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Thromb Haemost 2002; 87(01): 80-85
DOI: 10.1055/s-0037-1612947
DOI: 10.1055/s-0037-1612947
Review Article
Oxidized Low-density Lipoprotein Associates Strongly with Carboxy-terminal Domain of Tissue Factor Pathway Inhibitor and Reduces the Catalytic Activity of the Protein
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Further Information
Publication History
Received
13 June 2001
Accepted after revision
14 August 2001
Publication Date:
13 December 2017 (online)
Summary
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 lowdensity 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.
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