論文

査読有り
2002年1月

Oxidized low-density lipoprotein associates strongly with carboxy-terminal domain of tissue factor pathway inhibitor and reduces the catalytic activity of the protein

THROMBOSIS AND HAEMOSTASIS
  • S Horie
  • ,
  • S Hiraishi
  • ,
  • T Hamuro
  • ,
  • Y Kamikubo
  • ,
  • J Matsuda

87
1
開始ページ
80
終了ページ
85
記述言語
英語
掲載種別
研究論文(学術雑誌)
出版者・発行元
SCHATTAUER GMBH-VERLAG MEDIZIN NATURWISSENSCHAFTEN

Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor of the extrinsic blood coagulation pathway. Previously we have shown that 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 TRI.


リンク情報
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000173512500015&DestApp=WOS_CPL
ID情報
  • ISSN : 0340-6245
  • Web of Science ID : WOS:000173512500015

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