PMC:7408073 / 13827-15276 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7408073","sourcedb":"PMC","sourceid":"7408073","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7408073","text":"ACE and ACE2 are two zinc metalloproteases involved in the biogenesis of the components of renin-angiotensin system (RAS). ACE2 processes angiotensin (Ang) I and II into Ang (1–9) and Ang (1–7), respectively, and it also has other known peptide targets, such as des-Arg(9)-bradykinin, which mediates B1 receptor activation. Ang (1–7) and Ang (1–9) peptides, opposing the effects of ACE/Ang II/Ang II type 1 receptor (AT1R) pathway, are known to mediate vasodilatative (hypotension), antiproliferative and apoptotic effects through Mas and AT2 receptors, respectively, both involving downstream nitric oxide synthase (NOS) pathway activation [38,39,40,41,42,43,44,45,46]. Physiology teaches us that there is a range of normality for every biological parameter, below (defect) and above (excess) of which there is a dysfunction. This is likely to be true for ACE as well as for ACE2. It is well known that excessive Ang II/AT1R pathway activation induces vasoconstriction, aldosterone, inflammation, excessive cell proliferation, thrombosis, cardiac dysfunction and lung alterations (see Figure 1). Moreover, most of the experiments show that increased ACE2 activity leads to beneficial effects; however, the experiments were usually performed using models in which its “antagonist“ (ACE) pathway was upregulated or ACE2 itself was downregulated, therefore balancing an unbalanced situation. What does it happen in models in which the opposite 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