non-synonymous polymorphisms in the fcn1 gene determine ligand-binding ability and serum levels of m-ficolin非同义fcn1基因的多态性和血清水平的m-ficolin确定配体结合能力.pdfVIP

Non-Synonymous Polymorphisms in the FCN1 Gene Determine Ligand-Binding Ability and Serum Levels of M-Ficolin 1 2 3 1 Christian Gytz Ammitzbøll *, Troels Rønn Kjær , Rudi Steffensen , Kristian Stengaard-Pedersen , Hans 4 2 5,6 2 Jørgen Nielsen , Steffen Thiel , Martin Bøgsted , Jens Christian Jensenius 1 Department of Rheumatology, Aarhus University Hospital, Aarhus, Denmark, 2 Department of Biomedicine, Aarhus University, Aarhus, Denmark, 3 Department of Clinical Immunology, Aalborg Hospital, Aarhus University Hospital, Aarhus, Denmark, 4 Department of Surgical Gastroenterology, Hvidovre University Hospital, Copenhagen, Denmark, 5 Department of Haematology, Aalborg Hospital, Aarhus University Hospital, Aarhus, Denmark, 6 Department of Mathematical Sciences, Aalborg University, Aalborg, Denmark Abstract Background: 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. Principal Findings: We genotyped 26 polymorphisms in the FCN1 gene and found 8 o