Studies on iron uptake and micelle formation in ferritin and apoferritin.
Abstract: Iron uptake and micelle formation in ferritin and apoferritin have been followed both spectrophotometrically and by means of sedimentation velocity experiments. Information was thus obtained on the molecular weight distribution of the reconstitution product. To achieve incorporation 'native' ferritin (whole ferritin as purified from horse spleen), 'native' apoferritin (apoferritin prepared by fractionation of ferritin preparations) and 'reduced' apoferritin (apoferritin prepared by reduction of ferritin by dithionite or ascorbic acid) have been incubated with ferrous salts in the presence of oxidizing agents under different experimental conditions. Although some iron is incorporated in 'native' ferritin, full saturation is not achieved and the molecular weight distribution of the incubated products remains heterogeneous. 'Native' and 'reduced' apoferritin show a similar iron incorporation, but the reconstitution products markedly differ in terms of their iron distribution. Ferritin reconstituted from 'native' apoferritin has a broad molecular weight distribution, while that reconstituted from 'reduced' apoferritin is characterized by a narrow, homogeneous molecular weight distribution. However treatment of apoferrition with reducing or oxidizing agents prior to the incubation alters the characteristics of the iron distribution without changing the iron incorporation properties. These results point to a role of the protein moiety not only in iron oxidation, but also in micelle formation.
Publication Date: 1976-10-30 PubMed ID: 1004497DOI: 10.1007/BF01732396Google Scholar: Lookup
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- Journal Article
Summary
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The research focused on the process of iron uptake and micelle formation in ferritin and apoferritin, proteins responsible for storing and releasing iron in the body. The study also explored how different experimental conditions affect the iron incorporation and distribution in these proteins.
Research Design and Methodology
- The researchers used spectrophotometry and sedimentation velocity experiments to study the processes of iron uptake and micelle formation in ferritin and apoferritin.
- They gathered information on the molecular weight distribution of the reconstitution product, which helped understand how the proteins behave under different experimental conditions.
- To study the incorporation of iron, ‘native’ ferritin, ‘native’ apoferritin, and ‘reduced’ apoferritin were observed. The ‘native’ versions were derived directly from horse spleen or by fractionation of ferritin preparations while the ‘reduced’ version was prepared by the reduction of ferritin using dithionite or ascorbic acid.
- This slew of proteins were then incubated with ferrous salts in the presence of oxidizing agents under varying experimental conditions.
Key Findings
- Despite some incorporation of iron, ‘native’ ferritin did not achieve full saturation and yielded a heterogeneous product in terms of molecular weight distribution.
- Interestingly, both ‘native’ and ‘reduced’ apoferritins showed comparable iron incorporation. However, there was a noticeable difference in the iron distribution of the reconstitution products between these two types.
- The ferritin reconstituted from ‘native’ apoferritin showed a broad molecular weight distribution, while ‘reduced’ apoferritin produced ferritin with a narrow, homogeneous molecular weight distribution.
- Modifying the apoferritin with reducing or oxidizing agents prior to the incubation changed the iron distribution characteristics, without altering the iron incorporation properties.
Conclusions and Implications
- The results of this research suggest that the protein moiety of ferritin and apoferritin plays a significant role not only in iron oxidation but also in micelle formation.
- The study also sheds light on how iron distribution and incorporation can be influenced through experimental conditions and could provide a foundation for further research into therapeutic interventions for disorders related to iron metabolism.
Cite This Article
APA
Stefanini S, Chiancone E, Vecchini P, Antonini E.
(1976).
Studies on iron uptake and micelle formation in ferritin and apoferritin.
Mol Cell Biochem, 13(1), 55-61.
https://doi.org/10.1007/BF01732396 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Apoferritins / metabolism
- Binding Sites
- Colloids
- Dithionite
- Ferricyanides
- Ferritins / analogs & derivatives
- Ferritins / metabolism
- Horses
- Iron / metabolism
- Kinetics
- Micelles
- Protein Binding
- Spleen
- Ultracentrifugation
References
This article includes 6 references
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- Bryce CF, Crichton RR. The catalytic activity of horse spleen apoferritin. Preliminary kinetic studies and the effect of chemical modification.. Biochem J 1973 Jun;133(2):301-9.
- Macara IG, Hoy TG, Harrison PM. The formation of ferritin from apoferritin. Kinetics and mechanism of iron uptake.. Biochem J 1972 Jan;126(1):151-62.
- Niederer W. Ferritin: iron incorporation and iron release.. Experientia 1970;26(2):218-20.
- LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent.. J Biol Chem 1951 Nov;193(1):265-75.
- Crichton RR. Studies on the structure of ferritin and apoferritin from horse spleen. I. Tryptic digestion of ferritin and apoferritin.. Biochim Biophys Acta 1969 Nov 11;194(1):34-42.
Citations
This article has been cited 5 times.- Wang Y, Zang J, Wang C, Zhang X, Zhao G. Structural Insights for the Stronger Ability of Shrimp Ferritin to Coordinate with Heavy Metal Ions as Compared to Human H-Chain Ferritin.. Int J Mol Sci 2021 Jul 23;22(15).
- Ghirlando R, Mutskova R, Schwartz C. Enrichment and characterization of ferritin for nanomaterial applications.. Nanotechnology 2016 Jan 29;27(4):045102.
- May CA, Grady JK, Laue TM, Poli M, Arosio P, Chasteen ND. The sedimentation properties of ferritins. New insights and analysis of methods of nanoparticle preparation.. Biochim Biophys Acta 2010 Aug;1800(8):858-70.
- Bellapadrona G, Stefanini S, Zamparelli C, Theil EC, Chiancone E. Iron translocation into and out of Listeria innocua Dps and size distribution of the protein-enclosed nanomineral are modulated by the electrostatic gradient at the 3-fold "ferritin-like" pores.. J Biol Chem 2009 Jul 10;284(28):19101-9.
- Calver GA, Kenny CP, Kushner DJ. Inhibition of the growth of Neisseria meningitidis by reduced ferritin and other iron-binding agents.. Infect Immun 1979 Sep;25(3):880-90.
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