Characterization of interaction between blood coagulation factor VIII and LRP1 suggests dynamic binding by alternating complex contacts
Haarin Chun, James H. Kurasawa, Philip Olivares, Ekaterina S. Marakasova, Svetlana A. Shestopal, Gabriela U. Hassink, Elena Karnaukhova, Mary Migliorini, Juliet O. Obi, Ally K. Smith, Patrick L. Wintrode, Prasannavenkatesh Durai, Keunwan Park, Daniel Deredge, Dudley K. Strickland, Andrey G. Sarafanov
Journal of thrombosis and haemostasis
Deficiency in blood coagulation factor VIII (FVIII) results in life-threating bleeding (hemophilia A) treated by infusions of FVIII concentrates. To improve disease treatment, FVIII has been modified to increase its plasma half-life, which requires understanding mechanisms of FVIII catabolism. An important catabolic actor is hepatic low density lipoprotein receptor-related protein 1 (LRP1), which also regulates many other clinically significant processes. Previous studies showed complexity of FVIII site for binding LRP1.
FVIII, protein, LRP1