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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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Hauptverfasser: Eberhardt, Hannes Uwe (VerfasserIn) , Buhlmann, Denise (VerfasserIn) , Hortschansky, Peter (VerfasserIn) , Chen, Qian (VerfasserIn) , Böhm, Sascha (VerfasserIn) , Kemper, Markus J. (VerfasserIn) , Wallich, Reinhard (VerfasserIn) , Hartmann, Andrea (VerfasserIn) , Hallström, Teresia (VerfasserIn) , Zipfel, Peter F. (VerfasserIn) , Skerka, Christine (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: November 18, 2013
In: PLOS ONE
Year: 2013, Jahrgang: 8, Heft: 11
ISSN:1932-6203
DOI:10.1371/journal.pone.0078617
Online-Zugang: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
Volltext
Verfasserangaben: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
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 07.01.2021
Beschreibung:Online Resource
ISSN:1932-6203
DOI:10.1371/journal.pone.0078617

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