• Applied Biological Chemistry
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• v.41 no.7
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• pp.522-526
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• 1998

Ferritin from germinated soybean seeds was purified by ammonium sulfate precipitation (0.55 saturation), ion-exchange chromatography on DEAE-cellulose, gel filtration chromatography on Sephacryl S-300, and HPLC with Bio-Scale Q2 column. SDS-PAGE analysis showed that the purified ferritin is composed of subunit with an apparent M, 21,000. The molecular mass of the native soybean ferritin estimated by gel filtration on Sephacryl S-300 and non-denaturing polyacrylamide gel electrophoresis appeared to be $510{\sim}560\;kDa$. Soybean ferritin contained 833 mol Fe/mol protein, which is 31-fold more iron than pumpkin ferritin and stained positive for iron on non-denaturing gel. Soybean ferritin cross-reacted with anti-soybean rabbit ferritin antiserum.

• BMB Reports
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• v.28 no.3
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• pp.238-242
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• 1995

The tadpole H-ferritin produced in E. coli was purified and its molecular properties were investigated to obtain information about the contribution of the H-subunit in the reaction of iron core formation. All the expressed subunits were assembled into complete holoprotein in vitro, presumably 24-mer, and the protein was heat-stable. Electron microscopy revealed that the recombinant ferritin forms spherically and contains iron core. No difference was observed in the absorption spectrum of the expressed protein compared to that of the natural ferritin. The Ouchterlony double diffusion of the expressed protein showed that the H-chain ferritin shares an antigenic determinant with natural tadpole ferritin. Rabbit anti-horse spleen ferritin discriminated the H-ferritin from natural ferritin. The rate of ferritin formation by the recombinant H-chain apoferritin was determined to be higher than that shown by natural tadpole ferritin, which consists of H, M and L-subunits. This phenomenon may be caused by the absence of M and L-subunits in the recombinant H-chain apoferritin.

• Applied Biological Chemistry
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• v.41 no.3
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• pp.224-227
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• 1998

The expression of ferritin involved in iron metabolism is regulated at the translational level by the interaction of iron regulatory protein with iron-responsive element(IRE) in the 5'-untranslated region of ferritin transcript. To identify the role of structural element utilized for translational regulation of ferritin, we studied the effects of mutations in the ferritin IRE by measuring IRP binding activity and translational activity. Our data suggest that the cytosine at bulged position of IRE within ferritin is important for the formation of RNA secondary structure involved in translational regulation.

• Journal of Hospice and Palliative Care
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• v.18 no.1
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• pp.51-59
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• 2015

Purpose: Predicting life expectancy of terminally ill cancer patients is very important. In many studies, ferritin is detected at higher levels in the sera of cancer patients, and higher ferritin level correlates with aggressiveness of disease and poor outcomes of patients. This study evaluated a prognostic role of serum ferritin levels in terminally ill cancer patients. Methods: This study enrolled 65 terminally ill cancer patients from March through June 2012. We assessed routine laboratory findings including serum ferritin levels as well as demographic and clinical characteristics of the patients. To examine the association between serum ferritin levels and patient's characteristics, we used Spearman's correlation analysis, Wilcoxon's rank sum test or Kruskal-Wallis test, as appropriately. For multivariate analysis, Cox's proportional hazard regression model was used to evaluate significance of serum ferritin levels as a prognostic factor. Results: A negative correlation between serum ferritin levels and survival time was found. After adjusting for sex, age, performance status, creatinine levels and white blood cell counts, serum ferritin levels were significantly associated with survival time. Conclusion: Even at the very end of life of terminal cancer patients, serum ferritin levels were an independent prognostic factor for survival.

• BMB Reports
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• v.44 no.3
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• pp.165-169
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• 2011

Excess free iron generates oxidative stress that may contribute to the pathogenesis of various causes of neurodegenerative diseases. In this study, we assessed the modification of ferritin induced by $H_2O_2$. When ferritin was incubated with $H_2O_2$, the degradation of ferritin L-chain increased with the $H_2O_2$ concentration whereas ferritin H-chain was remained. Free radical scavengers, azide, thiourea, and N-acetyl-$_L$-cysteine suppressed the $H_2O_2$-mediated ferritin modification. The iron specific chelator, deferoxamine, effectively prevented $H_2O_2$-mediated ferritin degradation in modified ferritin. The release of iron ions from ferritin was increased in $H_2O_2$ concentration-dependent manner. The present results suggest that free radicals may play a role in the modification and iron releasing of ferritin by $H_2O_2$. It is assumed that oxidative damage of ferritin by $H_2O_2$ may induce the increase of iron content in cells and subsequently lead to the deleterious condition.

• Journal of the East Asian Society of Dietary Life
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• v.16 no.1
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• pp.93-98
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• 2006

This study examined whether or not the iron that is accumulated in the recombinant microbes that produce ferritin is bioavailable to rats with iron deficiency. Rats induced with iron deficiency were treated with iron preparations of $Fe(NH_4)_2(SO_4)_2$, horse spleen ferritin, control yeast, and ferritin-producing recombinant yeast for 14 days. The bioavailability of iron was examined by measuring hemoglobin concentration, hematocrit value, and tissue iron stores. Differences between dietary groups were determined by one-way ANOVA, at the level of significance p<0.05. Based on hemoglobin concentration and hematocrit value, iron in $Fe(NH_4)_2(SO_4)_2$, horse spleen ferritin, and ferritin-producing yeast were bioavailable in rats and cured iron deficiency. The efficacy of ferritin and ferritin-producing yeast was confirmed in establishing tissue iron stores after the induction of iron deficiency. The iron sources of ferritin and the ferritin-producing yeast seemed to be as effective for the recovery from iron deficiency as the iron compounds of ferric citrate and ferrous ammonium sulfate. The results suggest that the iron stored in ferritin of the recombinant yeast is bioavailable, and that the recombinant yeast may contribute widely as a source of iron to resolve the global problem of iron deficiency.

• Biotechnology and Bioprocess Engineering:BBE
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• v.10 no.6
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• pp.500-504
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• 2005

Fusion ferritin (heavy chain ferritin, $F_H+$ light chain ferritin, $F_L$), an iron-binding protein, was primarily purified from recombinant Escherichia coli by two-step sonications with urea [1]. Unfolded ferritin was refolded by gel filtration chromatography (GFC) with refolding enhancer, where 50 mM Na-phosphate (pH 7.4) buffer containing additives such as Tween 20, PEG, and L-arginine was used. Ferritin is a multimeric protein that contains approximately 20 monomeric units for full activity. Fusion ferritin was expressed in the form of inclusion bodies (IBs). The IBs were initially solubilized in 4 M urea denaturant. The refolding process was then performed by decreasing the urea concentration on the GFC column to form protein multimers. The combination of the buffer-exchange effect of GFC and the refolding enhancers in refolding buffer resulted in an efficient route for producing properly folded fusion ferritin.

• International Journal of Industrial Entomology and Biomaterials
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• v.4 no.2
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• pp.163-168
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• 2002

We report for the first time the cDNA sequence encoding a ferritin subunit from the spiders Araneus ventricosus. The complete cDNA sequence of A. ventricosus ferritin subunit comprised 516 bp with 172 amino acid residues. The A. ventricosus ferritin subunit cDNA contained a conserved iron responsive element sequence in the 5 untranslated region. An alignment of the deduced protein sequence of the A. ventricosus ferritin subunit gene to that of other heavy chain ferritin molecules showed that A. ventricosus ferritin subunit is most similar to the great pond snail, Lymnaea stagnalis, ferritin with 70.2% of protein sequence identity.

• Journal of Microbiology and Biotechnology
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• v.14 no.1
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• pp.68-73
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• 2004

Ferritin is an iron storage protein found in most living organisms. For expression and industrial use, human light chain ferritin (L-ferritin) was cloned from human liver cDNA library and expressed in Pichia pastoris strain GS115. The recombinant L-ferritin in Pichia pastoris was glycosylated. In a fed-batch culture, the cell mass reached about 57 g/l of dry cell weight, and the L-ferritin in the cell was increased to about 95 mg/l after 150 h. In an atomic absorption spectrometry analysis, the intracellular content of iron in the L-ferritin transformant was measured as $1,694{\pm}85\;\mu\textrm{g}g/g$, which is 5.4-fold more than that of the control strain. This L-ferritin transformant could serve as iron-fortified nutrients in animal feed stock.

• BMB Reports
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• v.46 no.4
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• pp.225-229
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• 2013

Methylglyoxal (MG) is an endogenous metabolite which is present in increased concentrations in diabetics and reacts with amino acids to form advanced glycation end products. In this study, we investigated whether ferritin enhances DNA cleavage by the reaction of MG with lysine. When plasmid DNA was incubated with MG and lysine in the presence of ferritin, DNA strand breakage was increased in a dose-dependent manner. The ferritin/MG/lysine system-mediated DNA cleavage was significantly inhibited by reactive oxygen species (ROS) scavengers. These results indicated that ROS might participate in the ferritin/MG/lysine system-mediated DNA cleavage. Incubation of ferritin with MG and lysine resulted in a time-dependent release of iron ions from the protein molecules. Our data suggest that DNA cleavage caused by the ferritin/MG/lysine system via the generation of ROS by the Fenton-like reaction of free iron ions released from oxidatively damaged ferritin.