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J. Evan Sadler talks with and answers a few questions about this month's Fast Moving Front in the field of Clinical Medicine. The author has also sent along images of their work.
J. Evan Sadler Article: Update on the pathophysiology and classification of von Willebrand disease: a report of the Subcommittee on von Willebrand Factor
Authors: Sadler, JE, et. al
J THROMB HAEMOST, 4 (10): 2103-2114 OCT 2006

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Figures and descriptions:

Figure 1:  
Figure 1:  Biosynthesis of VWF. The VWF precursor is translocated into the ER, where the signal peptide (SP) is cleaved and disulfide bonds form between C-terminal domains to yield proVWF dimers. In the Golgi, disulfide bonds form between N-terminal domains to yield multimers, and the propeptide is cleaved. Multimers are secreted or packaged into Weibel-Palade bodies for later secretion. 

Figure 2:
Figure 2: Classification of VWD.

Figure 3:
Figure 3: Mutations in VWD type 2. The VWF precursor consists of a signal peptide (residues 1-22), propeptide (residues 23-763), and mature subunit residues 764-2813. Structural motifs are labeled. Locations are indicated for intersubunit disulfide bonds (S-S); binding sites for factor VIII, platelet GPIb, fibrillar collagen, platelet integrin aIIbß3; and the site cleaved by the metalloprotease ADAMTS13. Circles show the location of mutations known to cause VWD type 2A (orange), 2B (blue), 2M (yellow), and 2N (white). 

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2009 : September 2009 - Fast Moving Fronts : J. Evan Sadler - Figures & Descriptions