Type 1 von Willebrand disease mutation Cys1149Arg causes intracellular retention and degradation of heterodimers: a possible general mechanism for dominant mutations of oligomeric proteins.

@article{Bod2001Type1V,
  title={Type 1 von Willebrand disease mutation Cys1149Arg causes intracellular retention and degradation of heterodimers: a possible general mechanism for dominant mutations of oligomeric proteins.},
  author={I Bod{\'o} and Akira Fujimoto Hideo Katsumi and Elodee A. Tuley and Jeroen C J Eikenboom and Zhi-wei Dong and J Evan Sadler},
  journal={Blood},
  year={2001},
  volume={98 10},
  pages={
          2973-9
        }
}
Some families affected by von Willebrand disease type 1 show high penetrance with exceptionally low von Willebrand factor (VWF) levels. Previously, a mutation associated with this dominant phenotype, Cys1149Arg, was found to decrease the secretion of coexpressed normal VWF, and the mutation was proposed to cause intracellular retention of pro-VWF heterodimers. To demonstrate heterodimer formation, a model was developed in which subunits could be distinguished immunologically and by size… CONTINUE READING
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