Thromb Haemost 2001; 85(05): 830-836
DOI: 10.1055/s-0037-1615756
Review Article
Schattauer GmbH

Recombinant Tissue Factor Pathway Inhibitor Enhances the Binding of Factor Xa to Human Monocytes

Anguo Li
1   Cardiovascular Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA, Searle-Monsanto Co. St. Louis, MO, USA
,
Alvin C.K. Chang
1   Cardiovascular Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA, Searle-Monsanto Co. St. Louis, MO, USA
,
Glenn T. Peer
1   Cardiovascular Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA, Searle-Monsanto Co. St. Louis, MO, USA
,
Tze-Chen Wun
1   Cardiovascular Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA, Searle-Monsanto Co. St. Louis, MO, USA
,
Fletcher B. Taylor Jr.
1   Cardiovascular Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA, Searle-Monsanto Co. St. Louis, MO, USA
› Author Affiliations
Further Information

Publication History

Received 30 May 2000

Accepted after resubmission 08 January 2001

Publication Date:
11 December 2017 (online)

Summary

Tissue factor pathway inhibitor (TFPI) is a kunitz-type inhibitor of activated factor X (Xa). TFPI was reported to mediate Xa binding to a few of carcinoma cell lines. In this study it was observed that the Xa activity associated with human peripheral blood mononuclear cells (PBMC) incubated with Xa in the presence of recombinant TFPI (rTFPI) was much higher than with Xa alone. Xa activity on PBMC was also observed after whole blood was incubated with pre-formed Xa/TFPI complex. Further studies with flow cytometric analysis demonstrate that rTFPI enhances the binding of Xa to human monocytes. Western blot analysis showed that rTFPI was cleaved into a few of fragments after its incubation with monocytes either in the presence or absence of Xa. Based on these results and the observations reported by others, we speculate that Xa/TFPI complex may bind to human monocytes by a yet unidentified mechanism. The recovery of Xa activity from Xa/TFPI complex on PBMC may be related to the cleavage of rTFPI by Xa and/or monocyte proteases. This observation suggests a new mechanism by which monocytes become procoagulant in some pathological conditions in addition of the well known tissue factor expression on proinflammatic monocytes.

 
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