Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell

Watt, Richard K.; Hilton, Robert J.; Graff, D. Matthew

doi:10.1016/j.bbagen.2010.03.001

Cited by 78 publications

(60 citation statements)

References 140 publications

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“…The addition of phosphates to Ftns was shown to accelerate the oxidation and iron loading rates. It was suggested that phosphate also aids the migration of iron from the ferroxidase center to the Ftn core [23].…”

Section: Iron Mineralizationmentioning

confidence: 99%

Ferritin Iron Mineralization and Storage: From Structure to Function

2016

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Section: Iron Mineralizationmentioning

confidence: 99%

Ferritin Iron Mineralization and Storage: From Structure to Function

2016

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“…Several mechanisms allow iron to be released from ferritin as the LIP is depleted (Romeo et al 2001;De Domenico et al 2009;Kidane et al 2006). Recent studies have examined how this reaction might occur in vivo (De Domenico et al 2009) and in vitro (Theil et al 2008;Johnson et al 2011;Watt et al 2010).…”

mentioning

confidence: 97%

The many faces of the octahedral ferritin protein

Watt

2011

Biometals

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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.

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“…Second, genetic mutations affecting either the structure of the ferritin polypeptide [23], or the H [24] or L [25] ferritin mRNA IRE regions this leading to undesirable H/L ratios in the ferritin shells have been recently reported. Both mentioned pathways of ferritin dysfunctions have been intensively studied, related to neurological disorders and reviewed [26].…”

Section: Fig 1 Horse Spleen Ferritin Structure: a 24-subunit Oligommentioning

confidence: 99%

Ferritin iron uptake and release in the presence of metals and metalloproteins: Chemical implications in the brain

Carmona

Palacios

Gálvez

et al. 2013

Coordination Chemistry Reviews

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Living organisms have developed a chemical machinery based on the ferritin protein for the storage, under a nontoxic form, of the iron that is not required for immediate metabolic purposes. Whereas free iron causes extensive cell damage, ferritin iron is not toxic, yet still available for cell requirements. However, iron storage in ferritin is increasingly being recognized as a crucial process related with some neurodegenerative disorders and therefore, an understanding of the management of iron in the brain, especially the processes of iron uptake and release in ferritin, is compulsory to clarify the role of this metalloprotein in these neuropathologies.Although knowledge of iron storage and iron release in ferritin is nowadays still limited, even less information is currently available about the influence of free metal ions and other brain metalloproteins in these processes.In this sense, this review is an excellent opportunity to collect all the information today available about the influence of metals and metalloproteins in ferritin loading and unloading events, which until now are dispersed in the literature.Furthermore, we will focus on the importance of all the above-mentioned interactions in the brain, since the importance of the correct and safe balance of metals in the brain after their well-known implication in neurodegenerative 52 processes such as the lzheimer's ( ), Parkinson (P ) and prion protein (PP ) diseases is obvious. In this work, we will not only recall the importance and role of ferritin in the brain but also the putative influence of the interaction between ferritin and some metals and/or metalloproteins and other biomolecules on these neurological dysfunctions. The final part of the review will be devoted to draw some guidelines to where the future prospects point to on the basis of the existing information.

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Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell

Cited by 78 publications

References 140 publications

Ferritin Iron Mineralization and Storage: From Structure to Function

Ferritin Iron Mineralization and Storage: From Structure to Function

The many faces of the octahedral ferritin protein

Ferritin iron uptake and release in the presence of metals and metalloproteins: Chemical implications in the brain

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