Structural and functional relationship of mammalian and nematode ferritins

Abstract

Ferritin is a unique buffering protein in iron metabolism. By storing or releasing iron in a tightly controlled manner, it prevents the negative effects of free ferrous ions on biomolecules in all domains of life – from bacteria to mammals. This review focuses on the structural features and activity of the ferritin protein family with an emphasis on nematode ferritins and the similarities in their biological roles with mammalian ferritins. The conservative characteristic of the ferritin family across the species originates from the ferroxidase activity against redox-active iron. The antioxidative function of these proteins translates into their involvement in a wide range of important biological processes, e.g., aging, fat metabolism, immunity, anticancer activity, and antipathogenic activity. Moreover, disturbances in ferritin expression lead to severe iron-associated diseases. Research on the Caenorhabditis elegans model organism may allow us to better understand the wide spectrum of mechanisms involving ferritin activity.