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Related Experiment Videos

Hydrodynamics of cryogelation.

K Miyamoto1, Y Shimonishi, M Tokita

  • 1Department of Chemistry for Materials, Faculty of Engineering, Mie University, 1515 Kamihama-Chou, Tsu, 514-8507, Mie, Japan. miyamoto@chem.mie-u.ac.jp

International Journal of Biological Macromolecules
|November 24, 2001
PubMed
Summary

Rheumatoid arthritis patients develop cryogelation due to plasma fibronectin (pFN) and fibrinogen (Fbg) aggregates. Heparin (Hep) addition significantly enhances EDA(+)FN/Fbg aggregate formation, suggesting key interactions in cryogelation.

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Area of Science:

  • Biochemistry
  • Rheumatology
  • Materials Science

Background:

  • Cryogelation, observed in rheumatoid arthritis (RA) patients, involves plasma fibronectin (pFN) and fibrinogen (Fbg) aggregates.
  • Extra domain A-containing fibronectin (EDA(+)FN) is unusually prevalent in RA plasma and contributes to cryogel formation.

Purpose of the Study:

  • To investigate the physical properties of cryogel components using hydrodynamic radius (R(h)) measurements.
  • To elucidate the roles of fibrinogen self-aggregation and EDA(+)FN interactions in heparin-induced cryogelation.

Main Methods:

  • Dynamic light scattering (DLS) was employed to measure the hydrodynamic radius (R(h)) of fibrinogen (Fbg) and fibronectin (FN) components.
  • R(h) values were normalized to R(h) at 30°C (R(h30)) and analyzed across various temperatures.

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  • The effect of heparin (Hep) on Fbg/FN aggregate formation was assessed.

    • Main Results:

    • Fibrinogen (Fbg) R(h)/R(h30) increased due to self-aggregation, while fibronectin (FN) R(h)/R(h30) remained stable with temperature.
    • Heparin (Hep) addition significantly increased the R(h)/R(h30) of Fbg/FN aggregates.
    • The R(h)/R(h30) of Hep-induced EDA(+)FN/Fbg aggregates (12.5) was substantially higher than that of pFN/Fbg aggregates (2.5).

    Conclusions:

    • Cryogelation in RA plasma is dependent on fibrinogen self-aggregation.
    • The interaction between EDA(+)FN and heparin (Hep) is crucial for the formation of robust cryogel structures.