Ferritin (Ferritin heavy chain and Ferritin light chain) (FTL/FTH1)

Ferritin is the primary intracellular iron-storage protein, consisting of 24 subunits of heavy (FTH1) and light (FTL) chains that form a hollow shell capable of sequestering up to 4,500 iron atoms (UniProt P02794, P02792). The heavy chain possesses ferroxidase activity, which is essential for converting toxic ferrous iron (Fe2+) into the non-toxic ferric form (Fe3+) for storage, while the light chain facilitates the nucleation and stability of the iron core (StatPearls, Ferritin). Beyond its fundamental role in maintaining iron homeostasis and protecting cells from oxidative damage, ferritin is increasingly recognized for its involvement in various pathologies, including neurodegenerative diseases like neuroferritinopathy and various cancers where it supports rapid proliferation (PubMed, PMID: 33065011). In clinical practice, serum ferritin serves as a critical biomarker for iron deficiency and overload, as well as a non-specific marker of inflammation (NIH, Iron). Therapeutic strategies targeting ferritin include iron chelation therapy for transfusion-related iron overload and emerging approaches that modulate ferritin levels to induce ferroptosis in treatment-resistant tumors (PubMed, PMID: 31010913).

Other names

FerritinL-ferritinH-ferritinFTLFTH1Ferritin H subunitFerritin L subunitNBIA3

Iron chelation (binding and removing iron from the complex), iron supplementation (increasing iron stores), and modulation of ferritin degradation to induce ferroptosis.