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Dejo esto que ya puse en el principal:
el bichito-19 and iron dysregulation: distant sequence similarity between hepcidin and the novel cobi19 spike glycoprotein
el bichito-19 and iron dysregulation: distant sequence similarity between hepcidin and the novel cobi19 spike glycoprotein
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Moving back to the biology of the hepcidin protein itself, as noted previously, hepcidin binds to and mediates the degradation of the iron exporter ferroportin. If the sequence similarity reported here is actually playing a significant role at the cellular level, could it be that, although the cellular localizations appear to be different based on current knowledge, the SARS-CoV-2 spike protein cytoplasmic tail can partly mimic the structure of hepcidin and interact with ferroportin? Could the cytoplasmic tail even coordinate and bind iron? These remain to be investigated experimentally, but of note, Rishi and colleagues recently reported on the intracellular localization of ferroportin dimers, and concluded that both the carboxy- and amino-termini of the protein are intracellular [109]. As cited earlier, the details of hepcidin’s own interaction sites with ferroportin remain the subject of different structural determination projects [12, 18, 108]. Relatedly, and of interest, Neves and colleagues, using experiments on iron overload in European bass (Dicentrarchus labrax), have discussed the functional partnership between hepcidin and ferroportin from an evolutionary perspective and suggested that this may “open new possibilities for the pharmaceutical use of selected fish […] hepcidins during infections, with no impact on iron homeostasis” [90, 91].
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