Physiological iron-binding proteins

Physiological iron-binding proteins are a specialized group of proteins, including transferrin, ferritin, and lactoferrin, that regulate the acquisition, transport, and storage of iron in the body [1][2]. Transferrin serves as the primary vehicle for iron transport in the plasma, while ferritin provides a safe intracellular shell for iron storage, preventing the formation of toxic hydroxyl radicals via the Fenton reaction [2][3]. These proteins are essential for maintaining iron homeostasis, which is critical for erythropoiesis, DNA synthesis, and cellular respiration [3]. In clinical medicine, these proteins are the focus of treatments for iron-related disorders; for instance, iron chelators like deferoxamine are used to treat systemic iron overload by binding to iron and facilitating its removal [4]. Conversely, iron deficiency is managed by providing exogenous iron to saturate these binding proteins and restore physiological levels [1]. Beyond metabolism, proteins like lactoferrin contribute to the innate immune system by sequestering iron from microbes, thereby inhibiting their growth [5].

Other names

Iron-binding proteinsIron-sequestration proteinsSiderophilinsIron transport and storage proteins

Iron chelators (e.g., deferoxamine) bind to ferric iron with high affinity to form stable complexes that are excreted, thereby reducing systemic iron load [4]. Iron supplements provide elemental iron that is incorporated into these binding proteins to support erythropoiesis and cellular function [1][3].