ABSTRACT
This chapter describes the work involving molecular identification and characterization of a novel ferritin H chain complementary deoxyribonucleic acid from the adult and fetal human brains. Ferritin, a 480-kDa protein, is composed of 24 subunits of a 21-kDa heavy chain and a 19-kDa light chain. Ferritin is an important protein involved in the regulation of iron and it is evident that the H subunit is of major significance in the central nervous system. Free intracellular iron regulates the rates of synthesis of ferritin and transferrin receptors. In higher organisms, iron bound to transferrin and ferritin constitutes more than 90% of non-heme iron. Both the proteins also sequester other metal ions including aluminum. High performance liquid chromatography of human brain ferritin revealed several distinct molecular species of brain FTH but, only one major species of ferritin L chain was identified. The accumulation of iron and the synthesis of ferritin in the human brain is developmentally regulated.
