Angiotensin-Converting Enzyme 2: The First Decade

The renin-angiotensin system (RAS) is a critical regulator of hypertension, primarily through the actions of the vasoactive peptide Ang II, which is generated by the action of angiotensin-converting enzyme (ACE) mediating an...

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Main Authors: Nicola E. Clarke, Anthony J. Turner
Format: Article
Language:English
Published: Wiley 2012-01-01
Series:International Journal of Hypertension
Online Access:http://dx.doi.org/10.1155/2012/307315
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author Nicola E. Clarke
Anthony J. Turner
author_facet Nicola E. Clarke
Anthony J. Turner
author_sort Nicola E. Clarke
collection DOAJ
description The renin-angiotensin system (RAS) is a critical regulator of hypertension, primarily through the actions of the vasoactive peptide Ang II, which is generated by the action of angiotensin-converting enzyme (ACE) mediating an increase in blood pressure. The discovery of ACE2, which primarily metabolises Ang II into the vasodilatory Ang-(1-7), has added a new dimension to the traditional RAS. As a result there has been huge interest in ACE2 over the past decade as a potential therapeutic for lowering blood pressure, especially elevation resulting from excess Ang II. Studies focusing on ACE2 have helped to reveal other actions of Ang-(1-7), outside vasodilation, such as antifibrotic and antiproliferative effects. Moreover, investigations focusing on ACE2 have revealed a variety of roles not just catalytic but also as a viral receptor and amino acid transporter. This paper focuses on what is known about ACE2 and its biological roles, paying particular attention to the regulation of ACE2 expression. In light of the entrance of human recombinant ACE2 into clinical trials, we discuss the potential use of ACE2 as a therapeutic and highlight some pertinent questions that still remain unanswered about ACE2.
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spelling doaj-art-57e4575b834b42058b161698675780c22025-02-03T05:57:58ZengWileyInternational Journal of Hypertension2090-03842090-03922012-01-01201210.1155/2012/307315307315Angiotensin-Converting Enzyme 2: The First DecadeNicola E. Clarke0Anthony J. Turner1Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UKInstitute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UKThe renin-angiotensin system (RAS) is a critical regulator of hypertension, primarily through the actions of the vasoactive peptide Ang II, which is generated by the action of angiotensin-converting enzyme (ACE) mediating an increase in blood pressure. The discovery of ACE2, which primarily metabolises Ang II into the vasodilatory Ang-(1-7), has added a new dimension to the traditional RAS. As a result there has been huge interest in ACE2 over the past decade as a potential therapeutic for lowering blood pressure, especially elevation resulting from excess Ang II. Studies focusing on ACE2 have helped to reveal other actions of Ang-(1-7), outside vasodilation, such as antifibrotic and antiproliferative effects. Moreover, investigations focusing on ACE2 have revealed a variety of roles not just catalytic but also as a viral receptor and amino acid transporter. This paper focuses on what is known about ACE2 and its biological roles, paying particular attention to the regulation of ACE2 expression. In light of the entrance of human recombinant ACE2 into clinical trials, we discuss the potential use of ACE2 as a therapeutic and highlight some pertinent questions that still remain unanswered about ACE2.http://dx.doi.org/10.1155/2012/307315
spellingShingle Nicola E. Clarke
Anthony J. Turner
Angiotensin-Converting Enzyme 2: The First Decade
International Journal of Hypertension
title Angiotensin-Converting Enzyme 2: The First Decade
title_full Angiotensin-Converting Enzyme 2: The First Decade
title_fullStr Angiotensin-Converting Enzyme 2: The First Decade
title_full_unstemmed Angiotensin-Converting Enzyme 2: The First Decade
title_short Angiotensin-Converting Enzyme 2: The First Decade
title_sort angiotensin converting enzyme 2 the first decade
url http://dx.doi.org/10.1155/2012/307315
work_keys_str_mv AT nicolaeclarke angiotensinconvertingenzyme2thefirstdecade
AT anthonyjturner angiotensinconvertingenzyme2thefirstdecade