scholarly journals Expression and characterization of Kunitz domain 3 and C-terminal of human tissue factor pathway inhibitor-2

2009 ◽  
Vol 41 (11) ◽  
pp. 948-954 ◽  
Author(s):  
L. Zhu ◽  
J. Wang ◽  
J. Mu ◽  
H. Wang ◽  
C. Zhang ◽  
...  
Biochemistry ◽  
2002 ◽  
Vol 41 (1) ◽  
pp. 78-85 ◽  
Author(s):  
Shouhei Mine ◽  
Toshio Yamazaki ◽  
Toshiyuki Miyata ◽  
Saburo Hara ◽  
Hisao Kato

1997 ◽  
Vol 269 (3) ◽  
pp. 395-407 ◽  
Author(s):  
Maurits J.M Burgering ◽  
Leon P.M Orbons ◽  
Antoon van der Doelen ◽  
John Mulders ◽  
Henri J.M Theunissen ◽  
...  

1993 ◽  
Vol 268 (18) ◽  
pp. 13344-13351
Author(s):  
J.G. Petersen ◽  
G. Meyn ◽  
J.S. Rasmussen ◽  
J. Petersen ◽  
S.E. Bjørn ◽  
...  

2010 ◽  
Vol 286 (6) ◽  
pp. 4329-4340 ◽  
Author(s):  
Madhu S. Bajaj ◽  
Godwin I. Ogueli ◽  
Yogesh Kumar ◽  
Kanagasabai Vadivel ◽  
Gregory Lawson ◽  
...  

1996 ◽  
Vol 75 (05) ◽  
pp. 796-800 ◽  
Author(s):  
Sanne Valentin ◽  
Inger Schousboe

SummaryIn the present study, the interaction between tissue factor pathway inhibitor (TFPI) and phospholipids has been characterized using a microtitre plate assay. TFPI was shown to bind calcium-independently to an acidic phospholipid surface composed of phosphatidylserine, but not a surface composed of the neutral phosphatidylcholine. The interaction was demonstrated to be dependent on the presence of the TFPI C-terminus. The presence of heparin (1 U/ml, unfractionated) was able to significantly reduce the binding of TFPI to phospholipid. The interaction of TFPI with phosphatidylserine was significantly decreased in the presence of calcium, but this was counteracted, and even enhanced, following complex formation of TFPI with factor Xa prior to incubation with the phospholipid surface. Moreover, a TFPI variant, not containing the third Kunitz domain and the C-terminus, was unable to bind to phospholipid. However, following the formation of a TFPI/factor Xa-complex this TFPI variant was capable of interacting with the phospholipid surface. This indicates that the role of factor Xa as a TFPI cofactor, at least in part, is to mediate the binding of TFPI to the phospholipid surface.


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