Impact of mutations in the von Willebrand factor A2
domain on ADAMTS13-dependent proteolysis
by Wolf Achim Hassenpflug, Ulrich Budde, Tobias Obser, Dorothea Angerhaus, Elke
Drewke, Sonja Schneppenheim, and Reinhard Schneppenheim
Blood
Volume 107(6):2339-2345
March 15, 2006
©2006 by American Society of Hematology
Distribution of VWD type 2A mutations.
Wolf Achim Hassenpflug et al. Blood 2006;107:2339-2345
©2006 by American Society of Hematology
Outline of the pIRES neo 2 A1-A2-A3 WT construct.
Wolf Achim Hassenpflug et al. Blood 2006;107:2339-2345
©2006 by American Society of Hematology
Typical VWF multimer patterns in classical VWD type 2A.
Wolf Achim Hassenpflug et al. Blood 2006;107:2339-2345
©2006 by American Society of Hematology
ADAMTS13 assay using wild-type full-length von Willebrand factor (VWF).
Wolf Achim Hassenpflug et al. Blood 2006;107:2339-2345
©2006 by American Society of Hematology
ADAMTS13 assay using mutant full-length VWF. rhuVWF-WT and mutant VWF were digested by
ADAMTS13 and subject to multimer analysis.
Wolf Achim Hassenpflug et al. Blood 2006;107:2339-2345
©2006 by American Society of Hematology
Digestion of the A1-A2-A3 domain fragments of VWF (rhuVWFA1-A2-A3) by rhuADAMTS13.
Wolf Achim Hassenpflug et al. Blood 2006;107:2339-2345
©2006 by American Society of Hematology
Quantitative analysis of ADAMTS13-mediated proteolysis of representative mutant and WT
VWFA1-A2-A3 fragments.
Wolf Achim Hassenpflug et al. Blood 2006;107:2339-2345
©2006 by American Society of Hematology