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J Biol Chem, Vol. 275, Issue 20, 15357-15362, May 19, 2000

Normal Blood Pressure and Plasma Renin Activity in Mice Lacking the Renin-binding Protein, a Cellular Renin Inhibitor*

Christian SchmitzDagger §, Michael GotthardtDagger , Stephan Hinderlich§§, Jörg-Robert LehesteDagger , Volkmar GrossDagger , Henrik Vorum, Erik Ilsø Christensen||, Friedrich C. Luft**, Saori Takahashi¶¶, and Thomas E. WillnowDagger Dagger Dagger

From the Dagger  Max-Delbrück-Center for Molecular Medicine, §§ Department of Molecular Biology and Biochemistry, Free University, and ** Franz-Volhardt-Clinic, Humboldt University, D-13125 Berlin, Germany, the Departments of  Medical Biochemistry and || Cell Biology, University of Aarhus, 8000 Aarhus C, Denmark, and ¶¶ Akita Research Institute for Food and Brewing, Akita 010-1623, Japan

In renal extracts, some renin is present as "high molecular weight renin," a heterodimeric complex of renin with the 46-kDa renin-binding protein (RnBP), also known as N-acyl-D-glucosamine 2-epimerase. Because RnBP specifically inhibits renin activity, the protein was proposed to play an important role in the regulation of the renin-angiotensin system (RAS). Using gene targeting, we have generated mice lacking RnBP and tested this hypothesis in vivo. In particular, we analyzed biosynthesis, secretion, and activity of renin and other components of the RAS in mice lacking RnBP. Despite extensive investigations, we were unable to detect any major effects of RnBP deficiency on the plasma and renal RAS or on blood pressure regulation. Contrary to previous hypotheses, we conclude that RnBP does not play a significant role in the regulation of renin activity in plasma or kidney. However, RnBP knockout mice excrete an abnormal pattern of carbohydrates in the urine, indicating a role of the protein in renal carbohydrate metabolism.

* This work was supported by grants from the Deutsche Forschungsgemeinschaft, Klinisch-Pharmakologischer Verbund, Berlin-Brandenburg, and the Danish Medical Research Council.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a fellowship from the Helmholtz Society. To whom correspondence should be addressed: Max-Delbrück-Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13125 Berlin, Germany. Tel.: 49-30-9406-2589; Fax: 49-30-9406-2110; E-mail: cschmitz@mdc-berlin.de.

Dagger Dagger Heisenberg fellow of the Deutsche Forschungsgemeinschaft.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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