Ferritin Heavy Chain Binds Peroxiredoxin 6 and Inhibits Cell Proliferation and Migration.

Maria Concetta Faniello, Maddalena Di Sanzo, Flora Cozzolino, Anna Martina Battaglia, Ilenia Aversa, Vittoria Monaco, Alessandro Sacco, Flavia Biamonte, Camillo Palmieri, Francesca Procopio, Gianluca Santamaria, Francesco Ortuso, Piero Pucci, Maria Monti

Journal: International journal of molecular sciences 2022;23(21):12987

PMID: 36361777

Abstract

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.

Address: Research Center of Biochemistry and Advanced Molecular Biology, Department of Experimental and Clinical Medicine, "Magna Graecia" University of Catanzaro, 88100 Catanzaro, Italy.; Department of Chemical Sciences, Università degli Studi di Napoli "Federico II", Via Cinthia 21, 80126 Napoli, Italy.; CEINGE Biotecnologie Avanzate, Via G. Salvatore 486, 80145 Napoli, Italy.; Interdepartmental Centre of Services, "Magna Graecia" University of Catanzaro, 88100 Catanzaro, Italy.; Department of Health Science, "Magna Graecia" University of Catanzaro, 88100 Catanzaro, Italy.
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