Ferritin (primary iron storage protein), and Hemosiderin (secondary storage form in iron overload) (Ferritin (FT); Hemosiderin (no widely accepted abbreviation))

Body iron stores encompass the total iron available in the body, primarily stored intracellularly as the protein **ferritin** and, in overload states, as **hemosiderin**[4]. Ferritin is a globular, 24-subunit protein with a hollow cavity capable of storing up to 4,500 iron atoms as Fe(III), serving as the main regulated intracellular iron buffer[3][6]. Hemosiderin is a less structured, insoluble aggregate formed from ferritin breakdown once storage capacity is exceeded, commonly found in liver, spleen, bone marrow, and muscle[4]. Regulation of iron storage involves iron-responsive elements (IREs) in mRNA and iron regulatory proteins (IRPs), which control translation of proteins such as ferritin and transferrin receptors, adapting to body iron supply[1]. Iron stores are essential for growth, DNA synthesis, immunity, and erythropoiesis, but excessive accumulation leads to cellular toxicity, oxidative stress, and organ failure[2][4][6]. In summary: "Body iron stores" is not a molecule or receptor and should not be used as a canonical drug target. The relevant molecular targets are the proteins involved in iron storage and regulation, predominantly ferritin.

Other names

Total body ironiron reservessystemic ironferritin ironhemosiderin iron

Chelators bind and remove stored iron from ferritin/hemosiderin. Supplements increase available iron for storage and utilization. Hepcidin modulators regulate systemic iron release via ferroportin, indirectly affecting body iron stores.