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Aldosterone‐induced Na+ Absorption is Regulated by Protein Acetylation in a Cellular Model of the Cortical Collecting Duct

Fine‐tuning of total body sodium content occurs within the aldosterone‐sensitive distal nephron (ASDN). Here, the volume‐regulating hormone aldosterone can promote Na+ retention to offset changes in extracellular fluid volume by binding the mineralocorticoid receptor (MR). The resulting transcription of key intracellular proteins, including serum and glucocorticoid‐induced kinase 1 (SGK1), promote Na+ reabsorption via the epithelial sodium channel (ENaC). Acetylation, a post‐translational modification involving attachment of acetyl groups to lysine residues, appears to control the transcriptional activity of the MR. Indeed recently it was demonstrated in rats that experimentally‐induced hypertension could be ameliorated by inhibiting histone deacetylases (HDACs), which remove acetyl groups. The molecular mechanisms underpinning this response, however, remain unclear. The aim of this study was to explore the role of acetylation in mediating aldosterone‐induced Na+ absorption using a highly differentiated cellular model of the cortical collecting duct, mCCDcl1 cells.