Cited by 296Renin-Angiotensin System StudiesCoagulation, Bradykinin, Polyphosphates, and AngioedemaEicosanoids and Hypertension Pharmacology

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Devil and angel in the renin–angiotensin system: ACE–angiotensin II–AT1 receptor axis vs. ACE2–angiotensin-(1–7)–Mas receptor axis

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Iwai, Masaru, Horiuchi, Masatsugu·2009·Hypertension Research

DOI 10.1038/hr.2009.74PMC PMC7091931

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Abstract

Recent studies have established a new regulatory axis in the renin-angiotensin system (RAS). In this axis, angiotensin (Ang)-(1-7) is finally produced from Ang I or Ang II by the catalytic activity of angiotensin-converting enzyme 2 (ACE2). Ang-(1-7) shows actions different from those of AT(1) receptor stimulation, such as vasodilatation, natriuresis, anti-proliferation and an increase in the bradykinin-NO (nitric oxide) system. As the catalytic efficiency of ACE2 is approximately 400-fold higher with Ang II as a substrate than with Ang I, this axis is possibly acting as a counter-regulatory system against the ACE/Ang II/AT(1) receptor axis. The signaling pathway of the ACE2-Ang-(1-7) axis has not yet been totally and clearly understood. However, a recent report suggests that the Mas oncogene acts as a receptor for Ang-(1-7). Intracellular signaling through Mas is not clear yet. Several factors such as Akt phosphorylation, protein kinase C activation and mitogen-activated protein (MAP) kinase inhibition seem to be involved in this signaling pathway. Further investigations are needed to clarify the regulation and mechanism of action of ACE2 and Ang-(1-7). However, this second axis through ACE2 and Ang-(1-7) in RAS can be an important target for the therapy of cardiovascular and metabolic disorders.

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Santos RA, Ferreira AJ, E Silva AC . Recent advances in the angiotensin-converting enzyme 2-angiotensin(1-7)-Mas axis. Exp Physiol 2008; 93: 519–527. · DOI

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Authors: Iwai, M., & Horiuchi, M.
Affiliations: Ehime University (JP)
Corresponding author: Horiuchi, Masatsugu
Venue: Hypertension Research
Publisher: Springer Science and Business Media LLC
Published: 2009-05-22
Volume: 32
Issue: 7
Pages: 533-536
ISSN: 0916-9636 (ISSN-L)
1348-4214
DOI: 10.1038/hr.2009.74
PMC: PMC7091931
OpenAlex: W2067142583
Cited by: 296
References: 37
Citations by year: 2026: 9 · 2025: 9 · 2024: 11 · 2023: 20 · 2022: 21 · 2021: 29 · 2020: 29 · 2019: 12 · 2018: 14 · 2017: 10 · 2016: 17 · 2015: 27 · 2014: 19 · 2013: 19 · 2012: 23
FWCI: 2.51
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Hypertension Research (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
Health Sciences › Medicine › Hematology › Coagulation, Bradykinin, Polyphosphates, and Angioedema
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Eicosanoids and Hypertension Pharmacology
Keywords: renin-angiotensin system, angiotensin-(1-7), angiotensin-converting enzyme 2, Mas receptor, angiotensin II type 1 receptor, angiotensin II, vasodilation, sodium excretion, Akt phosphorylation, protein kinase C, MAP kinase inhibition, cardiovascular disease treatment
MeSH terms: Angiotensin-Converting Enzyme 2, Proto-Oncogene Mas, Angiotensin I, Animals, Humans, Peptidyl-Dipeptidase A, Peptide Fragments, Proto-Oncogene Proteins, Renin-Angiotensin System, Signal Transduction, Receptors, G-Protein-Coupled, Receptor, Angiotensin, Type 1

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Devil and angel in the renin–angiotensin system: ACE–angiotensin II–AT1 receptor axis vs. ACE2–angiotensin-(1–7)–Mas receptor axis

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