Iron transport and storage proteins (null)

Iron transport and storage proteins encompass a diverse group including transferrin, which is a glycoprotein that binds ferric iron (Fe(III)) in blood plasma for safe delivery to cells via receptor-mediated endocytosis, and ferritin, the primary intracellular storage protein composed of heavy (H) and light (L) chain subunits that can sequester up to 4,500 iron atoms per molecule to prevent toxicity from free ferrous iron (Fe(II)). These proteins maintain cellular iron homeostasis by regulating uptake, transport, storage, and export through mechanisms involving transporters like DMT1 for apical iron entry and ferroportin for efflux, often coupled with ferroxidases such as hephaestin. Dysregulation leads to disorders like hemochromatosis from excess iron accumulation or anemia from deficiency, with roles in neurodegeneration and infection via microbial iron competition.[2][3][4][5][6][7] Emerging bacterial systems, such as encapsulin-based IMEF compartments, provide alternative high-capacity storage (over 20 times ferritin's capacity) via specialized ferritin-like cargos and porous shells optimized for iron mineralization.[1] Therapeutically, iron chelators target overload states but face challenges like off-target depletion of essential metals.[3]

Other names

FerritinTransferrinBacterioferritinDMT1 (divalent metal transporter 1)FerroportinHephaestinEncapsulin-associated iron mineralization proteins (IMEF)

Iron chelation to reduce toxic iron accumulation, Competitive binding to transferrin receptor (e.g., some investigational agents), Modulation of ferroportin export