Devil and angel in the renin–angiotensin system: ACE–angiotensin II–AT1 receptor axis vs. ACE2–angiotensin-(1–7)–Mas receptor axis
Identifieur interne : 001531 ( Main/Exploration ); précédent : 001530; suivant : 001532Devil and angel in the renin–angiotensin system: ACE–angiotensin II–AT1 receptor axis vs. ACE2–angiotensin-(1–7)–Mas receptor axis
Auteurs : Masaru Iwai ; Masatsugu HoriuchiSource :
- Hypertension Research [ 0916-9636 ] ; 2009.
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 AT1 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/AT1 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.
Url:
DOI: 10.1038/hr.2009.74
PubMed: 19461648
PubMed Central: 7091931
Affiliations:
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<front><div type="abstract" xml:lang="en"><p id="Par1">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<sub>1</sub>
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<sub>1</sub>
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.</p>
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<affiliations><list></list>
<tree><noCountry><name sortKey="Horiuchi, Masatsugu" sort="Horiuchi, Masatsugu" uniqKey="Horiuchi M" first="Masatsugu" last="Horiuchi">Masatsugu Horiuchi</name>
<name sortKey="Iwai, Masaru" sort="Iwai, Masaru" uniqKey="Iwai M" first="Masaru" last="Iwai">Masaru Iwai</name>
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