Ferritins: A family of molecules for iron storage, antioxidation and more

Arosio, Paolo; Ingrassia, Rosaria; Cavadini, Patrizia

doi:10.1016/j.bbagen.2008.09.004

Cited by 740 publications

(657 citation statements)

References 164 publications

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“…In comparison to other iron oxide agents currently available, the proposed magnetoferritin particle is simple to create. To incorporate Fe(III) into the core, ferritin uses O 2 as an oxidant and a catalytic site located in the center of the protein (18). Two routes of iron loading have been identified, a catalytic pathway (due to the ferroxidase on H-ferritin) and an auto oxidative route that becomes important once the metal core has started to form (19,20).…”

Section: Discussionmentioning

confidence: 99%

Simplified synthesis and relaxometry of magnetoferritin for magnetic resonance imaging

Jordan

Caplan

Bennett

2010

Magnetic Resonance in Med

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Magnetoferritin nanoparticles have been developed as highrelaxivity, functional contrast agents for MRI. Several previous techniques have relied on unloading native ferritin and reincorporation of iron into the core, often resulting in a polydisperse sample. Here, a simplified technique is developed using commercially available horse spleen apoferritin to create monodisperse magnetoferritin. Iron oxide atoms were incorporated into the protein core via a step-wise Fe(II)Chloride addition to the protein solution under low O 2 conditions; subsequent filtration steps allow for separation of completely filled and superparamagnetic magnetoferritin from the partially filled ferritin. This method yields a monodisperse and homogenous solution of spherical particles with magnetic properties that can be used for molecular magnetic resonance imaging. With a transverse per-iron and per-particle relaxivity of 78 mM 21 sec 21 and 404,045 mM 21 sec 21 , respectively, it is possible to detect~10 nM nanoparticle concentrations in vivo. Magn Reson Med 64:1260-1266, 2010. V C 2010 Wiley-Liss, Inc.Key words: ferritin; magnetoferritin; molecular imaging; MRI Targeted contrast agents have been developed to detect molecules noninvasively with magnetic resonance imaging (MRI). MRI is non-invasive and inherently threedimensional. MRI contrast agents are being detected in increasingly lower concentrations in vivo (1). Typical molecular MRI requires the binding of contrast agents to a specific site and subsequent removal of the unbound agent. Many of the applications of molecular imaging agents require detection in low (

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Section: Discussionmentioning

confidence: 99%

Simplified synthesis and relaxometry of magnetoferritin for magnetic resonance imaging

Jordan

Caplan

Bennett

2010

Magnetic Resonance in Med

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“…Storage of excess iron in ferritin is essential to prevent iron-mediated oxidative processes and ferritin is therefore a most important anti-oxidant (Arosio et al, 2009, Balla et al, 1992, Balla et al, 1993. Ferritin is a high molecular weight 24-mer consisting of heavy (H-ferritin) and light (L-ferritin) subunits (Harrison and Arosio, 1996).…”

Section: Systemic Iron Homeostasismentioning

confidence: 99%

“…Ferritin is a high molecular weight 24-mer consisting of heavy (H-ferritin) and light (L-ferritin) subunits (Harrison and Arosio, 1996). The ferroxidase activity of the H-chain is responsible for converting Fe(II) to Fe(III) and then together with the L-form for its storage as a ferric oxohydroxide mineral (Arosio et al, 2009). The final complex is a 12 nm wide structure with an 8 nm wide core that may harbor up to 4,500 atoms of iron in a bioavailable but safe form (Chasteen and Harrison, 1999).…”

Section: Systemic Iron Homeostasismentioning

confidence: 99%

The role of lysosomes in iron metabolism and recycling

Kurz

Eaton

Brunk

2011

The International Journal of Biochemistry & Cell Biology

172

134

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Iron is the most abundant transition metal in the earths crust. It cycles easily between ferric (oxidized; Fe(III)) and ferrous (reduced; Fe(II)) and readily forms complexes with oxygen, making this metal a central player in respiration and related redox processes. However, loose iron, not within heme or iron-sulfur cluster proteins, can be destructively redox-active, causing damage to almost all cellular components, killing both cells and organisms. This may explain why iron is so carefully handled by aerobic organisms. Iron uptake from the environment is carefully limited and carried out by specialized iron transport mechanisms. One reason that iron uptake is tightly controlled is that most organisms and cells cannot efficiently excrete excess iron. When even small amounts of intracellular free iron occur, most of it is safely stored in a non-redox-active form in ferritins. Within nucleated cells, iron is constantly being recycled from aged iron-rich organelles such as mitochondria and used for construction of new organelles. Much of this recycling occurs within the lysosome, an acidic digestive organelle. Because of this, most lysosomes contain relatively large amounts of redox-active iron and are therefore unusually susceptible to oxidant-mediated destabilization or rupture. In many cell types, iron transit through the lysosomal compartment can be remarkably brisk. However, conditions adversely affecting lysosomal iron handling (or oxidant stress) can contribute to a variety of acute and chronic diseases. These considerations make normal and abnormal lysosomal handling of iron central to the understanding and, perhaps, therapy of a wide range of diseases

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“…As a consequence, an imbalance in their ratio has the potential to alter the intracellular iron content and availability: ferritin molecules in cells containing high levels of iron, such as liver and spleen, tend to be L-rich, and may have a long-term storage function, whereas H-rich ferritins are more active in rapid iron uptake and release and lead to a cell phenotype more responsive to acute environmental changes (7).…”

Section: Introductionmentioning

confidence: 99%

H ferritin silencing induces protein misfolding in K562 cells: A Raman analysis

Zolea

Biamonte

Candeloro

et al. 2015

Free Radical Biology and Medicine

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The redox state of the cell is involved in the regulation of many physiological functions as well as in the pathogenesis of several diseases, and is strictly dependent on the amount of iron in its catalytically active state.Alterations of iron homeostasis determine increased steady-state concentrations of Reactive Oxygen Species (ROS) that cause lipid peroxidation, DNA damage and altered protein folding. Ferritin keeps the intracellular iron in a non-toxic and readily available form and consequently plays a central role in iron and redox homeostasis. The protein is composed by 24 subunits of the H-and L-type, coded by two different genes, with structural and functional differences. The aim of this study was to shed light on the role of the single H ferritin subunit (FHC) in keeping the native correct protein three-dimensional structure. To this, we performed Raman spectroscopy on protein extracts from K562 cells subjected to FHC silencing. The results show a significant increase in the percentage of disordered structures content at a level comparable to that induced by H 2 O 2 treatment in control cells. ROS inhibitor and iron chelator were able to revert protein misfolding. This integrated approach, involving Raman spectroscopy and targeted-gene silencing, indicates that an imbalance of the heavyto-light chain ratio in the ferritin composition is able to induce severe but still reversible modifications in protein folding and uncovers new potential pathogenetic mechanisms associated to intracellular iron perturbation.

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Ferritins: A family of molecules for iron storage, antioxidation and more

Cited by 740 publications

References 164 publications

Simplified synthesis and relaxometry of magnetoferritin for magnetic resonance imaging

Simplified synthesis and relaxometry of magnetoferritin for magnetic resonance imaging

The role of lysosomes in iron metabolism and recycling

H ferritin silencing induces protein misfolding in K562 cells: A Raman analysis

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