Title |
Non-Synonymous Polymorphisms in the FCN1 Gene Determine Ligand-Binding Ability and Serum Levels of M-Ficolin
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Published in |
PLOS ONE, November 2012
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DOI | 10.1371/journal.pone.0050585 |
Pubmed ID | |
Authors |
Christian Gytz Ammitzbøll, Troels Rønn Kjær, Rudi Steffensen, Kristian Stengaard-Pedersen, Hans Jørgen Nielsen, Steffen Thiel, Martin Bøgsted, Jens Christian Jensenius |
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. |
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