Recent advances in the angiotensin-converting enzyme 2-angiotensin(1-7)-Mas axis

Exp Physiol. 2008 May;93(5):519-27. doi: 10.1113/expphysiol.2008.042002. Epub 2008 Feb 29.


In the past few years, the classical concept of the renin-angiotensin system (RAS) has experienced substantial conceptual changes. The identification of: the renin/prorenin receptor; the angiotensin-converting enzyme homologue, ACE2, as an angiotensin peptide-processing enzyme and a virus receptor for severe acute respiratory syndrome, the Mas as a receptor for angiotensin (1-7) [Ang(1-7)], and the possibility of signaling through ACE have contributed to switch our understanding of the RAS from the classical limited-proteolysis linear cascade to a cascade with multiple mediators, multiple receptors and multifunctional enzymes. With regard to Ang(1-7), the identification of ACE2 and of Mas as a receptor implicated in its actions contributed to decisively establish this heptapeptide as a biologically active member of the RAS cascade. In this review, we will focus on the recent findings related to the ACE2-Ang(1-7)-Mas axis and, in particular, on its putative role as an ACE-Ang II-AT(1) receptor counter-regulatory axis within the RAS.

Publication types

  • Review

MeSH terms

  • Angiotensin I / metabolism
  • Angiotensin I / pharmacology*
  • Angiotensin-Converting Enzyme 2
  • Animals
  • Humans
  • Myocardium / enzymology
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology*
  • Peptidyl-Dipeptidase A / genetics
  • Peptidyl-Dipeptidase A / metabolism*
  • Polymorphism, Genetic
  • Proto-Oncogene Mas
  • Proto-Oncogene Proteins / physiology*
  • Receptors, G-Protein-Coupled / physiology*


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