Abstract:
:Tissue factor pathway inhibitor (TFPI) inhibits the activity of coagulation factors VIIa and Xa through Kunitz domains, thereby inhibiting the activity of tissue factor. However, it has been shown that the C-terminal of this inhibitor is essential for the maximal anticoagulant activity of TFPI. We have investigated the endogenous ability of the C-terminal of TFPI to influence coagulation. A synthetic peptide corresponding to residues 254-265 within the C-terminal of TFPI was prepared and shown to be capable of inhibiting tissue factor pathway by preventing the activation of factor VII. Mutational analysis of the peptide revealed the identity of the key lysine residues.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ettelaie C,Adam JM,James NJ,Oke AO,Harrison JA,Bunce TD,Bruckdorfer KRdoi
10.1016/s0014-5793(99)01663-4keywords:
subject
Has Abstractpub_date
1999-12-17 00:00:00pages
341-4issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01663-4journal_volume
463pub_type
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