PMC:7352545 / 44988-48096 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":"Structure and Role of the Host SARS-CoV Receptor ACE2\nSARS-CoV-2 needs ACE2 for entry. Host proteases such as human ACE2 help viral entry through removement of a barrier to enter human cells through unknown receptors. Human ACE2 is known for its role as the SARS-CoV-2 entry receptor and the SARS-CoV receptor. The enzyme ACE-2 in the renin-angiotensin system (RAS) is associated with CoV entry into lungs. ACE2 mediates SARS-2002 entry into host cells via S glycoprotein interaction with the ACE2 receptor. The ACE2 levels on the plasma membrane correlate with virus infectivity. ACE2 expression is present in most tissues such as the lung epithelium. It is highly expressed by respiratory epithelial cells and type I/II lung alveolar epithelial cells [88]. The host receptor is not linked to the classification of CoVs. MERS-CoV, a β-CoV, does not recognize the ACE2 receptor. In contrast, the α-CoV HCoV-NL63 recognizes the ACE2 receptor. ACE2 is a membrane-anchored carboxypeptidase with 805 amino acid residues and is captopril-insensitive. It contains 17 amino acid residues as a signal peptide in the N-terminal region, a type I membrane-anchored domain in the C-terminal region, an extracellular N-terminal domain with heavy N-glycans, a N-terminal SARS-CoV-binding and carboxypeptidase site and a short C-terminal cytoplasmic tail. The ACE2 gene is located on chromosome Xp22. Two ACE2 forms are known, a membrane-bound form and a soluble form.\nACE 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. The biggest difference between ACE2 and ACE is that ACE2 has a non-inhibitory property by ACE inhibitors.\nPulmonary ACE2 is potentially a candidate target in CoV-involved inflammatory pathogenesis. If ACE inhibitors and Ang II-AT1 blockers are dosed, ACE2 expression is increased. However, currently we have no conclusive evidence that the inhibitors help SARS-CoV or SARS-CoV-2 entry. Rather, SARS-CoV infection reduces ACE2 expression. Therefore, SARS-CoV-2 host tropism is not related to ACE2 expression. ACE2 levels and ANG II/ANG 1–7 levels regulate the pathogenic progression. ACE2 expression is upregulated by gene polymorphisms and ACE inhibitors or Angiotensin II receptor blockers such as 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