• Korean Journal of Clinical Laboratory Science
• /
• v.48 no.4
• /
• pp.287-295
• /
• 2016

This study was conducted to assess the relationship amongst serum ferritin, and metabolic syndrome (MetS) and metabolic syndrome score (MSS) in Korean adults. The data of 16,096 adults (6,840 men as well as 4,916 premenopausal and 4,340 postmenopausal women) aged ${\geq}20years$ in the Korean National Health and Nutrition Examination Survey (KNHANES) between 2010 and 2012 were analyzed. The prevalence rate of MetS was 3,978 (24.7%) (men, 24.6%; premenopausal women, 11.1%; postmenopausal women, 40.3%). The key study results were as follows: First, after the adjustment for relevant variables, the serum ferritin level ($M{\pm}SE$) was significantly higher (p<0.001) in the MetS group (men, $132.25{\pm}1.98ng/mL$; premenopausal women, $39.89{\pm}1.49ng/mL$; postmenopausal women, $73.45{\pm}1.14ng/mL$) than in the non-MetS group (men, $111.08{\pm}1.01ng/mL$; premenopausal women, $32.26{\pm}0.50ng/mL$; postmenopausal women, $63.26{\pm}0.98ng/mL$). Second, the serum ferritin levels increased as MSS increased in all groups (men, premenopausal women, and postmenopausal women) (p<0.001). In conclusion, MetS and MSS increases were positively associated with higher serum ferritin levels.

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

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.33 no.3
• /
• pp.542-548
• /
• 2004

This study consisted of designing a sensitive assay to measure the rate of L-ascorbic acid (AsA)-prompted release of ferritin iron, the use of ferrozine as a chelating agent to trap releases Fe(II). The initial rate of iron release was measured in the appearance of Fe(ferrozine)$_3$$^{2+}$ at 562 nm. The release of iron from ferritin by AsA was dependent on time and AsA conditions under aerobic and anaerobic conditions. Effect of oxygen on the release of iron from ferritin was also confirmed. It was suggested that the release of iron from ferritin was participate not only AsA but also $O_2$$^{[-10]}$ . In this study, it was found that iron can be released from ferritin and chelate as Fe(ferrozine)$_3$$^{2+}$ and the release was more than 50% in the presence of AsA without $O_2$$^{[-10]}$ . Based on the findings, the following can be assumed (1) AsA is diffused into ferritin (2) ferric ion is reduced to ferrous ion (3) is diffused from ferritin.tin.

• BMB Reports
• /
• v.44 no.3
• /
• pp.165-169
• /
• 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 Microbiology and Biotechnology
• /
• v.17 no.10
• /
• pp.1695-1699
• /
• 2007

Ferritin is an iron storage protein found in most living organisms as a natural assembled macromolecule. For studying the functional ability of the ferritin assembly, human H- and L-ferritins were expressed and purified from Pichia pastoris strain GS115. The recombinant H- and L-ferritins showed a globular form with transmission electron microscopy. The rate of iron uptake for H-ferritin was significantly faster than that for the L-ferritin in vitro. By gel permeation chromatography analysis, recombinant ferritins were confirmed as multimeric subunits with high molecular weight and it was indicated that assembled subunits were able to store iron in vivo.

• The Korean Journal of Food And Nutrition
• /
• v.27 no.3
• /
• pp.406-413
• /
• 2014

The objective of this study was to identify the nutritional risk factors by blood analysis, in 1,083 preschool children of age 3 to 6 years. The frequency of anemic children was 7.3% with Hb<11.1 g/dL, 29.9% with ferritin<20 ng/mL, and 16.7% with transferrin Fe saturation(%)<15%. The prevalence of anemia in these children were 12.8% for those with MCV<79 fL, and it was 71% for those with TIBC> $400{\mu}g/dL$. Serum ferritin concentration was 20 ng/mL in the normal children. Thirty two percent of the children had anemia with Hb<12 g/dL, which is below the normal range of Hb. Exactly 15.4% of the children had serum Fe concentration of $60{\mu}g/dL$. The transferrin Fe saturation of the children (16.3%) was >15%. The serum ferritin concentration showed low correlations with Hb, Fe, transferrin Fe saturation, and MCV. The transferrin Fe saturation, higher Hb concentration, MCV, and Hct values were increased significantly. Consequently, iron-deficiency anaemia was thus defined as having Hb concentration <12 g/dL accompanied by ferritin concentration <20 ng/mL or Hct <33%.

• KSBB Journal
• /
• v.31 no.2
• /
• pp.105-112
• /
• 2016

Ferritin is known to regulate iron metabolism and maintain iron in a variety of the eukaryotic organisms. The region encoding the mature ferritin (0.47 kb, H-type) of Periserrula leucophryna was amplified using the designed primers including restriction enzyme site and termination codon and subcloned in frame to the pRBAS secretion vector containing the signal sequence, RBS, and promoter of amylase gene (E. coli-Bacillus shuttle vector), resulting in recombinant pRBAS-PLF vector. Recombinant ferritin (18 kDa) was correctly processed and secreted from Bacillus subtilis LKS strain harboring the pRBAS-PLF vector and quantitatively analyzed by SDS-PAGE and western blot, respectively. Secretion of the ferritin was optimized by culture conditions (host, medium, temperature, nitrogen source) in 3 L batch culture and 5 L jar fermenter. Finally. the ferritin was largely produced using 50 L fermenter as the following conditions; at $30^{\circ}C$, 150 rpm, 1 vvm in Bacillus subtilis LKS using PY medium. The secreted ferritin was maximally measured (approximately 177.6 ug/ml) when the cell density reached to 14.4 at $OD_{600}$ (20 h incubation). The iron binding activity was confirmed by Perls' staining in 7.5% non-denaturing gel, indicating that the multimeric ferritin (composed of 24 subunits) was formed in the culture broth after secretion. Biologically, the culture broth and powder type containing ferritin were tested for possibility as feed additive in chicken broiler. As a result, the ferritin stimulated the growth of chick broil and improved feed efficiency and production index.

• Korean Journal of Clinical Laboratory Science
• /
• v.51 no.2
• /
• pp.145-154
• /
• 2019

This study examined the relationship between the estimated glomerular filtration rate (eGFR) and urine microalbumin/creatinine ratio (uACR) with ferritin in Korean adults. This study included 4,948 adults aged ${\geq}20years$ from the 2012 Korea National Health and Nutrition Examination Survey (KNHANES) data. A covariance test adjusted for covariates was performed for the ferritin levels in relation to the decreased eGFR (eGFR<$60ml/min/1.73m^2$) and elevated uACR ($uACR{\geq}30mg/g$). Several key findings were made in the present study. First, after adjusting for the related variables, the ferritin level was higher in the decreased eGFR group [$103.04{\pm}6.59mL/min/1.73m^2$; 95% confidence interval (CI), 90.12~115.96] than in the normal eGFR group ($84.87{\pm}1.16mL/min/1.73m^2$; 95% CI, 82.59~87.14; P=0.007). Second, after adjusting for the related variables, the ferritin level ($M{\pm}SE$) was similar in the normal uACR group ($85.70{\pm}1.20mg/g$; 95% CI, 83.35~88.05) and elevated uACR group ($82.72{\pm}4.09mg/g$; 95% CI, 74.71~90.73) (P=0.487). Chronic kidney disease was positively associated with the ferritin level in Korean adults but albuminuria was not.

• Korean Journal of Human Ecology
• /
• v.4 no.1
• /
• pp.36-45
• /
• 2001

This study was performed to determine the changes of maternal iron status during pregnancy cross sectionally, and to evaluate the appropriateness of the cut-off points of hemoglobin (Hb). hematocrit (Hct), serum transferrin receptor (sTfR) and sTfR : ferritin ratio for assessing iron deficiency status based on serum ferritin level (< 12${\mu}g$/L). Serum Hb concentrations in the first trimester were significantly higher (p < 0.05) than those in the second and third trimester. Serum levels of iron and ferritin in the third trimester were significantly lower (p < 0.05) than those in the first and second trimester. On the other hand, sTfR:ferritin ratios in the third trimester were significantly higher (p < 0.05) than those in the first and second trimester. sTfR concentrations did not change significantly during pregnancy. The appropriate cut-off points of Hb were 11.5g/dL for whole period of pregnancy. 12.0g/dL for 1st trimester. and 11.5g/dL for both 2nd and 3rd trimester. The good cut-off points of Hct were 34% for whole period of pregnancy. 36% for 1st trimester. and 34% for both 2nd and 3rd trimester The suitable cut-off points of TIBC were 400${\mu}g$/dL for whole period of pregnancy. 360${\mu}g$/dL for 1st trimester, and 400${\mu}g$/dL for both 2nd and 3rd trimester. Any cut-off point of sTfR could not be selected because of its low sensitivity and specificity. The proper cut-off point of sTfR : ferritin ratio was 600 or 650 for all the periods determined except the first trimester. In conclusion, there were no reliable cut-off levels of sTfR and those of sTfR : ferritin ratio showed low specificity. The cut-off values of Hb and Hct for assessing iron deficiency were slightly higher than the values used to evaluate anemia. Thus, if appropriate cut-off levels were applied, Hb. Hct, or TIBC might be useful indices for evaluating iron deficiency as well as anemia.

• Journal of Microbiology and Biotechnology
• /
• v.15 no.2
• /
• pp.254-258
• /
• 2005

We have conducted in vitro reconstitution study of ferritin from its subunits FerH and FerL. For the reconstitution, FerH was produced from an expression vector construct in Escherichia coli and was purified from a heat treated cell extract by using one-step column chromatography. FerL was expressed as inclusion bodies. The denatured form of FerL was obtained by a simple washing step of the inclusion bodies with 3 M urea. The reconstitution experiment was conducted with various molar ratios of urea-denatured FerH and FerL to make the ferritin nanoparticle with a controlled composition of FerH and FerL. SDS-PAGE analysis of the reconstituted ferritins revealed that the reconstitution required the presence of more than 40 molar$\%$ of FerH in the reconstitution mixture. The assembly of the subunits into the ferritin nanoparticle was confmned by the presence of spherical particles with diameter of 10 nm by the atomic force microscopic image. Further analysis of the particles by using a transmission electron microscope revealed that the reconstituted particles exhibited different percentages of population with dense iron core. The reconstituted ferritin nanoparticles made with molar ratios of [FerH]/[FerL]=l00/0 and 60/40 showed that 80 to $90\%$ of the particles were apoferritin, devoid of iron core. On the contrary, all the particles formed with [FerH]/[FerL]=85/ 15 were found to contain the iron core. This suggests that although FerH can uptake iron, a minor portion of FerL, not exceeding $40\%$ at most, is required to deposit iron inside the particle.