caa a22 4500 44532158X CHVBK 20180317142705.0 cr unu---uuuuu 170323e20110601xx s 000 0 eng 10.1007/s10534-011-9415-8 doi (NATIONALLICENCE)springer-10.1007/s10534-011-9415-8 Watt Richard Department of Chemistry and Biochemistry, Brigham Young University, C-210 BNSN Building, 84604, Provo, UT, USA aut The many faces of the octahedral ferritin protein [Elektronische Daten] [Richard Watt] Iron is an essential trace nutrient required for the active sites of many enzymes, electron transfer and oxygen transport proteins. In contrast, to its important biological roles, iron is a catalyst for reactive oxygen species (ROS). Organisms must acquire iron but must protect against oxidative damage. Biology has evolved siderophores, hormones, membrane transporters, and iron transport and storage proteins to acquire sufficient iron but maintain iron levels at safe concentrations that prevent iron from catalyzing the formation of ROS. Ferritin is an important hub for iron metabolism because it sequesters iron during times of iron excess and releases iron during iron paucity. Ferritin is expressed in response to oxidative stress and is secreted into the extracellular matrix and into the serum. The iron sequestering ability of ferritin is believed to be the source of the anti-oxidant properties of ferritin. In fact, ferritin has been used as a biomarker for disease because it is synthesized in response to oxidative damage and inflammation. The function of serum ferritin is poorly understood, however serum ferritin concentrations seem to correlate with total iron stores. Under certain conditions, ferritin is also associated with pro-oxidant activity. The source of this switch from anti-oxidant to pro-oxidant has not been established but may be associated with unregulated iron release from ferritin. Recent reports demonstrate that ferritin is involved in other aspects of biology such as cell activation, development, immunity and angiogenesis. This review examines ferritin expression and secretion in correlation with anti-oxidant activity and with respect to these new functions. In addition, conditions that lead to pro-oxidant conditions are considered. Springer Science+Business Media, LLC., 2011 Ferritin nationallicence Iron storage nationallicence Anti-oxidant nationallicence Pro-oxidant nationallicence Iron-regulation nationallicence BioMetals Springer Netherlands 24/3(2011-06-01), 489-500 0966-0844 24:3<489 2011 24 10534 https://doi.org/10.1007/s10534-011-9415-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10534-011-9415-8 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Watt Richard Department of Chemistry and Biochemistry, Brigham Young University, C-210 BNSN Building, 84604, Provo, UT, USA aut NATIONALLICENCE 773 0- BioMetals Springer Netherlands 24/3(2011-06-01), 489-500 0966-0844 24:3<489 2011 24 10534 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer