A new approach to the ferritin iron core growth: influence of the H/L ratio on the core shape

López-Castro, Juan de Dios; Delgado, Juan J.; Pérez-Omil, Jose A.; Gálvez, Natividad; Cuesta, Rafael; Watt, Richard K.; Domínguez‐Vera, José M.

doi:10.1039/c1dt11205h

Cited by 59 publications

(59 citation statements)

References 27 publications

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“…The average size of iron cores of ferritin in the hippocampus measured by electron 70 microscopy was about 3.1 nm. In agreement with previous studies reported by our group [66], which correlate size and morphology of the ferritin core with shell composition, this small size should correspond to a high content of H subunits, in agreement with ELISA studies that revealed a higher average concentration of H ferritin (150 ± 30 ng/mg) than L ferritin (20 ± 10 ng/mg) on the same type of samples [100].…”

Section: Fig 6 Predominant Ferritin Type (H-or L-rich) In Neuron Ansupporting

confidence: 80%

“…62 In this context, and after a transmission electron microscopy study of horse spleen, heart and recombinant H and L ferritins, we have recently proposed a new model for the ferritin iron core growth based on 24-n nucleation sites (where n is the number of H subunits) [66]. This implies that only L subunits participate in the mineral growth with a nucleation center per subunit.…”

Section: Ferritin Iron Uptakementioning

confidence: 99%

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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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Section: Fig 6 Predominant Ferritin Type (H-or L-rich) In Neuron Ansupporting

confidence: 80%

Section: Ferritin Iron Uptakementioning

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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“…Safe tissue packaging of cellular iron is accomplished by the ferritin protein, a sphere-like shell composed of 24 H and L ferritin subunits. The L:H ratio of the ferritin molecule varies according to tissue type; L-rich ferritin is abundant in iron-storage organs such as the liver and spleen while H-rich ferritin is found in organs of low iron content such as the heart and brain [38]. While L-rich protein has prolonged turnover time and is more resistant to proteolysis than H-rich protein [39], it is the H-ferritin subunit that possesses the ferroxidase ability required for a functional ferritin molecule [40, 41].…”

Section: Discussionmentioning

confidence: 99%

mRNA regulation of cardiac iron transporters and ferritin subunits in a mouse model of iron overload

Brewer

Wood

2014

Experimental Hematology

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Iron cardiomyopathy is the leading cause of death in iron overload. Men have twice the mortality rate of women, though the cause is unknown. In hemojuvelin-knockout mice, a model of the disease, males load more cardiac iron than females. We postulated that sex differences in cardiac iron import cause differences in cardiac iron concentration. RT-PCR was used to measure mRNA of cardiac iron transporters in hemojuvelin-knockout mice. No sex differences were discovered among putative importers of non-transferrin bound iron (L-type and T-type calcium channels, ZRT/IRT-like protein 14 zinc channels). Transferrin-bound iron transporters were also analyzed; these are controlled by the iron regulatory element/iron regulatory protein (IRE/IRP) system. There was a positive relationship between cardiac iron and ferroportin mRNA in both sexes, but it was significantly steeper in females (p<0.05). Transferrin receptor 1 and divalent metal transporter 1 were more highly expressed in females than males (p<0.01 and p<0.0001, respectively), consistent with their lower cardiac iron levels, as predicted by IRE/IRP regulatory pathways. Light-chain (L) ferritin showed a positive correlation with cardiac iron that was nearly identical in males and females (R2=0.41, p<0.01 and R2=0.56, p<0.05, respectively), while heavy-chain (H) ferritin was constitutively expressed in both sexes. This represents the first report of IRE/IRP regulatory pathways in the heart. Transcriptional regulation of ferroportin was suggested in both sexes, creating a potential mechanism for differential set points for iron export. Constitutive H-ferritin expression suggests a logical limit to cardiac iron buffering capacity at levels known to produce heart failure in humans.

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“…The structure of the iron core in ferritin is intensively studied by various structural techniques such as electron nanodiffraction and high resolution electron microscopy. As a result, various models of the corefrom monocrystalline to polyphasic -have been suggested [29][30][31][32][33]. It should be noted that Mössbauer spectra of ferritin and its analogues, both in paramagnetic and magnetic states, were also fitted using different approaches: 1) using a model-free way with a distribution function of quadrupole splitting or magnetic hyperfine field, 2) using one quadrupole doublet or one magnetic sextet, 3) using more than one spectral component.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the Debye temperature for iron cores in human liver ferritin and its pharmaceutical analogue, Ferrum Lek, using Mössbauer spectroscopy

Dubiel

Cieślak

Alenkina

et al. 2014

Journal of Inorganic Biochemistry

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An iron-polymaltose complex Ferrum Lek used as antianemic drug and considered as a ferritin analogue and human liver ferritin were investigated in the temperature range of 295-90 K by means of 57 Fe Mössbauer spectroscopy with a high velocity resolution (in 4096 channels). The Debye temperatures Ө D =50224 K for Ferrum Lek and Ө D =46116 K for human liver ferritin were determined from the temperature dependence of the center shift obtained using two different fitting procedures.

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A new approach to the ferritin iron core growth: influence of the H/L ratio on the core shape

Cited by 59 publications

References 27 publications

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

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

mRNA regulation of cardiac iron transporters and ferritin subunits in a mouse model of iron overload

Evaluation of the Debye temperature for iron cores in human liver ferritin and its pharmaceutical analogue, Ferrum Lek, using Mössbauer spectroscopy

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