ArticleThe Journal of physiology2002
Functional differences between alpha subunit isoforms of the rat Na,K-ATPase expressed in Xenopus oocytes.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 66 citations in OpenAlex.
- Spreading depolarizations exhaust neuronal ATP in a model of cerebral ischemia.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A TMT-Based Proteomic Analysis of Osmoregulation in the Gills ofInternational journal of molecular sciences · 2025Article
- Light-Driven Sodium Pump as a Potential Tool for the Control of Seizures in Epilepsy.Molecular neurobiology · 2024Article
- A Na pump with reduced stoichiometry is up-regulated by brine shrimp in extreme salinities.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Critical Role of Spreading Depolarizations in Early Brain Injury: Consensus and Contention.Neurocritical care · 2022Review
- Migraine Aura, Transient Ischemic Attacks, Stroke, and Dying of the Brain Share the Same Key Pathophysiological Process in Neurons Driven by Gibbs-Donnan Forces, Namely Spreading Depolarization.Frontiers in cellular neuroscience · 2022Review
- NaJournal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2020Article
- A novel ATP1A2 mutation in a patient with hypokalaemic periodic paralysis and CNS symptoms.Brain : a journal of neurology · 2018Article
- Age-related changes in Na, K-ATPase expression, subunit isoform selection and assembly in the stria vascularis lateral wall of mouse cochlea.Hearing research · 2018Article
- Gestation changes sodium pump isoform expression, leading to changes in ouabain sensitivity, contractility, and intracellular calcium in rat uterus.Physiological reports · 2017Article
- Hypoxia Stress Modifies NaJournal of experimental neuroscience · 2017Article
- The Structure and Function of the Na,K-ATPase Isoforms in Health and Disease.Frontiers in physiology · 2017Review
- Glutamate transporter activity promotes enhanced NaThe Journal of physiology · 2016Article
- Managing Brain Extracellular K(+) during Neuronal Activity: The Physiological Role of the Na(+)/K(+)-ATPase Subunit Isoforms.Frontiers in physiology · 2016Review
- Functional Interaction Between Na/K-ATPase and NMDA Receptor in Cerebellar Neurons.Molecular neurobiology · 2015Article
- Importance of the Voltage Dependence of Cardiac Na/K ATPase Isozymes.Biophysical journal · 2015Article
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- Na/K pump regulation of cardiac repolarization: insights from a systems biology approach.Pflugers Archiv : European journal of physiology · 2014Review
- Regulation of the cardiac sodium pump.Cellular and molecular life sciences : CMLS · 2013Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The functional properties of the three most widely distributed alpha subunit isoforms of the Na,K-ATPase are not well known, particularly concerning the voltage dependence of their activity and cation binding kinetics. We measured the electrogenic activity generated by Na,K-ATPases resulting from co-expression of the rat alpha1, alpha2* or alpha3* subunits with the rat beta1 subunit in Xenopus oocytes; alpha2* and alpha3* are ouabain-resistant mutants of the alpha2 and alpha3 isoform, which allowed selective inhibition of the endogenous Na(+),K(+)-pump of the oocyte. In oocytes expressing the three isoforms of the alpha subunit, K(+) induced robust outward currents that were largely ouabain-sensitive. In addition, ouabain-sensitive inward currents were recorded for all three isoforms in sodium-free and potassium-free acid solutions. The very similar voltage dependence of the Na(+),K(+)-pump activity observed in the absence of extracellular Na(+) indicated a similar stoichiometry of the transported cations by the three isoforms. The affinity for extracellular K(+) was slightly lower for the alpha2* and alpha3* than for the alpha1 isoform. The alpha2* isoform was, however, more sensitive to voltage-dependent inhibition by extracellular Na(+), indicating a higher affinity of the extracellular Na(+) site in this isoform. We measured and controlled [Na(+)](i) using a co-expressed amiloride-sensitive Na(+) channel. The intracellular affinity for Na(+) was slightly higher in the alpha2* than in the alpha1 or alpha3* isoforms. These results suggest that the alpha2 isoform could have an activity that is strongly dependent upon [Na(+)](o) and [K(+)](o). These concentrations could selectively modulate its activity when large variations are present, for instance in the narrow intercellular spaces of brain or muscle tissues.
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