. 2 For periods up to 2 h in ouabain the association and dissociation rate constants were measured and the equilibrium binding constant (KD) calculated; the apparent equilibrium binding constant (K'D) was measured after 1-2 days growth in ouabain.3 Ouabain had a K' after 2 days of 2-6 nm in 5 mM K' growth medium, a 4 fold greater blocking effect on sodium pumps after 2 days than expected from the association and dissociation rate constants measured in untreated or previously ouabain-treated cells. 4 This effect was: (a) approximately the same over a range of external potassium concentrations from 0.3 to 5 mm, although the absolute effect of ouabain over this range of potassium was much different; (b) probably not due to different isoforms of pumps in cells grown in ouabain compared to untreated cells; (c) apparently not a consequence of internalisation of pump-glycoside complexes. 5 We conclude that ouabain has only a limited access to sodium pumps in whole cells; this could be because sodium pumps cycle continuously through an inaccessible region of the plasma membrane. This effect needs to be considered both in the assessment of the magnitude of the long term effects of cardiac glycosides on cells, and in the measurement of the glycoside affinities of various isoforms of the pump.

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“…Chromosomal mapping studies revealed that the three (x subunit isoforms are encoded by separate genes, each of which is located on a different murine chromosome (18). Both ouabain resistance and the murine Na,K-ATPase al subunit gene have been assigned to mouse chromosome 3 (18,20). Gene transfer experiments have shown that rat and mouse Na,K-ATPase otl subunit * Corresponding author.…”

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Identification of a region within the Na,K-ATPase alpha subunit that contributes to differential ouabain sensitivity.

et al. 1989

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To analyze determinants within the Na,K-ATPase a subunit that contribute to differential ouabain sensitivity, we constructed and expressed a panel of chimeric cDNA molecules between ouabain-resistant and ouabain-sensitive a subunit cDNAs. When introduced into ouabain-sensitive monkey CV-1 cells, ouabainresistant rat al subunit cDNA and chimeras in which the 5' end of ouabain-sensitive human al or rat OL2 subunit cDNA was replaced by the 5' end of rat al subunit cDNA conferred resistance to 100 ,uM ouabain. Monkey cells transfected with the reciprocal chimeras were unable to survive selection in 1 ,uM ouabain. Rat a2 subunit cDNA and a chimera in which the 5' end of rat al subunit cDNA was replaced by the 5' end of rat a2 subunit cDNA conferred resistance to 0.5 ,uM ouabain. These results suggest that determinants of ouabain resistance reside within the amino-terminal portions of the rat otl and at2 subunits. Expression of chimeric a subunit cDNAs should prove useful for elucidating the structural basis of Na,K-ATPase function.

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Amplification of DNA sequences coding for the Na,K-ATPase alpha-subunit in ouabain-resistant C+ cells.

Cited by 32 publications

References 20 publications

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Discrepancy between the short and long term effects of ouabain on the sodium pumps of human cells grown in culture

Identification of a region within the Na,K-ATPase alpha subunit that contributes to differential ouabain sensitivity.

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Amplification of DNA sequences coding for the Na,K-ATPase alpha-subunit in ouabain-resistant C+ cells.

Cited by 32 publications

References 20 publications

Advances in Na+,K+‐ATPase studies: from protein to gene and back to protein

Advances in Na+,K+‐ATPase studies: from protein to gene and back to protein

Discrepancy between the short and long term effects of ouabain on the sodium pumps of human cells grown in culture

Identification of a region within the Na,K-ATPase alpha subunit that contributes to differential ouabain sensitivity.

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Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein

Advances in Na⁺,K⁺‐ATPase studies: from protein to gene and back to protein