PMC:7161517 / 17805-19353 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7161517","sourcedb":"PMC","sourceid":"7161517","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7161517","text":"The mechanisms by which ACE inhibitors act are complex. Although ACE2 is not inhibited by ACE inhibitors (19), an increase in Ang1-7 suggests their clinical effects are partly mediated by the angiotensinases. ACE inhibitors inhibit the conversion of Ang I to Ang II and inhibit the hydrolysis of bradykinin. ACE inhibition promotes the vasodilatory effects of bradykinin, improved endothelium-dependent vasodilation through increased prostaglandin and nitric oxide production, and down regulation of the AT1 receptor (50, 51, 52). Studies that elucidated the effect of ACE inhibition on the ACE2 gene showed that inhibition of Ang II synthesis regulated ACE2 mRNA but not ACE2 activity (53). However, ACE inhibition alone or in combination with losartan was demonstrated to increase plasma Ang1-7 while reducing plasma Ang II (53). Compared with the degree of ACE2 mRNA upregulation seen with post-losartan monotherapy, combination of losartan and lisinopril resulted in suppressed upregulation of ACE2 mRNA, which suggested ACE inhibitors might override a signal that regulates ACE2 transcription (53). Although Ang II is the predominant substrate, ACE2 can also convert Ang I into Ang 1-9, which, in turn, could be converted to Ang 1-7 via ACE; Ang I can be directly converted into Ang 1-7 via zinc metallopeptidase neprilysin (17), although with less favorable kinetics at baseline. Thus, it can be assumed ACE inhibitors disrupt the balance between catalytically active ACE and ACE2, resulting in favored activation of the ACE2/Ang1-7/Mas 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