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This study investigated the effect of long-term ACE inhibition on cardiac and renal ACE2 in rats with CKD induced by subtotal nephrectomy (STNx). Sprague�CDawley rats had sham (control) or STNx surgery. Control rats received vehicle (n= 9) and STNx rats ramipril (1 mg kg?1 day?1; n= 10) or vehicle (n= 10) for 28 days. Subtotal nephrectomy resulted in impaired creatinine clearance (P [http://www.selleckchem.com/products/iox1.html IOX1] (P [http://www.selleckchem.com/products/i-bet-762.html I-BET-762 clinical trial] fibrosis. There was no change in cardiac ACE2 in rats with CKD compared with control rats. In rats with CKD, ACE inhibition had major benefits to reduce blood pressure and cardiac hypertrophy and to improve creatinine clearance, but did not significantly impact on cardiac ACE2, cardiac interstitial fibrosis, renal fibrosis or proteinuria. Thus, in rats with CKD, renal ACE2 deficiency and lack of activation of cardiac ACE2 may contribute to the progression of cardiac and renal tissue injury. As long-term ACE inhibition only partly ameliorated the adverse cardio-renal effects of CKD, adjunctive therapies that lead to further increases in ACE2 activity may be needed to combat the cardio-renal complications of CKD. Kidney disease is a major worldwide problem, and patients with chronic kidney disease (CKD) are [http://en.wikipedia.org/wiki/Diglyceride diglyceride] at increased cardiovascular risk (Go et al. 2004; Levey et al. 2010; Couser & Riella, 2011). Chronic kidney disease is characterized by enhanced activity of the renin�Cangiotensin system (RAS), which plays a major role in the progression of cardiac and renal injury (Velez, 2009). Blockade of the RAS slows but does not prevent renal and cardiac injury, suggesting that factors beyond the ��traditional�� RAS are involved in progression of disease. Angiotensin-converting enzyme (ACE) converts angiotensin (Ang) I to Ang II, which is responsible for the pathophysiological effects of the RAS, but a homologue of ACE, known as ACE2, has now been identified (Donoghue et al. 2000; Burrell et al. 2004). The main role of ACE2 is to cleave Ang II and, in doing so, form the biologically active heptapeptide, Ang-(1�C7), which acts via the Mas receptor (Santos et al. 2003).