Ferritin heavy chain 1 (FTH1) (FTH1)

Ferritin heavy chain 1 (FTH1) is a critical intracellular protein responsible for the storage and management of iron, playing a central role in maintaining iron homeostasis and protecting cells from oxidative stress [1]. It assembles into a 24-subunit nanocage that sequesters up to 4,500 iron atoms, with the H-subunit specifically providing ferroxidase activity to convert reactive ferrous iron (Fe2+) into stable ferric iron (Fe3+) [1, 2]. In oncology, FTH1 is often overexpressed by tumor cells to support their high metabolic demands, and its targeted degradation—a process known as ferritinophagy—is a prerequisite for inducing ferroptosis, an iron-dependent form of regulated cell death [2, 5]. Beyond its role as a metabolic target, FTH1 is being developed as a versatile nanocarrier for drug delivery and molecular imaging, as it can be internalized through receptors like Transferrin receptor 1 (TfR1) and SCARA5 [3, 6]. Dysregulation of FTH1 is also implicated in neurodegenerative diseases, where iron accumulation contributes to lipid peroxidation and neuronal damage [7]. Consequently, FTH1 represents a multifaceted target for both direct therapeutic intervention and advanced drug delivery systems [3, 8].

Other names

Ferritin heavy chainFTHFTHL6PIG15PLIFFerritin H subunitApoferritinCell proliferation-inducing gene 15 protein

Sequestration of intracellular iron and conversion of ferrous iron (Fe2+) to ferric iron (Fe3+) via ferroxidase activity to prevent oxidative damage; also serves as a ligand for receptor-mediated endocytosis in drug delivery [1, 2, 3].