الفهرس 
Introduction
Aim of the workOnly 14 pages are availabe for public view
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Abstract
Table 20, summarized the homozygous expression results. Variants were listed by their domain location. Variants with abnormal secretion, collagen binding, platelet binding or multimer structurewere shaded in pink, while variants with normal secretion and function were shaded blue. Several variants showed defects in secretion or function.
Table 20: Summary of results of homozygous in-vitro expression of type 1 VWD novelSVs.
Table 21, summarized the heterozygous expression results. Variants with abnormal secretion, collagen binding, platelet binding or multimer structure were shaded in pink, while variants with normal secretion and function were shaded blue. Heterozygous expression of variants with wild-type VWF as seen in the patient, corrected many of the defects. Several SVs still have reduced VWF secretion that is consistent with the type 1 VWD phenotype observed in the patients.
Table 21: Summary of results of heterozygous in-vitro expression of type 1 VWD novelSVs.
In conclusion, 10 of the 19 SV (52.6%) theoretically are not causative of the VWD phenotype observed in the patients.These subjects had normal VWF pp/VWF:Ag suggesting reduced plasma survival is unlikely to be the causative mechanism. The VWD mechanism in these subjects remains undefined.
2 of 19 variants (10.6 %); R960P, C2693F demonstrated qualitative VWF defect; with either low VWF:CB/VWF:Ag or both low VWF:CB/VWF:Ag and loss of highest molecular weight multimers.
We identified 7 of 19 (36.8) % VWF SVs as likely to cause the type 1 VWD phenotype with reduced secretion (Fig. 29).
Fig. 29: Summary of the pathogenicity of the novels SVs.