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ABSTRACT: Background
Activated protein C (APC)-mediated inactivation of factor (F)Va is greatly enhanced by protein S. For inactivation to occur, a trimolecular complex among FVa, APC, and protein S must form on the phospholipid membrane. However, direct demonstration of complex formation has proven elusive.Objectives
To elucidate the nature of the phospholipid-dependent interactions among APC, protein S, and FVa.Methods
We evaluated binding of active site blocked APC to phospholipid-coated magnetic beads in the presence and absence of protein S and/or FVa. The importance of protein S and FV residues were evaluated functionally.Results
Activated protein C alone bound weakly to phospholipids. Protein S mildly enhanced APC binding to phospholipid surfaces, whereas FVa d
SUBMITTER: Gierula M
PROVIDER: S-EPMC6916587 | biostudies-literature | 2019 Dec
REPOSITORIES: biostudies-literature