Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome.

@article{Manuelian2003MutationsIF,
  title={Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome.},
  author={Tamara Manuelian and Jens Hellwage and Seppo Meri and Jessica Caprioli and Marina Noris and Stefan Heinen and Mih{\'a}ly J{\'o}zsi and Hartmut P. H. Neumann and Giuseppe Remuzzi and Peter F Zipfel},
  journal={The Journal of clinical investigation},
  year={2003},
  volume={111 8},
  pages={1181-90}
}
Hemolytic uremic syndrome (HUS) is a disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, and acute renal failure. Recent studies have identified a factor H-associated form of HUS, caused by gene mutations that cluster in the C-terminal region of the complement regulator factor H. Here we report how three mutations (E1172Stop, R1210C, and R1215G; each of the latter two identified in three independent cases from different, unrelated families) affect protein function. All… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 162 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 39 references

The molecular basis of familial hemolytic uremic syndrome: mutation analysis of factor H gene reveals a hot spot in short consensus repeat 20

  • J Caprioli
  • J. Am. Soc. Nephrol
  • 2001
Highly Influential
4 Excerpts

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

  • P Sanchez-Corral
  • Am. J. Hum. Genet. 71:1285–1295
  • 2002
1 Excerpt

Similar Papers

Loading similar papers…