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Home / Equine Research Bank / Biochem J / Permeation of small molecules into the cavity of ferritin as...
The Biochemical journal1995; 307 ( Pt 1)(Pt 1); 253-256; doi: 10.1042/bj3070253

Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation.

Abstract: The NMR relaxation technique was used to investigate the permeation of molecules into the cavity of ferritin. Spin-lattice relaxation times in the rotating frame of various probe molecules were measured for solutions of recombinant horse L-apoferritin without iron and horse spleen apoferritin with very small amounts of ferric ions. The results show that molecules larger than the size of the ferritin channels can pass through the channels into the ferritin interior, and that the maximum size of molecules for the permeation is smaller than maltotriose.
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Publication Date: 1995-04-01 PubMed ID: 7717984PubMed Central: PMC1136770DOI: 10.1042/bj3070253Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research study uses nuclear magnetic resonance (NMR) relaxation methodology to uncover how small molecules can permeate the cavity of a protein, ferritin. It was discovered that despite their size, some molecules can pass through the ferritin channels, but the size limit for these molecules is smaller than maltotriose.

Methodology

  • The researchers used a technique called spin-lattice relaxation in the rotating frame. This is a type of NMR technique that measures how quickly the spins of protons return to equilibrium following a disturbance, a process known as relaxation.
  • They performed this measurement on various probe molecules in solutions of two types of apoferritin: one obtained from recombinant horse L-apoferritin without iron and the other from horse spleen apoferritin containing very small amounts of ferric ions. Apoferritin is a protein that stores iron in a non-toxic form and releases it in a controlled manner.

Findings

  • The results shed light on how molecules larger than the size of ferritin channels manage to enter the cavity or interior of ferritin.
  • They found that the maximum size of the molecules that can permeate the ferritin structure is smaller than that of maltotriose. Maltotriose is a trisaccharide, a carbohydrate composed of three sugar units.

Significance

  • The research provides important insights into the behaviour and characteristics of the ferritin protein. This information can potentially enhance our understanding of iron storage and metabolism inside cells.
  • The findings also have implications for more targeted drug delivery methods where small molecule drugs can be specifically designed to permeate the cavities of proteins like ferritin.

Cite This Article

APA
Yang D, Nagayama K. (1995). Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation. Biochem J, 307 ( Pt 1)(Pt 1), 253-256. https://doi.org/10.1042/bj3070253

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 307 ( Pt 1)
Issue: Pt 1
Pages: 253-256

Researcher Affiliations

Yang, D
  • Nagayama Protein Array Project, ERATO, JRDC, Tsukuba Research Consortium, Japan.
Nagayama, K

    MeSH Terms

    • Animals
    • Apoferritins / chemistry
    • Carbohydrate Sequence
    • Dimethyl Sulfoxide / metabolism
    • Ferritins / chemistry
    • Glucose / metabolism
    • Horses
    • Iron / metabolism
    • Magnetic Resonance Spectroscopy
    • Maltose / analogs & derivatives
    • Maltose / metabolism
    • Molecular Sequence Data
    • Molecular Weight
    • Oligosaccharides / metabolism
    • Polyethylene Glycols / metabolism
    • Protein Conformation
    • Recombinant Proteins / chemistry
    • Spleen / chemistry
    • Trisaccharides / metabolism
    • Water / metabolism

    References

    This article includes 14 references
    1. Harrison PM, Hoy TG, Macara IG, Hoare RJ. Ferritin iron uptake and release. Structure-function relationships.. Biochem J 1974 Nov;143(2):445-51.
      pubmed: 4477953doi: 10.1042/bj1430445google scholar: lookup
    2. Jones T, Spencer R, Walsh C. Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues.. Biochemistry 1978 Sep 19;17(19):4011-7.
      pubmed: 708692doi: 10.1021/bi00612a021google scholar: lookup
    3. Ford GC, Harrison PM, Rice DW, Smith JM, Treffry A, White JL, Yariv J. Ferritin: design and formation of an iron-storage molecule.. Philos Trans R Soc Lond B Biol Sci 1984 Feb 13;304(1121):551-65.
      pubmed: 6142491doi: 10.1098/rstb.1984.0046google scholar: lookup
    4. Yang CY, Meagher A, Huynh BH, Sayers DE, Theil EC. Iron(III) clusters bound to horse spleen apoferritin: an X-ray absorption and Mössbauer spectroscopy study that shows that iron nuclei can form on the protein.. Biochemistry 1987 Jan 27;26(2):497-503.
      pubmed: 3828319doi: 10.1021/bi00376a023google scholar: lookup
    5. Theil EC. Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms.. Annu Rev Biochem 1987;56:289-315.
      pubmed: 3304136doi: 10.1146/annurev.bi.56.070187.001445google scholar: lookup
    6. Gillis P, Koenig SH. Transverse relaxation of solvent protons induced by magnetized spheres: application to ferritin, erythrocytes, and magnetite.. Magn Reson Med 1987 Oct;5(4):323-45.
      pubmed: 2824967doi: 10.1002/mrm.1910050404google scholar: lookup
    7. BOTHWELL TH, MALLETT B. The determination of iron in plasma or serum.. Biochem J 1955 Apr;59(4):599-602.
      pubmed: 14363152doi: 10.1042/bj0590599google scholar: lookup
    8. Stefanini S, Desideri A, Vecchini P, Drakenberg T, Chiancone E. Identification of the iron entry channels in apoferritin. Chemical modification and spectroscopic studies.. Biochemistry 1989 Jan 10;28(1):378-82.
      pubmed: 2539862doi: 10.1021/bi00427a052google scholar: lookup
    9. Brady MC, Lilley KS, Treffry A, Harrison PM, Hider RC, Taylor PD. Release of iron from ferritin molecules and their iron-cores by 3-hydroxypyridinone chelators in vitro.. J Inorg Biochem 1989 Jan;35(1):9-22.
      pubmed: 2709002doi: 10.1016/0162-0134(89)84002-4google scholar: lookup
    10. Jacobs DL, Watt GD, Frankel RB, Papaefthymiou GC. Redox reactions associated with iron release from mammalian ferritin.. Biochemistry 1989 Feb 21;28(4):1650-5.
      pubmed: 2541760doi: 10.1021/bi00430a033google scholar: lookup
    11. Andrews SC, Arosio P, Bottke W, Briat JF, von Darl M, Harrison PM, Laulhère JP, Levi S, Lobreaux S, Yewdall SJ. Structure, function, and evolution of ferritins.. J Inorg Biochem 1992 Aug 15-Sep;47(3-4):161-74.
      pubmed: 1431878doi: 10.1016/0162-0134(92)84062-rgoogle scholar: lookup
    12. Yang D, Matsubara K, Yamaki M, Ebina S, Nagayama K. Heterogeneities in ferritin dimers as characterized by gel filtration, nuclear magnetic resonance, electrophoresis, transmission electron microscopy, and gene engineering techniques.. Biochim Biophys Acta 1994 Jun 12;1206(2):173-9.
      pubmed: 8003522doi: 10.1016/0167-4838(94)90205-4google scholar: lookup
    13. LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent.. J Biol Chem 1951 Nov;193(1):265-75.
      pubmed: 14907713
    14. Watt GD, Jacobs D, Frankel RB. Redox reactivity of bacterial and mammalian ferritin: is reductant entry into the ferritin interior a necessary step for iron release?. Proc Natl Acad Sci U S A 1988 Oct;85(20):7457-61.
      pubmed: 2845407doi: 10.1073/pnas.85.20.7457google scholar: lookup

    Citations

    This article has been cited 7 times.
    1. Muhoberac BB, Vidal R. Iron, Ferritin, Hereditary Ferritinopathy, and Neurodegeneration.. Front Neurosci 2019;13:1195.
      doi: 10.3389/fnins.2019.01195pubmed: 31920471google scholar: lookup
    2. Zhen Z, Tang W, Todd T, Xie J. Ferritins as nanoplatforms for imaging and drug delivery.. Expert Opin Drug Deliv 2014 Dec;11(12):1913-22.
      doi: 10.1517/17425247.2014.941354pubmed: 25070839google scholar: lookup
    3. Huard DJ, Kane KM, Tezcan FA. Re-engineering protein interfaces yields copper-inducible ferritin cage assembly.. Nat Chem Biol 2013 Mar;9(3):169-76.
      doi: 10.1038/nchembio.1163pubmed: 23340339google scholar: lookup
    4. Barnés CM, Theil EC, Raymond KN. Iron uptake in ferritin is blocked by binding of [Cr(TREN)(H(2)O)(OH)](2+), a slow dissociating model for [Fe(H(2)O)(6)](2+).. Proc Natl Acad Sci U S A 2002 Apr 16;99(8):5195-200.
      doi: 10.1073/pnas.032089399pubmed: 11959967google scholar: lookup
    5. Yang X, Arosio P, Chasteen ND. Molecular diffusion into ferritin: pathways, temperature dependence, incubation time, and concentration effects.. Biophys J 2000 Apr;78(4):2049-59.
      doi: 10.1016/S0006-3495(00)76752-Xpubmed: 10733983google scholar: lookup
    6. Yang X, Chasteen ND. Molecular diffusion into horse spleen ferritin: a nitroxide radical spin probe study.. Biophys J 1996 Sep;71(3):1587-95.
      doi: 10.1016/S0006-3495(96)79361-Xpubmed: 8874032google scholar: lookup
    7. Levi S, Santambrogio P, Corsi B, Cozzi A, Arosio P. Evidence that residues exposed on the three-fold channels have active roles in the mechanism of ferritin iron incorporation.. Biochem J 1996 Jul 15;317 ( Pt 2)(Pt 2):467-73.
      doi: 10.1042/bj3170467pubmed: 8713073google scholar: lookup
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