Non-synonymous polymorphisms in the FCN1 gene determine ligand-binding ability and serum levels of M-ficolin

Christian Gytz Ammitzbøll, Troels Rønn Kjær, Rudi Nora Steffensen, Kristian Stengaard-Pedersen, Hans Jørgen Nielsen, Steffen Thiel, Martin Bøgsted, Jens Christian Jensenius

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26 Citations (Scopus)

Abstract

The innate immune system encompasses various recognition molecules able to sense both exogenous and endogenous danger signals arising from pathogens or damaged host cells. One such pattern-recognition molecule is M-ficolin, which is capable of activating the complement system through the lectin pathway. The lectin pathway is multifaceted with activities spanning from complement activation to coagulation, autoimmunity, ischemia-reperfusion injury and embryogenesis. Our aim was to explore associations between SNPs in FCN1, encoding M-ficolin and corresponding protein concentrations, and the impact of non-synonymous SNPs on protein function.
Original languageEnglish
JournalP L o S One
Volume7
Issue number11
Pages (from-to)e50585
Number of pages10
ISSN1932-6203
DOIs
Publication statusPublished - 2012

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