As a spherical
protein that acts as a repository for intracellular
iron,
Ferritin is the most important
iron storage form and is known to influence
tumor immunity. Unbound
ferritin is composed of 24 subunits, made up of
ferritin light chain (FTL) and
ferritin heavy chain (FTH).
Ferritin can be automatically put together to form hollow nanocages that measure 12 nm around the outside and 8 nm around the inside.
Cancer causes the second-most deaths worldwide, effective elimination of
tumor cells while protecting normal cells is the foundation of modern
tumor therapy. To this end, the innate
tumor-targeting activity of human FTH1, first identified ten years ago, is highly appealing. Unmodified human FTH1 binds to its
receptor, transferrin receptor 1 (TfR1), which is frequently overexpressed in
cancer cells. FTH1-TfR1 binding permits improved
drug efficacy by promoting
ferritin-mediated targeted delivery. In addition, FTH is also associated with the prognosis of multiple typies of
cancer. The level of FTH1 is significantly and positively correlated with the infiltration of tumor-associated macrophages. FTH1 also plays an important role in regulating the
tumor immunity of solid
cancer. As such, FTH1 has been extensively applied in the targeted delivery of anticancer drugs, diagnostic molecules (e.g.,
radioisotopes and fluorophones), and inorganic nanoparticles (NPs) to
tumors.This article reviews the role of FTH in
cancer and its potential as a therapeutic target.