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女子栄養大学 教員紹介 |
ヒライシ サユリ
Sayuri Hiraishi 平石 さゆり 所属 栄養科学研究所 職種 専任講師 |
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言語種別 | 英語 |
発行・発表の年月 | 2002 |
形態種別 | 学位論文(博士) |
査読 | 査読あり |
標題 | Oxidized low-density lipoprotein associates strongly with carboxy-terminal domain of tissue factor pathway inhibitor and reduces the catalytic activity of the protein. |
執筆形態 | 共著 |
掲載誌名 | Thromb. Haemost. |
巻・号・頁 | 87,pp.80-85 |
総ページ数 | null |
著者・共著者 | Horie S, Hiraishi S, Hamuro T, Kamikubo Y, Matsuda J |
概要 | Previously we have shown that tissue factor pathway inhibitor (TFPI) associates quite rapidly with oxidized low-density lipoprotein (ox-LDL), with a reduction of the inhibitory activity on factor X activation. In the present study, it was found, by means of agarose gel electrophoresis, that the pre-incubation of full-length rTFPI with heparin or the carboxy (C)-terminal part (peptide 240-265) of TFPI prevented the association with ox-LDL in a dose-dependent manner. When rTFPI lacking the C-terminal basic part of the molecule (rTFPI-C) was mixed with ox-LDL, only a small amount of rTFPI-C was shifted to the position of ox-LDL on electrophoresis. Further, ox-LDL did not reduce the activity of rTFPI-C. These results indicate that the C-terminal domain of TFPI molecule plays a predominant role in the binding to ox-LDL and the binding through the C-terminal part is essential for the ox-LDL-dependent reduction of the anticoagulant activity of TFPI. |