Pendrin is a Na⁺-independent Cl^-/HCO₃^- exchanger found in the apical regions of type B and non-A, non-B intercalated cells within the aldosterone-sensitive region of the nephron, i.e. the distal convoluted tubule (DCT), the connecting tubule (CNT) and the cortical collecting duct (CCD). Type B intercalated cells mediate Cl^- absorption and HCO₃^- secretion primarily through pendrin-mediated Cl^-/HCO₃^- exchange. This exchanger is upregulated with angiotensin II administration and in models of metabolic alkalosis, such as following administration of aldosterone or NaHCO₃. In the absence of pendrin-mediated HCO₃^- secretion, an enhanced alkalosis is observed following aldosterone or NaHCO₃ administration. However, probably of more significance is the role of pendrin in the pressor response to aldosterone. Pendrin mediates Cl^- absorption and modulates aldosterone-induced Na⁺ absorption mediated by ENaC. Pendrin changes ENaC channel activity by changing both channel open probability (Po) and surface density (N), at least partly by altering luminal HCO₃^- and ATP concentration. Thus, aldosterone and angiotensin II stimulate pendrin expression and function, which stimulates ENaC activity, thereby contributing to the pressor response of these hormones. However, pendrin may modulate blood pressure partly through its extra-renal effects. For example, pendrin is expressed in the adrenal medulla, where it modulates catecholamine release. The increase in catecholamine release observed with pendrin gene ablation, likely contributes to the increment in vascular contractile force observed in the pendrin null mouse. This review summarizes the signaling mechanisms that regulate pendrin abundance and function as well as the contribution of pendrin to distal nephron function.