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The role of the C‐terminal domain in the inhibitory functions of tissue factor pathway inhibitor
Author(s) -
Ettelaie Camille,
Adam Jacqueline M,
James Nicola J,
Oke Adedayo O,
Harrison Jillian A,
Bunce Tim D,
Bruckdorfer K.Richard
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01663-4
Subject(s) - tissue factor pathway inhibitor , tissue factor , coagulation , peptide , chemistry , endogeny , factor vii , lysine , c terminus , biochemistry , protein c , microbiology and biotechnology , biology , amino acid , medicine
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.