Human Factor VIII Structure & Function
Technician Amy Griffiths working in the Fay Lab
Factor VIII serves as a protein cofactor for the serine protease, factor IXa in the membrane-dependent conversion of factor X to factor Xa during the blood coagulation cascade reactions. Deficiency or defects in factor VIII result in hemophilia A, the most common of the severe, inherited bleeding disorders. Ongoing studies in our laboratory include physical and biochemical analyses of factor VIII structure, inter-subunit interactions, and intermolecular interactions with other components of the clotting cascade. Overall, our research program is aimed at gaining fundamental insights into the structure, activity and regulation of a protein central to hemostasis. This information will have specific implications for understanding hemophilia A and developing superior therapeutics for its treatment.
Recent Publications
- (2012 May 04). Sequences Flanking Arg336 in Factor VIIIa Modulate Factor Xa-catalyzed Cleavage Rates at this Site and Cofactor Function. J Biol Chem. 287, 15409-17.
- (2012 Apr 10). P3-P3' Residues Flanking Scissile Bonds in Factor VIII Modulate Rates of Substrate Cleavage and Procofactor Activation by Thrombin. Biochemistry. In press.
- (2012 Mar 01). Enhancing factor VIII and VIIIa stability by combining mutations at the A2 domain interface and A1-C2 domain interface. J Thromb Haemost. 10, 492-5.





