Systemic iron-binding and storage proteins

Systemic iron-binding and storage proteins are a group of specialized molecules, including transferrin, ferritin, lactoferrin, haptoglobin, and hemopexin, that regulate iron distribution and prevent its toxicity. Transferrin is the primary transport protein that delivers iron to tissues via receptor-mediated endocytosis, while ferritin serves as the major storage protein, sequestering iron in a non-reactive mineral core. These proteins are essential for preventing the Fenton reaction, which produces damaging free radicals, and for nutritional immunity, which restricts iron access for pathogens. In clinical practice, these proteins are targeted by iron chelators (e.g., deferoxamine) to treat iron overload and by iron supplements (e.g., ferrous sulfate) to treat iron deficiency. They also serve as critical diagnostic biomarkers, with serum ferritin and transferrin saturation being the gold standards for assessing a patient's iron status. Dysregulation of these proteins is implicated in various diseases, including hereditary hemochromatosis, anemia of chronic disease, and neurodegenerative disorders.

Other names

Iron-binding proteinsIron storage proteinsIron transport and storage systemSiderophilins

Iron chelation (binding and removal of iron from protein stores), Iron supplementation (replenishing iron to saturate transport and storage proteins), and Heme/Hemoglobin sequestration (binding free heme/hemoglobin to prevent toxicity).