Functional expression of N-terminal truncated alpha-subunits of Na,K-ATPase in Xenopus laevis oocytes

Détails

ID Serval
serval:BIB_6F0B9261C89B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Functional expression of N-terminal truncated alpha-subunits of Na,K-ATPase in Xenopus laevis oocytes
Périodique
FEBS Letters
Auteur(s)
Burgener-Kairuz  P., Horisberger  J. D., Geering  K., Rossier  B. C.
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
09/1991
Volume
290
Numéro
1-2
Pages
83-6
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Sep 23
Résumé
N-terminal deletion mutants of Na,K-ATPase alpha 1 isoforms initiating translation at Met34 (alpha 1T1) or at Met43 (alpha 1T2) were expressed in X. laevis oocytes. Compared to beta 3 cRNA injected controls, the co-expression of alpha 1wt, alpha 1T1, alpha 1T2 with beta 3 subunits results in a 2- to 3-fold increase of ouabain binding sites, parallelled by a concomitant increase in Na,K-pump current. The apparent K1/2 for potassium activation of the alpha 1T2/beta 3 Na,K-pumps is significantly higher than that of the alpha 1wt/beta 3 or alpha 1T1/beta 3 Na,K-pumps expressed at the cell surface. Total deletion of the lysine-rich N-terminal domain thus allows the expression of active Na,K-pump but with distinct cation transport properties.
Mots-clé
Amino Acid Sequence Animals Base Sequence Chromosome Deletion DNA Mutational Analysis Molecular Sequence Data *Na(+)-K(+)-Exchanging ATPase/genetics/*metabolism Oligonucleotides/chemistry Oocytes Potassium/metabolism Recombinant Proteins Structure-Activity Relationship Xenopus laevis/genetics/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 12:28
Dernière modification de la notice
20/08/2019 14:28
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