Tissue-specific host recognition by complement factor H is mediated by differential activities of its glycosaminoglycan-binding regions.

@article{Clark2013TissuespecificHR,
  title={Tissue-specific host recognition by complement factor H is mediated by differential activities of its glycosaminoglycan-binding regions.},
  author={S. James Clark and Liam A Ridge and Andrew Herbert and Svetlana Hakobyan and Barbara Mulloy and Rachel Lennon and Reinhard Wuerzner and B. Paul Morgan and Du{\vs}an Uhr{\'i}n and Paul N. Bishop and Anthony J Day},
  journal={Journal of immunology},
  year={2013},
  volume={190 5},
  pages={
          2049-57
        }
}
Complement factor H (CFH) regulates complement activation in host tissues through its recognition of polyanions, which mediate CFH binding to host cell surfaces and extracellular matrix, promoting the deactivation of deposited C3b. These polyanions include heparan sulfate (HS), a glycosaminoglycan with a highly diverse range of structures, for which two regions of CFH (CCP6-8 and CCP19-20) have been implicated in HS binding. Mutations/polymorphisms within these glycosaminoglycan-binding sites… CONTINUE READING
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