Human red blood cells alterations in primary aldosteronism

J Clin Endocrinol Metab. 2013 Jun;98(6):2494-501. doi: 10.1210/jc.2012-3571. Epub 2013 Mar 28.

Abstract

Context: Aldosterone (Aldo) effects include NADPH oxidase activation involved in Aldo-related oxidative stress. Red blood cells (RBCs) are particularly sensitive to oxidative assault, and both the formation of high molecular weight aggregates (HMWAs) and the diamide-induced Tyr phosphorylation (Tyr-P) level of membrane band 3 can be used to monitor their redox status.

Objective: The Aldo-related alterations in erythrocytes were evaluated by comparing in vitro evidence.

Design: This was a multicenter comparative study.

Study participants: The study included 12 patients affected by primary aldosteronism (PA) and 6 healthy control subjects (HCs), whose RBCs were compared with those of patients with PA. For in vitro experiments, RBCs from HCs were incubated with increasing Aldo concentrations.

Main outcome measures: The Tyr-P level, band 3 HMWA formation, and autologous IgG binding were evaluated.

Results: In patients with PA, both Tyr-P levels and band 3 HMWAs were higher than those in HCs. RBCs from HCs were treated with increasing Aldo concentrations in both platelet-poor plasma (PPP) and charcoal-stripped (CS)-PPP. Results showed that Aldo had dose- and time-dependent effects on band 3 Tyr-P and HMWA formation in CS-PPP more than in PPP. These effects were almost completely prevented by canrenone or cortisol. Aldo-related membrane alterations led to increased autologous IgG binding.

Conclusions: Erythrocytes from patients with PA show oxidative-like stress evidenced by increased HMWA content and diamide-induced band 3 Tyr-P level. Aldo effects are mediated by the mineralocorticoid receptor, as suggested by the inhibitory effects of canrenone, an antagonist of Aldo. In CS-PPP, in which Aldo induces remarkable membrane alterations leading to IgG binding, Aldo may be responsible for premature RBC removal from circulation.

Publication types

  • Multicenter Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aged
  • Anion Exchange Protein 1, Erythrocyte / analysis
  • Diamide / pharmacology
  • Erythrocyte Aggregation
  • Erythrocytes / metabolism*
  • Female
  • Humans
  • Hyperaldosteronism / blood*
  • Immunoglobulin G / metabolism
  • Male
  • Middle Aged
  • Oxidative Stress

Substances

  • Anion Exchange Protein 1, Erythrocyte
  • Immunoglobulin G
  • Diamide