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This Article Full Text Full Text (PDF) All Versions of this Article: 294/4/F990    most recent 00492.2007v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Yingst, D. R. Articles by Mattingly, R. R. Search for Related Content PubMed PubMed Citation Articles by Yingst, D. R. Articles by Mattingly, R. R.

Angiotensin II stimulates elution of Na-K-ATPase from a digoxin-affinity column by increasing the kinetic response to ligands that trigger the decay of E₂-P

Departments of ¹Physiology, ²Internal Medicine, and ³Pharmacology, Wayne State University, School of Medicine, Detroit, Michigan

Submitted 19 October 2007 ; accepted in final form 6 February 2008

We earlier observed that treating rat proximal tubules with concentrations of angiotensin II (ANG II) that directly stimulate Na-K-ATPase activity changed how Na-K-ATPase subsequently eluted from an ouabain-affinity column. In this study we tested whether ANG II increases the rate of elution in response to ligands that trigger the decay of E₂-P, which implies a change in functional properties of Na-K-ATPase, or by decreasing the amount subsequently eluted with SDS, which suggests a change in how Na-K-ATPase interacts with other proteins. We utilized a new digoxin-affinity column and novel lines of opossum kidney (OK) cells that coexpress the rat AT_1a receptor and either the wild-type rat ₁-isoform of Na-K-ATPase or a truncation mutant missing the first 32 amino acids of its NH₂ terminus. We characterized how rat kidney microsomes bind to and elute from the digoxin-affinity column and demonstrated that they are heterogeneous in the rate at which they release digoxin in response to ligands that trigger the decay of E₂-P. Incubating OK cells with ANG II stimulated the ensuing elution of wild-type rat ₁-subunit by increasing the kinetic response to ligands that cause a decay of E₂-P without affecting the amount later eluted with SDS. In contrast, ANG II had no effect on the kinetic response of the truncation mutant but decreased the amount eluted with SDS. These data suggest that ANG II regulates both the kinetic properties of Na-K-ATPase and its interaction with other proteins by a mechanism(s) involving its NH₂ terminus.

cardiac glycosides; ouabain; epithelial cells; sodium