Coexpression of alpha 1 with putative beta 3 subunits results in functional Na+/K+ pumps in Xenopus oocytes
Details
Serval ID
serval:BIB_76EF623E318F
Type
Article: article from journal or magazin.
Collection
Publications
Fund
Title
Coexpression of alpha 1 with putative beta 3 subunits results in functional Na+/K+ pumps in Xenopus oocytes
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424 (Print)
Publication state
Published
Issued date
10/1991
Volume
88
Number
19
Pages
8397-400
Notes
In Vitro
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Oct 1
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Oct 1
Abstract
The active Na+/K+ pump is composed of an alpha and a beta subunit. Until now, three putative isoforms of the beta subunit have been identified that share sequence similarity. We have expressed the beta 1 and beta 3 isoforms of Xenopus laevis Na+/K(+)-ATPase in Xenopus oocytes to compare functional properties of the Na+/K+ pump, including either of these two isoforms. Na+/K+ pump current, estimated as K(+)-induced outward current in voltage-clamped oocytes, was doubled by coexpression of alpha 1 subunits with either isoform of the beta subunit compared to expression of alpha 1 subunits alone. The kinetics of activation by external K+ and the voltage dependence of the electrogenic activity of the Na+/K+ pump were similar with both beta isoforms, indicating that both beta 1 and beta 3 isoforms can support expression at the oocyte surface of an active Na+/K+ pump with similar functional properties.
Keywords
Animals Biological Transport, Active Cell Membrane/enzymology Electric Conductivity Ion Channels/*chemistry/physiology Kinetics Membrane Potentials Na(+)-K(+)-Exchanging ATPase/*chemistry/physiology Oocytes Potassium/pharmacology Recombinant Proteins Strophanthidin/pharmacology Structure-Activity Relationship Xenopus laevis
Pubmed
Web of science
Create date
24/01/2008 13:28
Last modification date
03/03/2018 18:26