ArticleBiophysical journal2010
Dual mechanisms of allosteric acceleration of the Na(+),K(+)-ATPase by ATP.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Consensus, controversies, and conundrums of P4-ATPases: The emerging face of eukaryotic lipid flippases.The Journal of biological chemistry · 2024Review
- Bioinformatic Study of Possible Acute Regulation of Acid Secretion in the Stomach.The Journal of membrane biology · 2024Article
- Cholesterol depletion inhibits NaThe Journal of biological chemistry · 2019Article
- Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase.The Biochemical journal · 2012Article
- Comparative properties of caveolar and noncaveolar preparations of kidney Na+/K+-ATPase.Biochemistry · 2011Article
- Kinetics of K(+) occlusion by the phosphoenzyme of the Na(+),K(+)-ATPase.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Investigations of the E2 --> E1 conformational change of Na(+),K(+)-ATPase from shark rectal gland and pig kidney via the stopped-flow technique have revealed major differences in the kinetics and mechanisms of the two enzymes. Mammalian kidney Na(+),K(+)-ATPase appears to exist in a diprotomeric (alphabeta)(2) state in the absence of ATP, with protein-protein interactions between the alpha-subunits causing an inhibition of the transition, which occurs as a two-step process: E2:E2 --> E2:E1 --> E1:E1. This is evidenced by a biphasicity in the observed kinetics. Binding of ATP to the E1 or E2 states causes the kinetics to become monophasic and accelerate, which can be explained by an ATP-induced dissociation of the diprotomer into separate alphabeta protomers and relief of the preexisting inhibition. In the case of enzyme from shark rectal gland, the observed kinetics are monophasic at all ATP concentrations, indicating a monoprotomeric enzyme; however, an acceleration of the E2 --> E1 transition by ATP still occurs, to a maximum rate constant of 182 (+/- 6) s(-1). This indicates that ATP has two separate mechanisms whereby it accelerates the E2 --> E1 transition of Na(+),K(+)-ATPase alphabeta protomers and (alphabeta)(2) diprotomers.
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Registered trials
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