• 대한임상검사과학회지
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• 제48권4호
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• pp.287-295
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• 2016

본 연구는 국가자료인 2010~2012년도 국민건강영양조사 자료를 이용하여 제 2형 당뇨병을 가진 대한민국 20세 이상 성인 16,096명(남성, 6,840명; 폐경 전 여성, 4,916명; 폐경 후 여성, 4,340명)을 대상으로 대사증후군(MetS) 및 대사증후군 위험요소의 증가(MSS)와 혈청 Ferritin수준의 관련성을 평가하고자 실시하였다. 대사증후군의 발생률은 16,096명 중 3,978명으로 24.7%(남성, 24.6%; 폐경 전 여성, 11.1%; 폐경 후 여성, 40.3%)이었다. 본 연구의 주요결과는 첫째, 관련변수를 보정한 후의 결과에서, 혈청 ferritin 수준은 비 대사증후군(남성, $111.08{\pm}1.01ng/mL$; 폐경 전 여성, $32.26{\pm}0.50ng/mL$; 폐경 후 여성, $63.26{\pm}0.98ng/mL$)에 비하여 대사증후군(남성, $132.25{\pm}1.98ng/mL$; 폐경전 여성, $39.89{\pm}1.49ng/mL$; 폐경 후 여성, $73.45{\pm}1.14ng/mL$)에서 유의하게 증가하였다(p<0.001). 둘째, 남성과 폐경 전 및 폐경 후 여성 모두에서, 혈청 ferritin 수준은 대사증후군 위험요소의 증가함에 따라 증가하였다(p<0.001). 결론적으로, 대한민국 성인에서 대사증후군 및 대사증후군 위험요소의 증가는 혈청 ferritin 수준을 증가시킨다.

• Biotechnology and Bioprocess Engineering:BBE
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• 제10권6호
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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.

• 한국식품영양과학회지
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• 제33권3호
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• pp.542-548
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• 2004

생체 내에 있어서 AsA 대사와 철 대사는 상호 밀접하게 연결되어 있다고 생각하여, 본 연구에서는 철단백질의 하나인 ferritin을 이용해서 AsA와의 상호작용의 유무를 조사하였다. Ferritin으로부터 철의 유리를 측정하기 위하여 ferrozine을 사용하여 AsA에 의한 ferritin으로부터 철의 유리를 흡광도 562 nm에서 Fe(ferrozine)$_3$$^{2+}$의 형태로 측정하는 방법을 사용하였다. 호기적 및 혐기적 조건 하에서 AsA에 의한 영향을 살펴 본 결과, ferritin으로부터 철의 유리에 대해서 AsA의 농도 및 시간의 증가에 의존하는 것을 알 수 있었다. 또한ferritin으로부터 철의 유리에 있어서 산소의 영향을 살펴본 결과, 가시부영역의 흡수 스펙트럼변화의 측정 결과에 의해 호기적 및 혐기적 조건 하 모두에서 ferritin으로부터 철의 유리를 확인하여 산소의 영향이 나타났고, 혐기적 조건하에서 보다 호기적 조건 하에서의 ferritin으로부터 철의 유리가 증가하는 것이 확인되었다. 즉, ferritin으로부터 철을 유리하는데 $O_2$$^{-}$ 가 관여할 가능성이 나타났다. 그러나, 본 연구 결과에서 반응시간 1시간 후의 호기적 및 혐기적 조건 하에서 562 nm에서의 흡광도를 살펴 본 결과 호기적 조건 하에서 유리된 철의 50% 이상이 AsA 자신에 의해, 나머지는 AsA와 산소분자와의 반응에 의해 생긴 $O_2$$^{-}$에 의한다고 생각되어졌다. 지금까지 ferritin으로부터 철의 유리는O$_2$$^{-}$에 의한 것이라는 보고가 많았지만, 이 결과에 의해 ferritin으로부터 철의 유리에 $O_2$$^{-}$가 관여하지만, 그것과 같은 정도 혹은 그 이상 AsA가 중요하다는 것이 밝혀졌다.

• BMB Reports
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• 제44권3호
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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 Microbiology and Biotechnology
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• 제17권10호
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• pp.1695-1699
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• 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.

• 한국식품영양학회지
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• 제27권3호
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• pp.406-413
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• 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
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• 제31권2호
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• pp.105-112
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• 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.

• 대한임상검사과학회지
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• 제51권2호
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• pp.145-154
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• 2019

본 연구는 대한민국 성인에서 eGFR 및 uACR과 Ferritin의 관련성에 대한 연구이다. 2012년 국민건강영양조사자료에서 20세 이상의 4,948명을 대상으로 관련변수를 보정한 후, 만성신장질환(CKD, eGFR<$60mL/min/1.73m^2$) 및 알부민뇨($uACR{\geq}30mg/g$)에 따른 페리틴 수준을 분석하였다. 만성신장질환군의 ferritin 수준($M{\pm}SE$) [$103.04{\pm}6.59mL/min/1.73m^2$; 95% confidence interval (CI), 90.12~115.96]은 정상군($84.87{\pm}1.16mL/min/1.73m^2$; 95% CI, 82.59~87.14)에 비하여 유의하게 높았다(P=0.007). 그러나 정상군($82.72{\pm}4.09mg/g$; 95% CI, 74.71~90.73)과 알부빈뇨군($82.72{\pm}4.09mg/g$; 95% CI, 74.71~90.73)의 ferritin 수준은 유의한 차이가 없었다(P=0.487). 결과적으로, 대한민국 성인에서 만성신장질환과 ferritin수준은 양의 상관관계가 있었지만, 알부빈뇨에서는 유의한 차이가 없었다.

• 한국가정과학회지
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• 제4권1호
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• pp.36-45
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• 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
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• 제15권2호
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• pp.254-258
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• 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.