期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 281, 期 34, 页码 24713-24720出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M605083200
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资金
- MRC [MC_U138274352] Funding Source: UKRI
- Medical Research Council [MC_U138274352] Funding Source: researchfish
- Medical Research Council [MC_U138274352] Funding Source: Medline
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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