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A polymorphism in complement factor H has recently been associated with age-related macular degeneration (AMD), the leading cause of blindness in the elderly. A histidine rather than a tyrosine at residue position 384 in the mature protein increases the risk of AMD. Here, using a recombinant construct, we show that amino acid 384 is adjacent to a heparin-binding site in CCP7 of factor H and demonstrate that the allotypic variants differentially recognize heparin. This functional alteration may affect binding of factor H to polyanionic patterns on host surfaces, potentially influencing complement activation, immune complex clearance, and inflammation in the macula of AMD patients.

Original publication

DOI

10.1074/jbc.M605083200

Type

Journal article

Journal

J Biol Chem

Publication Date

25/08/2006

Volume

281

Pages

24713 - 24720

Keywords

Alleles, Amino Acid Substitution, Binding Sites, Complement Activation, Complement Factor H, Heparin, Histidine, Humans, Macular Degeneration, Models, Molecular, Protein Binding, Recombinant Proteins, Structure-Activity Relationship