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Luciana Bordin, Gabriella Donà, Chiara Sabbadin, Eugenio Ragazzi, Alessandra Andrisani, Guido Ambrosini, Anna Maria Brunati, Giulio Clari, Decio Armanini, Human Red Blood Cells Alterations in Primary Aldosteronism, The Journal of Clinical Endocrinology & Metabolism, Volume 98, Issue 6, 1 June 2013, Pages 2494–2501, https://doi.org/10.1210/jc.2012-3571
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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.
The Aldo-related alterations in erythrocytes were evaluated by comparing in vitro evidence.
This was a multicenter comparative study.
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.
The Tyr-P level, band 3 HMWA formation, and autologous IgG binding were evaluated.
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.
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.
