Cryogelation in vitro

Keiichi Miyamoto, Masayuki Tokita, Takashi Komai, Keiichi Miyashita, Eiji Sakashita

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


Cryogel is a physical gel formed by the heterophilic aggregation of extra domain A containing fibronectin (EDA(+)FN), plasma fibronectin (pFN), fibrinogen (Fbg) and heparin (Hep). Cryogelation is controlled by the interactions between each aggregate and the amount of aggregates. Therefore, the present study attempted to elucidate these properties by studying turbidity (τ). Although only Fbg formed a self-aggregate under low temperatures, from the temperature dependence of τ, the amount of aggregate in three-element (pFN/Fbg/Hep) solution surpassed that of the EDA(+)FN/Fbg/Hep system. The optimal condition for cryogelation was afforded by a solution with Fbg/EDA(+)FN/pFN/Hep expressed in the molar ratio of 12:0.04:0.79:1. This cryogel structure in solution was probably formed via structural changes induced by pFN in Fbg. The structural change in Fbg was examined by circular dichroism under optimal conditions. This concept was based on observations of the direct transmission scanning electron microscopy of a cryogel. The EDA(+)FN/pFN/Fbg/Hep aggregates displayed a network structure that manifested particulate crosslinkage. Cryogelation, a phenomenon related to induction of rheumatoid arthritis in humans, was facilitated by both the EDA(+)FN-Hep interaction and the structural changes of Fbg induced by pFN.

Original languageEnglish
Pages (from-to)183-189
Number of pages7
JournalInternational Journal of Biological Macromolecules
Issue number2
Publication statusPublished - Jan 10 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Structural Biology
  • Biochemistry


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