IMR Press / FBE / Volume 2 / Issue 4 / DOI: 10.2741/E183

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

Species specificity of prorenin binding to the (pro)renin receptor in vitro

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1 United Graduate School of Agricultural Science, Gifu University, Gifu 501-1193, Japan
2 Faculty of Applied Biological Sciences, Gifu University, Gifu 501-1193, Japan
Academic Editor:Fumiaki Suzuki
Front. Biosci. (Elite Ed) 2010, 2(4), 1234–1240; https://doi.org/10.2741/E183
Published: 1 June 2010
(This article belongs to the Special Issue Handle region peptide and prorenin receptor)
Abstract

In this study, binding properties of human prorenin to rat (pro)renin receptor [r(P)RR] and rat prorenin to human (pro)renin receptor [h(P)RR] were elucidated in vitro to investigate species specificity of prorenin bindings to (P)RR. Both (P)RRs were expressed in vitro based on wheat germ lysate and purified using His trap column. The association and dissociation rate constants of human and rat prorenin for the immobilized r(P)RR and h(P)RR were 6.64x106 and 1.01x106 M-1.s-1 and, 0.024 and 8.45x10-3 s-1, respectively. Their KD values were 3.7nM [3-fold higher than that of human prorenin vs h(P)RR (1.2nM)] and 8.3nM [1.2-fold lower than that of rat prorenin vs r(P)RR (10.2nM)], respectively. Additionally, human and rat prorenin bound to the pre-adsorbed rat and human (P)RR, respectively, performed enzymatic activities. Their molecular activities were 4.1h-1 [almost similar (3.8h-1) to human prorenin vs h(P)RR] and 0.98h-1 [~2-fold lower than rat prorenin vs r(P)RR], respectively. Thus, these results suggest the species specificity for bindings of prorenin to (P)RR, which could be useful in elucidating the biochemical properties of prorenin binding to the receptor.

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