Key result
Sequential deletions of the C-terminus of tissue factor pathway inhibitor decreased its inhibitory activity against factor Xa and its affinity for heparin.
Population
In vitro biochemical assays using human factor Xa and bovine gamma-carboxyglutamate (Gla)-domainless factor Xa
Comparison
Altered forms of recombinant tissue factor… vs Full-length rTFPI and varying assay conditions
Design
Preclinical
Authors
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Preclinical TFPI data should not change clinical anticoagulation; extends structure-function insights but requires human validation.
The C-terminal polypeptide of TFPI, including part of the third Kunitz-type domain, is essential for heparin binding and optimal factor Xa inhibition in the presence of calcium and phospholipids.
Wesselschmidt et al. (1993) studied this question. Altered forms of recombinant TFPI (rTFPI) vs. Full-length rTFPI was evaluated on Factor Xa inhibition and heparin binding. Sequential deletions of the C-terminus of tissue factor pathway inhibitor decreased its inhibitory activity against factor Xa and its affinity for heparin.
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