
Fulltext:
49894.pdf
Embargo:
until further notice
Size:
2.496Mb
Format:
PDF
Description:
publisher's version
Publication year
2006Source
Journal of Histochemistry and Cytochemistry, 54, 2, (2006), pp. 253-262ISSN
Publication type
Article / Letter to editor

Display more detailsDisplay less details
Organization
Pathology
Nephrology
Journal title
Journal of Histochemistry and Cytochemistry
Volume
vol. 54
Issue
iss. 2
Page start
p. 253
Page end
p. 262
Subject
IGMD 7: Iron metabolism; IGMD 9: Renal disorder; NCMLS 1: Immunity, infection and tissue repair; UMCN 5.4: Renal disordersAbstract
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 (EA) level in the kidney during nephrogenesis. Furthermore, we have studied the effect of inhibiting APA EA by injection of anti-APA antibodies into 1-day-old 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 EA caused temporary podocyte foot-process effacement, suggesting a minimum role for APA during nephrogenesis.
This item appears in the following Collection(s)
- Academic publications [202914]
- Electronic publications [101091]
- Faculty of Medical Sciences [80065]
Upload full text
Use your RU credentials (u/z-number and password) to log in with SURFconext to upload a file for processing by the repository team.