Ferritin light chain

Iron is extremely important in the development of neurons, transport through iron-sulfur clusters, the electron transport chain, and synthesis and breakdown of neurotransmitters. The function of the FTL is to act as both an iron reservoir and to remove excess iron from the body. Since iron plays a role in electron transfer, there is potential for the generation of free, highly toxic radicals which makes the role of the FTL as an iron detoxifier very significant. The rates of iron uptake and release may be affected by changes to the components of the ferritin light chains and heavy chains. == Clinical significance ==

Oxidative stress caused by iron radicals generated in the ETC and an increase in iron levels caused by defects in the FTL gene has been known to be a cause of the onset of neurodegenerative diseases and hyperferritinemia-cataract syndrome. Elevated levels of FTL1 may be associated with age-related cognitive decline. Mutations of the FTL gene cause the rare adult-onset basal ganglia disease also known as neuroferritinopathy. These mutations are specifically in exon four of the FTL gene. There are two distinct toxic mechanisms that lead to neuroferritinopathy and these are abnormalities in iron metabolism and the creation of free iron radicals, resulting in oxidative stress and cell death. == Interactions ==

Ferritin light chain has been shown to interact with FTH1. An oxygen molecule acts as the terminal electron acceptor during the oxidation of iron in aerobic metabolism. A study conducted with different apoferritins with distinct compositions of heavy and light subunits revealed that both subunits have key roles in the electron transport chain. == See also ==