Cryogel, prevalent in the plasma of rheumatoid arthritis patients, is a plasma fibronectin (pFN)-extra domain A containing FN [EDA(+)FN]-fibrinogen (Fbg) aggregate formed by the addition of heparin (Hep) at low temperature. Although EDA(+)FN is not usually present in normal plasma, its prevalence in rheumatic patients induces cryogelation. In this study, we determined the hydrodynamic radius (Rh) ratio (Rh/Rh30) of the cryogel component by dynamic light scattering in vitro. Rh/Rh30 was normalized to Rh at 30 °C (Rh30) at several temperatures. The Rh/Rh30 of Fbg was found to increase only by self-aggregation, whereas the Rh/Rh30 of FNs does not increase in response to temperature changes. The Rh/Rh30 of the Fbg/FN aggregate is increased by the addition of Hep, and the Rh/Rh30 (12.5) of the Hep-induced EDA(+)FN/Fbg aggregate is greater than that (2.5) of the pFN/Fbg aggregate. These results suggest that cryogelation requires Fbg self-aggregation and the interaction between EDA(+)FN and Hep.
|Number of pages||5|
|Journal||International Journal of Biological Macromolecules|
|Publication status||Published - Dec 10 2001|
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Economics and Econometrics