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JHC exPRESS: First Published November 14, 2005. doi:10.1369/jhc.5A6815.2005
Copyright © Histochemical Society, Inc.

A more recent version of this article appeared on February 1, 2006.
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The Expression and the Effect of Inhibition of Aminopeptidase-A during Nephrogenesis

Henry B.P.M. Dijkman 1*, Karel J.M. Assmann 1, Eric J. Steenbergen 1 and Jack F.M. Wetzels 1

1 Department of Pathology (HBPMD,KJMA,EJS) and Department of Internal Medicine (JFMW), Division of Nephrology, Radboud University Nijmegen Medical Centre, Nijmegen, the Netherlands

* To whom correspondence should be addressed. E-mail: h.dijkman{at}pathol.umcn.nl.

Submitted on August 16, 2005
Accepted on 27 October 2005


  Abstract
Aminopeptidase-A (APA) is a metalloprotease, that cleaves N-terminal aspartyl and glutamyl residues from peptides. Its best known substrate is Angiotensin II (Ang II), the most active compound of the renin angiotensin system (RAS). The RAS is involved in renal development. Most components of the RAS system are expressed in the developing kidney. Thus far, APA has not been studied in detail. In the present study we have evaluated the expression of APA at the protein-, mRNA-, and enzyme activity level in the kidney during nephrogenesis. Furthermore, we have studied the effect of inhibiting APA enzyme activity by injection of antiAPA antibodies into 1-day-old newborn mice. APA expression was observed from the comma stage onwards, predominantly in the developing podocytes and brush borders of proximal tubular cells. Notably, APA was absent in the medulla or the renal arterioles. Inhibition of APA enzyme activity caused temporary podocyte foot process effacement, suggesting a minimum role for APA during nephrogenesis.

Key Words: podocyte, nephrogenesis, aminopeptidase-A, albuminuria, monoclonal antibodies, inhibition, enzyme activity, mouse


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