ACE2 does not act on bradykinin metabolism and its activity is not inhibited by classic ACE inhibitors (ACEIs) [9] . Thus it has been proposed that ACE2 activity may counterbalance the effects of ACE by preventing the accumulation of Ang II in tissues where both ACE2 and ACE are expressed [25, 26] . ACE2 has several biological substrates and it is considered a multifunctional enzyme. Acting as a monocarboxypeptidase, it cleaves several other non-RAAS peptides which have roles in maintaining cardiovascular homeostasis such as (des-Arg9)-bradykinin, a member of the kininogen-kinin system [13] . (des-Arg9)-Bradykinin is formed from bradkinin by the action of carboxypeptidases and is an agonist of the B1 receptor, which is induced after tissue injury [27] . Bradykinin, a vasodilator which acts through the B2 receptor, is produced from its precursor kininogen by kallikrein and is degraded by ACE [13] . While, degradation of bradykinin by ACE is known to be an important aspect of BP regulation, the significance of the degradation of (des-Arg9)-bradykinin by ACE2 remains to be established. In addition to (des-Arg9)-bradykinin, ACE2 is also able to degrade apelin-13, a peptide proposed to cause vasoconstriction and known to regulate fluid homeostasis, and other non-RAAS peptides such as kinetensin, dynorphin A and neurotensin [20] .