Ferritin heavy chain binds peroxiredoxin 6 and inhibits cell proliferation and migration

M Di Sanzo, F Cozzolino, AM Battaglia… - International Journal of …, 2022 - mdpi.com
M Di Sanzo, F Cozzolino, AM Battaglia, I Aversa, V Monaco, A Sacco, F Biamonte
International Journal of Molecular Sciences, 2022mdpi.com
The H Ferritin subunit (FTH1), as well as regulating the homeostasis of intracellular iron, is
involved in complex pathways that might promote or inhibit carcinogenesis. This function
may be mediated by its ability to interact with different molecules. To gain insight into the
FTH1 interacting molecules, we analyzed its interactome in HEK293T cells. Fifty-one
proteins have been identified, and among them, we focused our attention on a member of
the peroxiredoxin family (PRDX6), an antioxidant enzyme that plays an important role in cell …
The H Ferritin subunit (FTH1), as well as regulating the homeostasis of intracellular iron, is involved in complex pathways that might promote or inhibit carcinogenesis. This function may be mediated by its ability to interact with different molecules. To gain insight into the FTH1 interacting molecules, we analyzed its interactome in HEK293T cells. Fifty-one proteins have been identified, and among them, we focused our attention on a member of the peroxiredoxin family (PRDX6), an antioxidant enzyme that plays an important role in cell proliferation and in malignancy development. The FTH1/PRDX6 interaction was further supported by co-immunoprecipitation, in HEK293T and H460 cell lines and by means of computational methods. Next, we demonstrated that FTH1 could inhibit PRDX6-mediated proliferation and migration. Then, the results so far obtained suggested that the interaction between FTH1/PRDX6 in cancer cells might alter cell proliferation and migration, leading to a less invasive phenotype.
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