Heterophilic Aggregation and Gelation of Plasma Proteins by Cell Adhesion Protein.
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- MIYAMOTO Keiichi
- Department of Chemistry for Materials, Faculty of Engineering, Mie University
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- TOKITA Masayuki
- Department of Chemistry for Materials, Faculty of Engineering, Mie University
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- KOMAI Takashi
- Department of Chemistry for Materials, Faculty of Engineering, Mie University
Bibliographic Information
- Other Title
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- 細胞接着タンパク質による血しょうタンパク質のヘテロ凝集とゲル化
Abstract
Cryogel is a coprecipitate of a cell adhesion protein with human plasma proteins produced from patient plasma. Cryogel is insoluble at a low temperature (4°C), and it is soluble at a high temperature (37°C). The diseases producing cryogel are rheumatoid arthritis, thrombosis, and so on. Cryogel is a physical gel formed by the heterophilic aggregation of EDA (+) fibronectin (EDA (+) FN), plasma fibronectin (pFN), fiburinogen (Fbg), and heparin (Hep). EDA (+) FN is a cell adhesion protein that does not exist in the blood, pFN and Fbg are plasma proteins, and Hep is a glucosaminoglycan. In this report, we describe the interaction of the cryogel composition molecules, and the condition of cryogel formation. The binding constant (KA) is measured by surface plasmon resonance (SPR). The order of strength for the interaction was Fbg-Hep>EDA (+) FN-Hep>Fbg-Fbg>Fbg-EDA (+) FN>Hep-pFN>Fbg-pFN. Hep-EDA (+) FN affinity is about 70 times bigger than that of Hep-pFN. It is thought that cryogel formation is controlled by the balance between aggregation size and aggregation concentration. So, the most suitable gelation condition was examined from the diffusion coefficient of the aggregate and the amount of aggregate by the dynamic light scattering measurement and the turbidity measurement. It was found that the cryogel grew around the self-aggregate of Fbg from the temperature dependence of diffusion coefficient. The diffusion coefficient ratio at a low temperature (5°C) became 1/1000 by adding Hep and EDA (+) FN into Fbg. On the other hand, the amount of aggregate by the three-element Fbg-Hep-pFN was much more than that of Fbg-Hep-EDA (+) FN. In other words, an important factor is the ratio of EDA (+) FN to pFN for the cryogel formation. Aggregation occurred most efficiently at EDA (+) FN: pFN: Fbg: Hep=0.05: 0.95: 15: 1 (mol%). Cryogelation is thus the Fbg-pFN aggregations of plasma proteins crosslinked by EDA (+) FN-Hep aggregates.
Journal
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- KOBUNSHI RONBUNSHU
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KOBUNSHI RONBUNSHU 55 (10), 603-612, 1998
The Society of Polymer Science, Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390282681499977984
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- NII Article ID
- 130004035276
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- ISSN
- 18815685
- 03862186
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- Text Lang
- ja
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed