Influence of site-directed modifications on the formation of iron cores in ferritin

Wade, Vanessa J.

doi:10.1016/0022-2836(91)80137-j

Cited by 44 publications

(75 citation statements)

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“…The total amount of intracellular iron content was ranked sequentially in transformants as follows: H-ferritin > HL-ferritin > LH-ferrtitin > L-ferritin transformants. These results are due to the ferroxidase site of human H-ferritin as previously reported (Levi et al, 1988(Levi et al, , 1989(Levi et al, , 1996Wade et al, 1991). It is suggested that recombinant human H-ferritin has a major role in iron accumulation and oxidation.…”

Section: Iron-uptake Capacity Of the Recombinant Human H- L- And Cosupporting

confidence: 68%

“…The H-ferritin catalyzes a fast iron oxidation from Fe (II) to Fe (III) in the inner portion of the subunit fold (Levi et al, 1988(Levi et al, , 1989(Levi et al, , 1996Wade et al, 1991). The L-ferritin has a higher efficiency in accumulating iron mineralization within the cavity and is more stable to physical denaturation than H-ferritin (Wade et al, 1991;Levi et al, 1994). In vivo, two main subunit types are found in various assembled molecules.…”

Section: Introductionmentioning

confidence: 97%

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Expression and Iron Storage Properties of Recombinant Human Ferritins inEscherichia Coli:Relevance for Functional Ferritins in Food Systems

Lee

Kim

2008

Food Biotechnology

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Ferritin is an iron storage protein found in most living organisms. Human heavy chain (H-) and light chain (L-) ferritin were amplified from human heart cDNA library. Each ferritin gene was inserted down stream of the T7 promoter of bacterial expression, and finally four types of H-, L-, and co-expression vectors were constructed. Recombinant human ferritins were overexpressed and identified with SDS-PAGE and western blotting. The expression levels of recombinant ferritin proteins ranged about 29-36% of whole cell total protein. From atomic absorption spectrometry (AAS) analysis, the rate of iron uptake for H-ferritin was significantly faster than that for the HL-, LH-, and L-ferritin, respectively. From AAS analysis, the levels of iron content in cells progressively increased in transformants with 0-30 mM ferric citrate in the media. Among these ferritin transformants, the highest amount of cellular iron was observed with H-ferritin transformant. The total amounts of iron content in E. coli could be sequentially ranked as H-ferritin > HL-ferritin > LH-ferritin > L-ferritin > negative transformants. Expressed recombinant human ferritins indicated that their assembled subunits were able to store iron in the cells. The results of this study further enhances our understanding of iron uptake properties in vivo and suggest similar strategies for using food-grade ferritins for functional foods or iron-fortified food ingredients.

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Section: Iron-uptake Capacity Of the Recombinant Human H- L- And Cosupporting

confidence: 68%

Section: Introductionmentioning

confidence: 97%

Expression and Iron Storage Properties of Recombinant Human Ferritins inEscherichia Coli:Relevance for Functional Ferritins in Food Systems

Lee

Kim

2008

Food Biotechnology

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“…The nucleation site on the inner surface of many Ftn shells provides a binding site that can coordinate iron ions [14]. The arrangement of the surface-charged residues leaves some coordination spheres around the iron that allow the growth of the mineral phase ( Figure 6.4e).…”

Section: The Nucleation Sitementioning

confidence: 99%

Ferritin Iron Mineralization and Storage: From Structure to Function

2016

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“…It seems plausible that once the mineral is formed in the core, it acts as a seed for nucleation, which leads to the autocatalysis of the mineral formation. Although there have been several reports on comparative experiments conducted to investigate mineral formation in the ferritin core, to the best of our knowledge the present study is the first to analyze the core minerals formed by H-ferritins produced from different hosts [27,28]. These finding are also of particular interest to material scientists producing nanoparticles with specific characteristics such as size and size-homogeneity.…”

Section: Reconstitution Of H-ferritinsmentioning

confidence: 77%

Purification and biochemical characterization of recombinant human H-ferritins from Saccharomyces cerevisiae

Seo

Kim

2011

Biotechnol Bioproc E

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Recombinant human H-ferritins produced from Saccharomyces cerevisiae were purified and their molecular properties were characterized. Electrophoresis of the recombinant H-ferritins showed revealed bands with mobilities similar to those of the H-ferritins produced by Escherichia coli. The pI of H-ferritins from yeast was more basic than that of H-ferritins produced by E. coli. When the cells were treated with tunicamycin, the pI of H-ferritins was driven to a sharp band with the pI range similar to that of those produced by E. coli, implying that the H-ferritins from yeast are glycosylated. The iron uptake of H-ferritins was rapid in the initial stage, with a slight reduction when compared to ferritins from E. coli. Recombinant ferritins are commonly used during synthesis of inorganic nanoparticles in their cores for chemical and industrial purposes. Transmission electron microscopy revealed that the reconstitution yield and size distribution of the core minerals were affected depending on the protein shells. The Hferritins with higher reconstitution yields (64.4%) showed slightly larger sizes (mean 6.52 nm) with narrower size distribution.

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Influence of site-directed modifications on the formation of iron cores in ferritin

Cited by 44 publications

References 0 publications

Expression and Iron Storage Properties of Recombinant Human Ferritins inEscherichia Coli:Relevance for Functional Ferritins in Food Systems

Expression and Iron Storage Properties of Recombinant Human Ferritins inEscherichia Coli:Relevance for Functional Ferritins in Food Systems

Ferritin Iron Mineralization and Storage: From Structure to Function

Purification and biochemical characterization of recombinant human H-ferritins from Saccharomyces cerevisiae

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