PMC:7408073 / 46321-48148 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":"Zinc absorption occurs throughout the gastrointestinal tract into enterocytes by zinc transporters of the Zrt- and Irt-like protein (ZIP) family that take up Zn2+, but also Cu2+ and Fe2+ ions, both of which can inhibit zinc absorption [111]. The bioavailability of zinc is affected by several factors among them the amount of zinc in food, its chemical form (from very low availability, e.g., zinc oxide, to comparatively high, e.g., zinc chloride salt) and its binding to other (intestinal absorbed or non-absorbed) food components [111]. For example, phytates (components present in foods like rice, cereals and corn) and folic acid can form insoluble complexes with zinc that decrease zinc absorption and increase fecal zinc excretion [111]. On the other hand, Zn2+ can form complexes with most natural amino acids (AA) that for example can come from digested proteins; each Zn2+ can be coordinated with the amine groups and carboxylate anions of two AAs (a molar ratio of 1:2). Interestingly, in an in vitro model, the formulation of either ZnCl2 salt or Zn-AA complexes were absorbed by enterocytes and zinc was released on the opposite side of the enterocyte membrane, thus mimicking the intestinal absorption and release into the blood stream [111]. It is therefore conceivable that zinc chelates of AA, as well as zinc salts, may participate in bioavailability and uptake of zinc. The uptake of zinc-AA complexes by AA transporters of human enterocytes suggests that B0AT1 neutral AA transporter associated with ACE2 [28] might also be involved in zinc-AA uptake (a similar mechanism might be supposable for insulin biosynthesis/secretion in pancreatic β cells [91]). Indeed, a recycling of zinc-AAs, possibly supplied by membrane bound ACE2 monocarboxypeptidase cleavage, for ACE2 synthesis could be also 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