PMC:7408073 / 61707-63261
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7408073","sourcedb":"PMC","sourceid":"7408073","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7408073","text":"Based on ACE2 mechanism of action, there are alternative ways to inhibit ACE2 (and ACE), for example concentration of cation/anion might also targets of intervention to inhibit the zinc metalloprotease ACE2 (and ACE). In this regard, EDTA, a cation chelator, has been shown to be able to inhibit ACE2 activity [79]. Of interest, EDTA binds with 106- and 102-fold higher affinity to Zn2+ than to Ca2+ and Fe2+, respectively [123], and in plasma, free Ca2+ concentration (1.05–1.30 mmol/L) is “only” about 103-fold higher than free Zn2+ (0.1–2.0 µmol/L), while majority of iron in plasma is bound to transferrin. As a consequence, the iron concentration in plasma of healthy subjects is very low on the order of 10−18M [112]. Among the essential metal ions present in the organisms, the specific affinity of EDTA for systemic Zn2+ in physiologic conditions is highlighted by the evidence that prolonged treatment with CaNa2EDTA results in specific zinc depletion that is believed to mediate the teratogenic effects of the drug [123]. As already mentioned, zinc is an important mediator/messenger involved in several cellular activities and excess of free zinc has been shown to be toxic (see also Box 4); however, zinc deficiency has also detrimental effects on growth, neuronal development, and immunity, and in severe cases its consequences can be deadly [102]. For these reasons, treatments with CaNa2EDTA require a careful monitoring of the patient for the therapeutic effects as well as possible complications, so as to titrate the appropriate 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