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(前)肾素受体和前肾素:它们可能的相互作用部位。

(Pro)renin receptor and prorenin: their plausible sites of interaction.

机构信息

Department of Biochemistry and Molecular Biology, University of Dhaka, Bangladesh.

出版信息

Front Biosci (Landmark Ed). 2012 Jan 1;17(1):389-95. doi: 10.2741/3933.

DOI:10.2741/3933
PMID:22201750
Abstract

Before discovery of (pro)renin receptor, prorenin was regarded as a source of renin and probable diagnostic marker for diabetic nephropathy/Wilms' tumor. It is now considered that prorenin can perform renin activity by binding to (P)RR and binding mechanism of (pro)renin to (P)RR was indicated in many in vitro studies. Considering the physiological importance and pathological involvement of (P)RR, it is indeed a demand of time to determine the three dimensional structure of (P)RR to design (P)RR blocker(s) effective for (pro)renin. It may also facilitate to explain the incompatible data about the effective application of decoy peptide as (P)RR blocker. So far, studies have discussed the bindings of (pro)renin to (P)RR using peptides mimicking the structures of ligands (e.g., the decoy including "handle" region peptide, the "hinge" peptide etc). In this review, the binding mechanism of ligands has been highlighted from the structural aspect of (P)RR using several anti-(P)RR antibodies designed from the primary structure of (pro)renin receptor. Therefore, this review would give us a clue regarding the plausible binding region(s) for prorenin in the (P)RR.

摘要

在(前)肾素受体被发现之前,原肾素被认为是肾素的来源,也是糖尿病肾病/肾母细胞瘤的可能诊断标志物。现在认为,原肾素可以通过与(P)RR 结合来发挥肾素活性,许多体外研究都表明了(pro)renin 与(P)RR 的结合机制。考虑到(P)RR 的生理重要性和病理相关性,确定(P)RR 的三维结构以设计有效的(pro)renin (P)RR 阻滞剂确实是当务之急。这也可能有助于解释作为(P)RR 阻滞剂的诱饵肽的有效应用的不兼容数据。到目前为止,研究已经使用模拟配体结构的肽(例如,包括“把手”区域肽的诱饵肽、“铰链”肽等)讨论了(pro)renin 与(P)RR 的结合。在这篇综述中,使用从(pro)renin 受体的一级结构设计的几种抗(P)RR 抗体,从(P)RR 的结构方面突出了配体的结合机制。因此,这篇综述将为我们提供(P)RR 中可能的原肾素结合区域的线索。

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(Pro)renin receptor and prorenin: their plausible sites of interaction.(前)肾素受体和前肾素:它们可能的相互作用部位。
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Hypertens Res. 2023 Apr;46(4):959-971. doi: 10.1038/s41440-022-01094-w. Epub 2022 Dec 9.