TY - JOUR
T1 - Specific interactions between cryogel components
T2 - Role of extra domain A containing fibronectin in cryogelation
AU - Miyamoto, Keiichi
AU - Kodera, Nagisa
AU - Umekawa, Hayato
AU - Furuichi, Yukio
AU - Tokita, Masayuki
AU - Komai, Takashi
PY - 2002/6/18
Y1 - 2002/6/18
N2 - Cryogel is a physical gel formed by heterophilic aggregation of extra domain A containing fibronectin [EDA(+)FN], plasma fibronectin (pFN), fibrinogen (Fbg) and heparin (Hep), which are found in high concentrations in the blood of patients suffering from rheumatoid arthritis. In this study, we clarify the specific interactions between cryogel components in terms of the affinity constant (KA), obtained by surface plasmon resonance (SPR). It is found that Fbg self-interactions occur at lower temperatures, and that KA of Fbg-Hep changes with temperature. Specifically, KA (2.0×108 [M-1]) of Fbg-Hep at 5°C increases significantly from that (1.0×107 [M-1]) at 40°C. KA of EDA(+)FN-Hep increases with temperature, by approximately 100-fold between 40°C (KA=1012 [M-1]) and 20°C (KA=1010 [M-1]). Although KA of the FN fragments of Hep-binding domain containing an EDA region [EDA(+)HBD(+)] and Hep increases with temperatures above 30°C, KAs of HBD(+)-Hep and EDA(+)-Hep are not temperature-dependent. Therefore, EDA(+)HBD(+), formed as a special structure for high Hep affinity, exhibits temperature-dependent interaction with Hep. These results suggest that the main role of EDA(+)FN in cryogelation is to support the interaction with Hep.
AB - Cryogel is a physical gel formed by heterophilic aggregation of extra domain A containing fibronectin [EDA(+)FN], plasma fibronectin (pFN), fibrinogen (Fbg) and heparin (Hep), which are found in high concentrations in the blood of patients suffering from rheumatoid arthritis. In this study, we clarify the specific interactions between cryogel components in terms of the affinity constant (KA), obtained by surface plasmon resonance (SPR). It is found that Fbg self-interactions occur at lower temperatures, and that KA of Fbg-Hep changes with temperature. Specifically, KA (2.0×108 [M-1]) of Fbg-Hep at 5°C increases significantly from that (1.0×107 [M-1]) at 40°C. KA of EDA(+)FN-Hep increases with temperature, by approximately 100-fold between 40°C (KA=1012 [M-1]) and 20°C (KA=1010 [M-1]). Although KA of the FN fragments of Hep-binding domain containing an EDA region [EDA(+)HBD(+)] and Hep increases with temperatures above 30°C, KAs of HBD(+)-Hep and EDA(+)-Hep are not temperature-dependent. Therefore, EDA(+)HBD(+), formed as a special structure for high Hep affinity, exhibits temperature-dependent interaction with Hep. These results suggest that the main role of EDA(+)FN in cryogelation is to support the interaction with Hep.
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U2 - 10.1016/S0141-8130(02)00021-1
DO - 10.1016/S0141-8130(02)00021-1
M3 - Article
C2 - 12063123
AN - SCOPUS:0037129801
VL - 30
SP - 205
EP - 212
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
IS - 3-4
ER -