Ferritin and metallothionein: dangerous liaisons

Orihuela, Rubén; Fernández, Belén; Palacios, Òscar; Valero, Elsa; Atrian, Sı́lvia; Watt, Richard K.; Domínguez‐Vera, José M.; Capdevila, Mercè

doi:10.1039/c1cc14819b

Cited by 27 publications

(34 citation statements)

References 29 publications

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“…MTs are small (6–10 kDa), cysteine-rich (33%) metalloproteins that catalyze redox reactions and contain metal binding sites. Although they are mainly involved in the homeostasis of physiological Zn 2+ , they still exhibit the capacity to bind iron because they are thiolate-rich biomolecules33. Considering that the expression of Mt1a and Mt2A was significantly increased in the Fe-Gly group, we speculate that a much larger amount of iron was indeed absorbed into the intestinal epithelia of the rats in this group.…”

Section: Discussionmentioning

confidence: 78%

Digital gene expression profiling analysis of duodenum transcriptomes in SD rats administered ferrous sulfate or ferrous glycine chelate by gavage

Zhao

Fang

et al. 2016

Sci Rep

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The absorption of different iron sources is a trending research topic. Many studies have revealed that organic iron exhibits better bioavailability than inorganic iron, but the concrete underlying mechanism is still unclear. In the present study, we examined the differences in bioavailability of ferrous sulfate and ferrous glycinate in the intestines of SD rats using Illumina sequencing technology. Digital gene expression analysis resulted in the generation of almost 128 million clean reads, with expression data for 17,089 unigenes. A total of 123 differentially expressed genes with a |log2(fold change)| >1 and q-value < 0.05 were identified between the FeSO4 and Fe-Gly groups. Gene Ontology functional analysis revealed that these genes were involved in oxidoreductase activity, iron ion binding, and heme binding. Kyoto Encyclopedia of Genes and Genomes pathway analysis also showed relevant important pathways. In addition, the expression patterns of 9 randomly selected genes were further validated by qRT-PCR, which confirmed the digital gene expression results. Our study showed that the two iron sources might share the same absorption mechanism, and that differences in bioavailability between FeSO4 and Fe-Gly were not only in the absorption process but also during the transport and utilization process.

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Section: Discussionmentioning

confidence: 78%

Digital gene expression profiling analysis of duodenum transcriptomes in SD rats administered ferrous sulfate or ferrous glycine chelate by gavage

Zhao

Fang

et al. 2016

Sci Rep

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“…Likewise, a combination of computational modeling methods allowed showing how flavin molecules bind to the ferritin protein surface and transfer electrons across the protein shell reaching the iron core [82]. We also recently demonstrated that some metallothioneins can promote iron release from ferritin by pumping electrons through the shell that reduce iron(III) to iron(II), which diffuses into the intracellular milieu [42].…”

Section: Fig 5 Schematic Representation Of the Two Main Mechanisms mentioning

confidence: 99%

“…Otherwise, some metalloproteins such as ceruloplasmin [41] or metallothioneins [42] are capable to respectively promote the uptake or the removal of iron from ferritin, the latter giving rise not only to the existence to free toxic iron(II) but also to putatively damaging free copper(I) or zinc(II) ions that were initially bound to it. Other biomolecules such as glutathione (GSH), xanthine oxidase and superoxide dismutase (SOD) have also been reported to interact with ferritin (cf.…”

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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“…If, according to the present results and those of Hagen and coworkers, [10] the Fe III ions produced at the Ft ferroxidase centers are available for complexation by a large molecule such as transferrin, it should also be able to act as an oxidant against metallothioneins (MTs). [12] This possibility takes special relevance in view of the Fenton reactivity of Cu I/II ions and the widely assumed presence of copper-containing MTs in brain cells. Bearing this in mind, we studied the iron reconstitution of the two different ferritins from our study (i.e., HuFtH and HsFt) in the presence of the copper-loaded forms of two mammalian MT isoforms (i.e., MT2 and MT3).…”

Section: Resultsmentioning

confidence: 99%

“…However, if this imbalance in L-and H-subunit synthesis leads to the synthesis of pure H apoferritins, and therefore to some events analogous to those we have described here in which the high ferroxidase activity and low Fe [12] provided that the correct combination of isoforms is preserved, otherwise metal-related neuronal disorders could be triggered if parting from this ideal combination.…”

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confidence: 79%

Chemically and Biologically Harmless versus Harmful Ferritin/Copper–Metallothionein Couples

Carmona

Mendoza

Kord

et al. 2014

Chemistry A European J

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Ferritin and metallothionein: dangerous liaisons

Abstract: Ferritin (Ft) interaction with the Zn-complexes of mammalian MT1, MT2 and MT3 metallothioneins (MT) leads to simultaneous Fe(II) and Zn(II) release.

Cited by 27 publications

References 29 publications

Digital gene expression profiling analysis of duodenum transcriptomes in SD rats administered ferrous sulfate or ferrous glycine chelate by gavage

Digital gene expression profiling analysis of duodenum transcriptomes in SD rats administered ferrous sulfate or ferrous glycine chelate by gavage

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

Chemically and Biologically Harmless versus Harmful Ferritin/Copper–Metallothionein Couples

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