PMC:7408073 / 32114-33463 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":"Finally, ACE2-loaded SARS-CoV-2 virions and S1-ACE2 complexes may impair both sACE2 proteolytic degradation by blood proteases and its renal excretion, therefore blunting the removal of its systemic enzymatic activity and indicating that circulating viral particles are dangerous even when they are not able to entry into the cells (see Figure 2). On the one hand, ACE2 hypertranscription and consequent increase of membrane (m)ACE2 exposure induced by hypoxia/hypotension may facilitate SARS-CoV-2 entry and its lifecycle into mACE2 expressing cells. On the other hand, the release of ACE2 from the cell membranes and its subsequent activity in the bloodstream and in local (lung/cardiac) extracellular fluids are likely critical steps in contributing to systemic disease pathogenesis. Nevertheless, the same aetiological agent, SARS-CoV-2, can produce a variety of clinical syndromes, which involves several organs in relation to the subject’s predisposition. Although in the present work I have supposed that most of the COVID-19 symptoms might derive from Ang (1–7), Ang II and Ang (1–9) peptide upregulation, the involvement of B1 receptor pathway suppression mediated by ACE2 metabolisation of des-Arg(9)-bradykinin to inactive bradykinin (1–7) or other ACE2-downstream peptides such as apelins, casomorphins and dynorphins cannot be rule 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