Structural and functional characterization of factor H mutations associated with atypical hemolytic uremic syndrome.

@article{SnchezCorral2002StructuralAF,
  title={Structural and functional characterization of factor H mutations associated with atypical hemolytic uremic syndrome.},
  author={Pilar S{\'a}nchez-Corral and David P{\'e}rez-Caballero and Olatz Huarte and Ari M Simckes and Elena Goicoechea and Margarita L{\'o}pez-Trascasa and Santiago Rodr{\'i}guez de C{\'o}rdoba},
  journal={American journal of human genetics},
  year={2002},
  volume={71 6},
  pages={1285-95}
}
Genetic studies have demonstrated the involvement of the complement regulator factor H in nondiarrheal, nonverocytotoxin (i.e., atypical) cases of hemolytic uremic syndrome. Different factor H mutations have been identified in 10%-30% of patients with atypical hemolytic uremic syndrome (aHUS), and most of these mutations alter single amino acids in the C-terminal region of factor H. Although these mutations are considered to be responsible for the disease, the precise role that factor H plays… CONTINUE READING