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NDT Advance Access originally published online on February 19, 2009
Nephrology Dialysis Transplantation 2009 24(5):1362-1365; doi:10.1093/ndt/gfp065
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© The Author [2009]. Published by Oxford University Press on behalf of ERA-EDTA. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org


The role of ACE2 in pulmonary diseases—relevance for the nephrologist

Gavin Y. Oudit1,2, Yumiko Imai3, Keiji Kuba3, James W. Scholey4 and Josef M. Penninger3

1 Division of Cardiology, Department of Medicine 2 Mazankowski Alberta Heart Institute, University of Alberta, Canada 3 Institute for Molecular Biotechnology of the Austrian Academy of Sciences, Austria 4 Division of Nephrology, Department of Medicine, University of Toronto, Canada

Correspondence and offprint requests to: Gavin Y. Oudit, Division of Cardiology, Department of Medicine, Mazankowski Alberta Heart Institute, University of Alberta, Edmonton, T6G 2S2, Alberta, Canada. Tel: +780-407-8569; Fax: +780-407-6452; E-mail: gavin.oudit@ualberta.ca.

Keywords: angiotesnin II; diabetes; kidney disease; renin–angiotensin system

The first 150 words of the full text of this article appear below.



   Biochemistry of ACE2
 
The renin–angiotensin system (RAS) is a central regulator of cardiovascular and renal functions and plays a key role in the pathophysiology of various cardiovascular and renal diseases. The RAS consists of a series of enzymatic reactions culminating in the generation of angiotensin II (Ang II) in plasma as well as in various tissues including the heart and kidneys. The discovery of angiotensin-converting enzyme 2 (ACE2) had added a new dimension to the RAS [1–5]. Human and rodent ACE2 are similar proteins containing 805 amino acids that include an N-terminal signal sequence, a single active-site catalytic region and a C-terminal hydrophobic membrane-anchor region [2,3,5]. ACE2 functions predominantly as a carboxymonopeptidase with a substrate preference for hydrolysis between proline and a hydrophobic or basic C-terminal residue [6]. Both ACE and ACE2 are endothelium-bound carboxypeptidases with ACE2 protein being highly expressed in the heart and . . . [Full Text of this Article]



   Role of ACE2 in lung diseases
 


   Role of ACE2 in renal diseases
 

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