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• W2014046827 abstract "Abstract Protein S is a cofactor for tissue factor pathway inhibitor (TFPI) that critically reduces the inhibition constant for FXa to below the plasma concentration of TFPI. TFPI Kunitz domain 3 is required for this enhancement to occur. To delineate the molecular mechanism underlying enhancement of TFPI function, in the present study, we produced a panel of Kunitz domain 3 variants of TFPI encompassing all 12 surface-exposed charged residues. Thrombin-generation assays in TFPI-depleted plasma identified a novel variant, TFPI E226Q, which exhibited minimal enhancement by protein S. This was confirmed in purified FXa inhibition assays in which no protein S enhancement of TFPI E226Q was detected. Surface plasmon resonance demonstrated concentration-dependent binding of protein S to wild-type TFPI, but almost no binding to TFPI E226Q. We conclude that the TFPI Kunitz domain 3 residue Glu226 is essential for TFPI enhancement by protein S." @default.
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• W2014046827 date "2012-12-13" @default.
• W2014046827 modified "2023-10-17" @default.
• W2014046827 title "Identification of functionally important residues in TFPI Kunitz domain 3 required for the enhancement of its activity by protein S" @default.
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• W2014046827 doi "https://doi.org/10.1182/blood-2012-05-432005" @default.
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