A hydrophobic patch (PLVIVG; 1481-1486) in the B-domain of factor V-short is crucial for its synergistic TFPIα-cofactor activity with protein S and for the formation of the FXa-inhibitory complex comprising FV-short, TFPIα, and protein S.

ABSTRACT:

Background

Factor V-short (FV756-1458) is a natural splice variant functioning in synergy with protein S as tissue factor pathway inhibitor alpha (TFPIα)-cofactor in inhibition of factor Xa (FXa). An exposed acid region (AR2; 1493-1537) in the B domain binds TFPIα. The preAR2 (1458-1492) is crucial for the synergistic TFPIα-cofactor activity between FV-short and protein S and for assembly of a trimolecular FXa-inhibitory complex among FV-short, protein S, and TFPIα.

Objective

To identify which part of preAR2 is required for the synergistic TFPIα-cofactor activity between FV-short and protein S.

Methods

A FXa-inhibition assay was used to test the synergistic TFPIα cofactor activity between protein S and new FV-short variants FV709-1476, FV712-1478, FV712-1481, FV712-14

SUBMITTER: Dahlback B 

PROVIDER: S-EPMC9313797 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature