C-terminal residues of activated protein C light chain contribute to its anticoagulant and cytoprotective activities.

ABSTRACT:

Background

Activated protein C (APC) is an important homeostatic blood coagulation protease that conveys anticoagulant and cytoprotective activities. Proteolytic inactivation of factors Va and VIIIa facilitated by cofactor protein S is responsible for APC's anticoagulant effects, whereas cytoprotective effects of APC involve primarily the endothelial protein C receptor (EPCR), protease activated receptor (PAR)1 and PAR3.

Objective

To date, several binding exosites in the protease domain of APC have been identified that contribute to APC's interaction with its substrates but potential contributions of the C-terminus of the light chain have not been studied in detail.

Methods

Site-directed Ala-scanning mutagenesis of six positively charged residues within G142-L155 was

SUBMITTER: Yamashita A 

PROVIDER: S-EPMC7380734 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature