Publications by authors named "Tahar Kaabache"
Introduction: Protein S (PS) is a vitamin K-dependent plasma glycoprotein with a key role in the control of coagulation pathway on phospholipid membranes. We compared anticoagulant and membrane binding properties of PS altered by natural mutations (N217S, DelI203D204) affecting the epidermal growth factor like-domain 4 (EGF4) and causing PS deficiency.
Materials And Methods: Binding of recombinant, immunopurified PS (rPS) to several conformation-specific antibodies, to C4BP and to phospholipid liposomes was investigated by ELISA.
Article Synopsis
- Researchers created two chimeric proteins combining parts of human protein S and prothrombin to study their functions, specifically focusing on the gamma-carboxyglutamic acid (Gla) domain.
- Neither chimera showed activated protein C (APC) cofactor activity, indicating the importance of the protein S Gla domain for this function, but both were good at binding to phospholipids.
- Computational analysis revealed key structural features in the Gla domain relevant for APC interaction and phospholipid binding, with specific residues identified as crucial for these functions through experiments with modified versions of protein S.