Three key proteases - angiotensin-l-converting enzyme (ACE), ACE2 and renin - within and beyond the renin-angiotensin system

被引：118

作者：

Guang, Cuie ^{[1
,2
]}

Phillips, Robert D. ^{[2
]}

Jiang, Bo ^{[1
]}

Milani, Franco ^{[3
]}

机构：

[1] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi, Jiangsu, Peoples R China

[2] Univ Georgia, Dept Food Sci & Technol, Griffin, GA 30223 USA

[3] Univ Wisconsin Madison, Dept Food Sci, Madison, WI USA

来源：

ARCHIVES OF CARDIOVASCULAR DISEASES | 2012年 / 105卷 / 6-7期

关键词：

Angiotensin; ACE; ACE2; Renin; (Pro)renin receptor; SPONTANEOUSLY HYPERTENSIVE-RATS; ASP-LYS-PRO; PUTATIVE (PRO)RENIN RECEPTOR; HANDLE-REGION PEPTIDE; AMYLOID BETA-PEPTIDE; ACTIVE-SITES; BLOOD-PRESSURE; N-DOMAIN; NONPROTEOLYTIC ACTIVATION; INHIBITORY PEPTIDES;

D O I：

10.1016/j.acvd.2012.02.010

中图分类号：

R5 [内科学];

学科分类号：

100201 [内科学];

摘要：

The discovery of angiotensin-l-converting enzyme 2 (ACE2) and a (pro)renin receptor has renewed interest in the physiology of the renin-angiotensin system (RAS). Through the ACE2/angiotensin-(1-7)/Mas counter-regulatory axis, ACE2 balances the vasoconstrictive, proliferative, fibrotic and proinflammatory effects of the ACE/angiotensin II/AT1 axis. The (pro)renin receptor system shows an angiotensin-dependent function related to increased generation of angiotensin I, and an angiotensin-independent aspect related to intracellular signalling. Activation of ACE2 and inhibition of ACE and renin have been at the core of the RAS regulation. The aim of this review is to discuss the biochemistry and biological functions of ACE, ACE2 and renin within and beyond the RAS, and thus provide a perspective for future bioactives from natural plant and/or food resources related to the three proteases. (C) 2012 Elsevier Masson SAS. All rights reserved.

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收藏

页码：373 / 385

页数：13

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