PMC:7352545 / 46442-47494 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7352545","sourcedb":"PMC","sourceid":"7352545","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7352545","text":"ACE cleaves angiotensin I (Ang I) substrate to Ang II. Ang II recognizes the Ang II receptor type 1 (AT1R), contributing to systemic and local vasoconstriction, fibrosis and salt retention in vascular organs. ACE2 has the opposite function of ACE. ACE2 is a close homolog to human ACE. ACE2 activity on Ang II is about 400-fold higher than that on Ang I. Ang-1 to Ang-7 recognize the G protein-coupled receptor (GPCR) Mas to activate vasorelaxation, cardioprotection, antioxidative action, antiinflammation and anti-Ang II-signaling. Therefore, the ACE2-Ang-1 to Ang-7 axis is a target candidate for cardiovascular diseases. ACE2 shows similar binding structures between nCoV and SARS-CoV. The three proteins of ACE, Ang II and AT1R contribute to progression of lung injury in humans. ACE2 removes a single amino acid residue from Ang II to yield the vasodilator, named Ang 1-Ang 7. ACE2 cleaves Ang-I to Ang 1–Ang 9 and Ang II to Ang-1 to Ang-7. 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