Functional differences between alpha subunit isoforms of the rat Na,K-ATPase expressed in Xenopus oocytes.

Détails

ID Serval
serval:BIB_3A936A6FB95D
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Functional differences between alpha subunit isoforms of the rat Na,K-ATPase expressed in Xenopus oocytes.
Périodique
Journal of Physiology
Auteur⸱e⸱s
Horisberger J.D., Kharoubi-Hess S.
ISSN
0022-3751
Statut éditorial
Publié
Date de publication
03/2002
Peer-reviewed
Oui
Volume
539
Numéro
Pt 3
Pages
669-680
Langue
anglais
Résumé
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.
Mots-clé
Animals, Binding, Competitive, Electric Conductivity, Extracellular Space/metabolism, Female, Oocytes, Potassium/metabolism, Rats/metabolism, Sodium/physiology, Sodium-Potassium-Exchanging ATPase/metabolism, Sodium-Potassium-Exchanging ATPase/physiology, Xenopus laevis
Pubmed
Web of science
Création de la notice
24/01/2008 12:38
Dernière modification de la notice
20/08/2019 13:30
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