Aldosterone-mediated Na/K-ATPase expression is α1 isoform specific in the renal cortical collecting duct

P. A. Welling, M. Caplan, M. Sutters, G. Giebisch

Research output: Contribution to journalArticlepeer-review

Abstract

In the renal cortical collecting duct (CCD), mineralocorticoid hormones, like aldosterone, augment the abundance of Na/K-ATPase molecules. It has been postulated that this response involves an isoform switch of the Na/K-ATPase catalytic subunit, α, as the molecular basis for the differential regulation of mineralocorticoid-induced and constitutively expressed Na/K-ATPase pools. In opposition to this attractive hypothesis, three lines of independent evidence are presented which demonstrate that the CCD exclusively expresses the α1 form despite mineralocorticoid-mediated changes in functional Na/K pump density. First, aldosterone increased [3H]ouabain binding in CCD 2.5- fold without changing the ouabain dissociation constant. Second, an electrophysiological assay for pump activity revealed that aldosterone increased maximum Na/K pump current in parallel with the change in ouabain binding without altering the apparent sodium affinity. Third, Western blot analysis with α isoform-specific, antipeptide antibodies demonstrated that aldosterone exclusively increased the total chemical pool of the α1 form of the pump without inducing other α subunit isoforms. In summary, aldosterone increases the abundance of Na/K-ATPase molecules in the CCD which are pharmacologically, physiologically, and chemically indistinguishable from those that are normally expressed.

Original languageEnglish (US)
Pages (from-to)23469-23476
Number of pages8
JournalJournal of Biological Chemistry
Volume268
Issue number31
StatePublished - 1993
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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