ACE2, angiotensin-(1–7), and Mas: the other side of the coin

Pflugers Arch. 2013 Jan;465(1):79-85. doi: 10.1007/s00424-012-1120-0.

Abstract

The renin–angiotensin system (RAS) has recently been extended by the addition of a novel axis consisting of the angiotensin-converting enzyme 2 (ACE2), the heptapeptide angiotensin (1–7) (Ang-(1–7)), and the G protein-coupled receptor Mas. ACE2 converts the vasoconstrictive and pro-oxidative peptide angiotensin II (Ang II) into Ang-(1–7) which exerts vasodilatory and antioxidative effects via its receptor Mas. Thereby, ACE2 regulates the local actions of the RAS in cardiovascular tissues and the ACE2/Ang-(1–7)/Mas axis exerts protective actions in hypertension, diabetes, and other cardiovascular disorders. Consequently, this novel RAS axis represents a promising therapeutic target for cardiovascular and metabolic diseases.

Publication types

  • Review

MeSH terms

  • Angiotensin I / genetics
  • Angiotensin I / metabolism*
  • Angiotensin III / genetics
  • Angiotensin III / metabolism
  • Angiotensin-Converting Enzyme 2
  • Animals
  • Brain / metabolism
  • Gene Expression
  • Humans
  • Kidney / metabolism
  • Lung / metabolism
  • Myocardium / metabolism
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism*
  • Peptidyl-Dipeptidase A / genetics
  • Peptidyl-Dipeptidase A / metabolism*
  • Proto-Oncogene Mas
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism*
  • Receptors, G-Protein-Coupled / genetics
  • Receptors, G-Protein-Coupled / metabolism*
  • Renin-Angiotensin System

Substances

  • Peptide Fragments
  • Proto-Oncogene Mas
  • Proto-Oncogene Proteins
  • Receptors, G-Protein-Coupled
  • Angiotensin III
  • Angiotensin I
  • Peptidyl-Dipeptidase A
  • ACE2 protein, human
  • Angiotensin-Converting Enzyme 2
  • angiotensin I (1-7)