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Journal of magnetic resonance (San Diego, Calif. : 1997)2012; 217; 36-40; doi: 10.1016/j.jmr.2012.02.005

The role of diffusion in ferritin-induced relaxation enhancement of protons.

Abstract: The influence of proton diffusion on nuclear magnetic resonance (NMR) relaxation was investigated in the presence of horse spleen ferritin at 7 T. Binary mixtures of water and glycerol were used to control diffusion within the range of 0.6-2.0 × 10(-9)m(2)/s, which was confirmed by pulsed gradient techniques. The effect of chemical exchange by hydrolysis between water and glycerol on relaxation was characterized with Carr-Purcell-Meiboom-Gill (CPMG) dispersion experiments. The relaxation rate enhancement of the protons due to ferritin was found to be inversely proportional to the diffusion coefficient. The enhancement increased by a factor of 3.6 over the range of diffusion coefficients, while the hydroxyl proton concentration decreased by a factor of 1.3. This result is in disagreement with the proton exchange dephasing model, which is independent of diffusion but predicts an inverse dependence on the hydroxyl concentration. Our data indicate that the role of diffusion dominates and must be considered when relaxation rates are used to determine iron concentration in vivo.
Publication Date: 2012-02-22 PubMed ID: 22410189DOI: 10.1016/j.jmr.2012.02.005Google Scholar: Lookup
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Summary

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The researchers have found that in the presence of ferritin, a protein that stores iron in your body, the diffusion of protons has a critical role in nuclear magnetic resonance (NMR) relaxation, a phenomenon used in medical imaging techiques. Unexpectedly, they discovered the rate of relaxation enhancement due to ferritin increased with a drop on diffusion coefficient and a decrease in the hydroxyl proton concentration, which contradicts with the existing theoretical model.

Background of the Study

  • This publication is based on an investigation on the influence of proton diffusion on nuclear magnetic resonance (NMR) relaxation in the presence of horse spleen ferritin, particularly at 7 T.
  • The function of ferritin is to store iron in the body. The study investigates the interaction of this protein with protons, a fundamental particle found in the nucleus of all atoms, and its influence on NMR relaxation – a scientific technique applied in medical imaging like MRI scans.

Methodology of the Study

  • For this study, the researchers used binary mixtures of water and glycerol to control diffusion within a certain range, which was confirmed by pulsed gradient techniques.
  • A notable part of this study included the utilization of Carr-Purcell-Meiboom-Gill (CPMG) dispersion experiments to characterize the effect of chemical exchange by hydrolysis between water and glycerol on relaxation.

Research Findings

  • The researchers found that the relaxation rate enhancement of the protons due to ferritin was inversely proportional to the diffusion coefficient. That means as the diffusion coefficient decreases, the relaxation rate enhancement by ferritin goes up.
  • The data showed that the enhancement increased by a factor of 3.6 as the diffusion coefficients changed.
  • Simultaneously, there was a decrease in the hydroxyl proton concentration by a factor of 1.3. Hydroxyl proton refers to a hydrogen atom that is part of a water molecule.

Implications and Discrepancies

  • This result does not align with existing models, specifically the proton exchange dephasing model, which doesn’t assume any link between proton diffusion and NMR relaxation.
  • This model predicts inverse dependence on the concentration of hydroxyl, going against the research findings.

Conclusion

  • Given their findings, the authors suggest that the role of diffusion is dominant and cannot be ignored when relaxation rates are used to determine iron concentration in vivo – that is, within a living organism.
  • This might mean that existing models and assumptions in medical imaging may need to be revisited and revised to incorporate the impact of diffusion.

Cite This Article

APA
Boss MA, Chris Hammel P. (2012). The role of diffusion in ferritin-induced relaxation enhancement of protons. J Magn Reson, 217, 36-40. https://doi.org/10.1016/j.jmr.2012.02.005

Publication

ISSN: 1096-0856
NlmUniqueID: 9707935
Country: United States
Language: English
Volume: 217
Pages: 36-40

Researcher Affiliations

Boss, Michael A
  • Department of Physics, The Ohio State University, Columbus, OH 43210, USA. michael.boss@nist.gov
Chris Hammel, P

    MeSH Terms

    • Animals
    • Artifacts
    • Diffusion
    • Ferritins / analysis
    • Ferritins / chemistry
    • Horses
    • Magnetic Resonance Spectroscopy / methods
    • Protons
    • Spleen / chemistry

    Citations

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