Multiple mechanisms of iron-induced ferritin synthesis in HeLa cells

Cairo, Gaetano; Bardella, Lidia; Schiaffonati, Luisa; Arosio, Paolo; Levi, Sonia; Bernelli‐Zazzera, Aldo

doi:10.1016/0006-291x(85)91877-7

Cited by 119 publications

(61 citation statements)

References 20 publications

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“…Specific members of the ferritin subunit family can be induced by excess iron in animals (25)(26)(27). To determine whether iron induces the same or different ferritin mRNA in plants, the sequence of a ferritin cDNA clone from a library constructed with poly(A)+ RNA from iron-induced soybean cells was compared to that from hypocotyl cDNA.…”

Section: Resultsmentioning

confidence: 99%

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Ferritin gene transcription is regulated by iron in soybean cell cultures.

Lescure

Proudhon

Pesey

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

171

164

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Section: Resultsmentioning

confidence: 99%

“…Iron-induced transcription and/or accumulation of ferritin mRNA also occur in animals. The effects are subunit-specific and are coupled to increases in translation (25)(26)(27)(28) and, apparently, to detoxification of the excess iron.…”

mentioning

confidence: 99%

Ferritin gene transcription is regulated by iron in soybean cell cultures.

Lescure

Proudhon

Pesey

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

171

164

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“…This is supported by the stimuli and mechanisms involved in controlling their expression, mostly related to iron and stress, both at the transcriptional and the translational levels (Torti and Torti 2002;Theil 2007). Transcriptional mechanisms are involved in determining the tissue specific H to L ratio and are only modestly elicited by chronic iron supplementation (Cairo et al 1985). However heme was shown to be a strong inducer in some cellular systems: it acts by removing Bach1 repressor and permitting the binding of the transcription factor Nrf2 (Hintze and Theil 2006;Hintze et al 2007).…”

Section: Regulation Of Ferritin Expressionmentioning

confidence: 99%

Biology of ferritin in mammals: an update on iron storage, oxidative damage and neurodegeneration

2014

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Iron is an abundant transition metal that is essential for life, being associated to many enzyme and oxygen carrier proteins involved in a variety of fundamental cellular processes. At the same time the metal is potentially toxic due to its capacity to engage in the catalytic production of noxious reactive oxygen species. The control of iron availability in the cells is largely dependent on ferritins, ubiquitous proteins with storage and detoxification capacity. In mammals, cytosolic ferritins are composed of two types of subunits, the H and the L chain, assembled to form a 24-mer spherical cage. Ferritin is present also in mitochondria, in the form of a complex with 24 identical chains. Even though the proteins have been known for a long time, their study is a very active and interesting field yet. In this review we will focus our attention to mammalian cytosolic and mitochondrial ferritins, describing the most recent advancement regarding their storage and antioxidant function, the effects of their genetic mutations in human pathology, and also the possible involvement in non-iron related activities. We will also discuss recent evidence connecting ferritins and the toxicity of iron in a set of neurodegenerative disorder characterized by focal cerebral siderosis. IntroductionThe adaptation of life to an oxic environment required the development of mechanisms to deal with the transformation of the water soluble ferrous ion (Fe 2+ ) to the insoluble ferric ion (Fe 3+ ) and with the concomitant generation of dangerous reactive oxygen species (ROS). The ferritin molecules represent an important and ancient mean developed by organisms in the three domains of life to safely handle the necessary, yet potentially toxic metal. Their ability to detoxify and store the metal through safe oxidation processes protects the cells from undue iron-dependent redox chemistry, while a controlled release of the metal guarantees its availability for different and essential enzymatic reactions. Storage and detoxification of iron represent the main functions of these molecules, and much work has been done to understand the chemical and molecular details of this

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“…The regulated expression of FTH appears to be of particular importance for cellular adaptation to Fe overload [26,31]. Transcriptional mechanisms are strictly involved in determining the tissuespecific H to L ratio [32]. In the case of oxidative stress, a significant elevation in the expression of ferritin-coding mRNA can be achieved [33].…”

Section: Functions Of Ferritin In Organismsmentioning

confidence: 99%