Regulation of labile iron with glutathione and ferritin | Poster Board #1803

Iron plays an essential role in a variety of biological processes, such as oxygen transport via hemoglobin or by acting as a cofactor of a variety of proteins. Unfortunately, iron is also a known oxidizer, which can contribute to the creation of radical species, such as ROS and RNS. These radicals can lead to lipid peroxidation, DNA damage, ferroptosis, and many inflammatory conditions. An understanding of iron regulation is crucial to understanding and preventing these adverse effects and diseases.
Regulation of the labile iron pool (LIP) is the focus of our research. We have found that glutathione (GSH) plays an essential role in this process. GSH is an iron chelator and stabilizes iron in its Fe(II) state, blocks oxygen species from being oxidized, and even reduces them should they be oxidized. Novel findings suggest that GSH also contributes to the storage of iron into a storage protein, ferritin.
Stability of the GS:Fe(II) complex and ferritin iron loading was tracked using the indicator bipyridine. Bipyridine exclusively binds Fe(II) and subsequently absorbs light at 520nm which can be measured using spectrophotometers.