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Human factor H-related protein 2 (CFHR2) regulates complement activation

Mutations and deletions within the human CFHR gene cluster on chromosome 1 are associated with diseases, such as dense deposit disease, CFHR nephropathy or age-related macular degeneration. Resulting mutant CFHR proteins can affect complement regulation. Here we identify human CFHR2 as a novel alter...

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Bibliographic Details
Main Authors: Eberhardt, Hannes Uwe (Author) , Buhlmann, Denise (Author) , Hortschansky, Peter (Author) , Chen, Qian (Author) , Böhm, Sascha (Author) , Kemper, Markus J. (Author) , Wallich, Reinhard (Author) , Hartmann, Andrea (Author) , Hallström, Teresia (Author) , Zipfel, Peter F. (Author) , Skerka, Christine (Author)
Format: Article (Journal)
Language:English
Published: November 18, 2013
In: PLOS ONE
Year: 2013, Volume: 8, Issue: 11
ISSN:1932-6203
DOI:10.1371/journal.pone.0078617
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1371/journal.pone.0078617
Verlag, lizenzpflichtig, Volltext: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0078617
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Author Notes:Hannes U. Eberhardt, Denise Buhlmann, Peter Hortschansky, Qian Chen, Sascha Böhm, Markus J. Kemper, Reinhard Wallich, Andrea Hartmann, Teresia Hallström, Peter F. Zipfel, Christine Skerka
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Summary:Mutations and deletions within the human CFHR gene cluster on chromosome 1 are associated with diseases, such as dense deposit disease, CFHR nephropathy or age-related macular degeneration. Resulting mutant CFHR proteins can affect complement regulation. Here we identify human CFHR2 as a novel alternative pathway complement regulator that inhibits the C3 alternative pathway convertase and terminal pathway assembly. CFHR2 is composed of four short consensus repeat domains (SCRs). Two CFHR2 molecules form a dimer through their N-terminal SCRs, and each of the two C-terminal ends can bind C3b. C3b bound CFHR2 still allows C3 convertase formation but the CFHR2 bound convertases do not cleave the substrate C3. Interestingly CFHR2 hardly competes off factor H from C3b. Thus CFHR2 likely acts in concert with factor H, as CFHR2 inhibits convertases while simultaneously allowing factor H assisted degradation by factor I.
Item Description:Gesehen am 07.01.2021
Physical Description:Online Resource
ISSN:1932-6203
DOI:10.1371/journal.pone.0078617

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