Angiotensin-converting enzyme 2, angiotensin-(1–7) and Mas: new players of the renin–angiotensin system

Journal of Endocrinology - Tập 216 Số 2 - Trang R1-R17 - 2013
Robson A.S. Santos1, Anderson J. Ferreira2, Thiago Verano‐Braga3, Michael Bäder4
1Departments of Physiology and Biophysics Morphology, Biological Sciences Institute, Federal University of Minas Gerais, Belo Horizonte, MG, Brazil.
2Federal University of Minas Gerais
3Institut for Biokemi og Molekylær Biologi
4Universidade Federal de Minas Gerais, Belo Horizonte, Brazil

Tóm tắt

Angiotensin (Ang)-(1–7) is now recognized as a biologically active component of the renin–angiotensin system (RAS). Ang-(1–7) appears to play a central role in the RAS because it exerts a vast array of actions, many of them opposite to those attributed to the main effector peptide of the RAS, Ang II. The discovery of the Ang-converting enzyme (ACE) homolog ACE2 brought to light an important metabolic pathway responsible for Ang-(1–7) synthesis. This enzyme can form Ang-(1–7) from Ang II or less efficiently through hydrolysis of Ang I to Ang-(1–9) with subsequent Ang-(1–7) formation by ACE. In addition, it is now well established that the G protein-coupled receptor Mas is a functional binding site for Ang-(1–7). Thus, the axis formed by ACE2/Ang-(1–7)/Mas appears to represent an endogenous counterregulatory pathway within the RAS, the actions of which are in opposition to the vasoconstrictor/proliferative arm of the RAS consisting of ACE, Ang II, and AT1receptor. In this brief review, we will discuss recent findings related to the biological role of the ACE2/Ang-(1–7)/Mas arm in the cardiovascular and renal systems, as well as in metabolism. In addition, we will highlight the potential interactions of Ang-(1–7) and Mas with AT1and AT2receptors.

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Journal of Endocrinology

Tập 216 Số 2

R1-R17

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