Hydrodynamics of cryogelation.
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 (R(h)) ratio (R(h)/R(h30)) of the cryogel component by dynamic light scattering in vitro. R(h)/R(h30) was normalized to R(h) at 30 degrees C (R(h30)) at several temperatures. The R(h)/R(h30) of Fbg was found to increase only by self-aggregation, whereas the R(h)/R(h30) of FNs does not increase in response to temperature changes. The R(h)/R(h30) of the Fbg/FN aggregate is increased by the addition of Hep, and the R(h)/R(h30) (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.
Miyamoto
K
K
Department of Chemistry for Materials, Faculty of Engineering, Mie University, 1515 Kamihama-Chou, Tsu, 514-8507, Mie, Japan. miyamoto@chem.mie-u.ac.jp
Shimonishi
Y
Y
Tokita
M
M
Komai
T
T
D001172:Arthritis, Rheumatoid / Q000097:blood*; D002448:Cell Adhesion; D002478:Cells, Cultured; D005340:Fibrinogen / Q000737:chemistry; D005353:Fibronectins / Q000737:chemistry; D006493:Heparin / Q000737:chemistry; D006801:Humans; D008027:Light; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D013696:Temperature
D005353:Fibronectins; D005340:Fibrinogen; D006493:Heparin