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. 2006 Aug 25;281(34):24713-20.
doi: 10.1074/jbc.M605083200. Epub 2006 Jun 20.

His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form

Simon J Clark  1 , Victoria A Higman, Barbara Mulloy, Stephen J Perkins, Susan M Lea, Robert B Sim, Anthony J Day
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Free article

His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form

Simon J Clark et al. J Biol Chem. .
Free article

Abstract

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.

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