IMR Press / FBE / Volume 2 / Issue 4 / DOI: 10.2741/E196

Frontiers in Bioscience-Elite (FBE) is published by IMR Press from Volume 13 Issue 2 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
New perspectives on secretion of (pro)renin receptor into extracellular space
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1 Department of Pharmacology, Saitama Medical University, , Moroyama, Saitama
2 Department of Cardiovascular Medicine, Saitama International Medical Center, , Moroyama, Saitama
3 Department of Biochemistry, Vanderbilt University School of Medicine, Vanderbilt University | Nashville, Tennessee
Academic Editor:Fumiaki Suzuki
Front. Biosci. (Elite Ed) 2010, 2(4), 1362–1367; https://doi.org/10.2741/E196
Published: 1 June 2010
(This article belongs to the Special Issue Handle region peptide and prorenin receptor)
Abstract

(Pro)renin receptor is a new molecule of the renin-angiotensin system. The (pro)renin receptor binds both renin and prorenin leading to protease activity. Furthermore, the binding of renin/prorenin to (pro)renin receptor activates intracellular signaling. Although these studies show the classical function of the (pro)renin receptor on the plasma membrane as a receptor, subcellular distribution and extracellular secretion of (pro)renin receptor remained controversial until recently when Cousin et al. reported possible existence of the soluble form of (pro)renin receptor. Chinese hamster ovary (CHO) cells transfected with human (pro)renin tagged with Venus showed bands at 74kDa and 35kDa without any stimulation in Western blot analysis. Moreover, these cells secreted a 29kDa form, which was the amino-terminal fragment of the (pro)renin receptor. In immunofluorescent staining, (pro)renin receptor tagged with Venus was mainly stained on the endoplasmic reticulum and in vesicle-like structures, but not on the plasma membrane. These data suggest that the (pro)renin receptor may be cleaved in the intracellular compartments of cells and secreted into the extracellular space.

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